Complex id;Complex name;Synonyms;organism;subunits (UniProt IDs);subunits (Entrez IDs);protein complex purification method;PubMed id;FunCat categories;"functional comment";"disease comment";"subunit comment";
1;BCL6-HDAC4 complex;;Human;P41182,P56524;604,9759;MI:0007- anti tag coimmunoprecipitation;11929873;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,43.03.07.02.01.01,70.10;"Transcriptional repression by BCL6 is thought to be achieved in part by recruiting a repressor complex containing histone deacetylases.";"";""
2;BCL6-HDAC5 complex;;Human;P41182,Q9UQL6;604,10014;MI:0007- anti tag coimmunoprecipitation;11929873;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,43.03.07.02.01.01,70.10;"Transcriptional repression by BCL6 is thought to be achieved in part by recruiting a repressor complex containing histone deacetylases.";"";""
3;BCL6-HDAC7 complex;;Human;P41182,Q8WUI4;604,51564;MI:0007- anti tag coimmunoprecipitation;11929873;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,43.03.07.02.01.01,70.10;"Transcriptional repression by BCL6 is thought to be achieved in part by recruiting a repressor complex containing histone deacetylases.";"";""
4;Multisubunit ACTR coactivator complex;;Human;Q92793,Q09472,Q9Y6Q9,Q92831;1387,2033,8202,8850;MI:0004- affinity chromatography technologies | MI:0018- two hybrid;9267036;11.02.03.04.01,30.01.11,70.10;"Cofactor ACTR binds directly nuclear receptors and stimulates their transcriptional activities in a hormone-dependent fashion.";"";""
9;6S-nuclear aryl hydrocarbon (Ah) receptor ligand-activated complex;;Mouse;P30561,P53762;11622,11863;MI:0019- coimmunoprecipitation;1317062;11.02.03.04,16.03.01,30.01.11,34.11.03,70.10;"Arnt contains a basic helix-loop-helix motif, which may be responsible for interacting with both the XRE (xenobiotic responsive element) and the ligand-binding subunit.";"";""
10;13S condensin complex;;Human;Q15021,Q9BPX3,Q15003,O95347,Q9NTJ3;9918,64151,23397,10592,10051;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;11136719;10.03.01.01.11,10.03.04.03,10.03.04.05,42.10.03,70.10.03;"";"";""
11;BLOC-3 (biogenesis of lysosome-related organelles complex 3);;Human;Q92902,Q9NQG7;3257,89781;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;12847290;42.22,42.25;"The results suggest that HPS1 and HPS4 are components of a protein complex that regulates the intracellular localization of lysosomes and late endosomes and may function in a BLOC-1-dependent pathway for melanosome biogenesis.";"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome (PMID:15030569).";""
12;BLOC-2 (biogenesis of lysosome-related organelles complex 2);;Human;Q969F9,Q9UPZ3,Q86YV9;84343,11234,79803;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients | MI:0071- molecular sieving;15030569;42.22,42.25;"The results suggest that BLOC-2 is not critical for basal levels of secretion of lysosomal enzymes by fibroblasts.";"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome.";""
13;MUS81-CDS1 complex;;Human;Q92903,Q96NY9;1040,80198;MI:0004- affinity chromatography technologies;11741546;10.01.05.01,10.01.05.03;"";"";""
14;BLOC-2 (biogenesis of lysosome-related organelles complex 2);;Mouse;Q91VB4,P59438,Q8BLY7;12807,246694,20170;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients | MI:0071- molecular sieving;14718540;42.22,42.25;"The results indicate that the Hps3, Hps5, and Hps6 proteins regulate vesicle trafficking to lysosome-related organelles at the physiological level as components of the BLOC-2 complex.";"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome (PMID:15030569).";""
15;NCOR complex;;Human;Q92828,Q13227,O15379,O75376,O60907,Q9BZK7;7464,2874,8841,9611,6907,79718;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;12628926;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"By using specific small interference RNAs (siRNAs), the authors demonstrate that HDAC3 is essential, whereas TBL1 and TBLR1 are functionally redundant but essential for repression by unliganded thyroid hormone receptor.";"";""
23;BLOC-1 (biogenesis of lysosome-related organelles complex 1);;Human;P78537,Q6QNY1,Q6QNY0,Q9NUP1,Q96EV8,Q8TDH9,Q9UL45,O95295;2647,282991,388552,55330,84062,63915,26258,23557;MI:0019- coimmunoprecipitation;15102850;42.22,42.25;"The authors identified Snapin, BLOS1, BLOS2, and BLOS3 as subunits of BLOC-1 and found that the HPS mouse model strain, reduced pigmentation, carries a nonsense mutation in BLOS3. The genes encoding these proteins may underlie the pathogenesis of novel forms of HPS in patients having no detectable mutation in any of the genes that cause HPS types 1-7. ";"PLDN, MUTED, CNO and DTNBP1 are involved in Hermansky-Pudlak syndrome (HPS), a genetic disorder characterized by hypopigmentation and platelet storage pool deficiency.";""
24;BLOC-1 (biogenesis of lysosome-related organelles complex 1);;Mouse;O55102,Q9CWG9,Q5U5M8,Q8VED2,Q91WZ8,Q8R015,Q9R0C0,Q9Z266;14533,73689,232946,117197,94245,17828,18457,20615;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;15102850;42.22,42.25;"The authors identified Snapin, BLOS1, BLOS2, and BLOS3 as subunits of BLOC-1 and found that the HPS mouse model strain, reduced pigmentation, carries a nonsense mutation in BLOS3. The genes encoding these proteins may underlie the pathogenesis of novel forms of HPS in patients having no detectable mutation in any of the genes that cause HPS types 1-7.";"PLDN, MUTED, CNO and DTNBP1 are involved in Hermansky-Pudlak syndrome (HPS), a genetic disorder characterized by hypopigmentation and platelet storage pool deficiency.";""
25;9S-cytosolic aryl hydrocarbon (Ah) receptor non-ligand activated complex;;Mouse;P30561,O08915,P07901,P11499;11622,11632,15519,15516;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;1310021;32.01,34.11.03,70.03;"The authors propose that the AhR exists in cytosol as a tetrameric species, while in the nucleus the AhR exists as a heterodimer.";"";""
26;Bestrophin-protein phosphatase 2A complex;;Pig;Q8WMR7,(P67776,P11493),(P54612,P54613);397169,(397656,397136),(397088,397470);MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;12058047;20.01.01.07.09,20.03.01.01,30.05.02.30,34.11.01,36.25.01.01,77.03.02.02;"The interaction of bestrophin and PP2A suggests that phosphorylation or dephosphorylation of bestrophin may act as the on/off switch for the light peak or modulate its amplitude or timing.";"";""
27;Arp2/3 protein complex;;Human;P61160,P61158,O15143,O15144,O15145,P59998,O15511;10097,10096,10095,10109,10094,10093,10092;MI:0027- cosedimentation | MI:0071- molecular sieving;9359840;16.01,42.04.03,70.03;"";"";""
28;Modulator;PA700-dependent proteasome activator;Bovine;Q3SZ81,Q2KIW6,Q3SZ19;508448,518637,513315;MI:0071- molecular sieving | MI:0226- ion exchange chromatography;8621709;14.13.01.01,16.19.03,18.01.07,18.02.01.01.03,70.03,70.10;"The modulator has no direct effect on the activity of the proteasome, but enhances PA700 activation of the proteasome by up to 8-fold. This activation is associated with the formation of a proteasome/PA700-containing complex that is significantly larger than that formed in its absence. Two of its proteins, p50 and p42, were also identified as components of PA700.";"";""
29;PA28gamma complex;;Human;P61289;10197;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;9325261;14.13.01.01,16.01,18.01.07,18.02.01.01.03,70.03,70.10;"";"";"According to gel filtration chromatography experiments, the protein complex probably consists of seven identical subunits."
30;PA28 complex; 11S REG;Human;Q06323,Q9UL46;5720,5721;MI:0071- molecular sieving | MI:0226- ion exchange chromatography;9325261;14.13.01.01,18.01.07,18.02.01.01.03,70.03;"PA28 is a regulatory complex of the 20S proteasome. It acts as proteasome activator and stimulates cleavage after basic, acidic, and most hydrophobic residues in many peptides.";"";""
31;PA28 complex; 11S REG;Bovine;Q2KJE7,Q5E9G3;510041,509857;MI:0226- ion exchange chromatography;7989312;14.13.01.01,18.01.07,18.02.01.01.03,70.03;"PA28 is a regulatory complex of the 20S proteasome. It acts as proteasome activator and stimulates cleavage after basic, acidic, and most hydrophobic residues in many peptides.";"";""
32;PA700 complex; 19S complex;Human;P62191,P35998,P17980,P43686,P62195,P62333,Q99460,O75832,O00231,O00232,Q9UNM6,O00487,Q13200,O43242,P55036,Q16401,Q15008,P51665,P48556,O00233;5700,5701,5702,5704,5705,5706,5707,5716,5717,5718,5719,10213,5708,5709,5710,5711,9861,5713,5714,5715;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;9148964;14.13.01.01,16.01,18.01.07,18.02.01.01.03,70.03;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
33;Prefoldin;;Human;O60925,Q9UHV9,Q9NQP4,Q99471,O15212,P61758;5201,5202,5203,5204,10471,7411;MI:0071- molecular sieving;14634002;14.01,16.01,42.04.03,42.04.05,70.03;"";"";""
34;Aqp4-Dag1-Dmd-Snta1 complex;;Rat;P47863,Q91XP6,Q498T0,(Q7TPH2,Q7TPH3,Q7TPH4);25293,114489,362242,(24907,24907,24907);MI:0019- coimmunoprecipitation;11717465;20.03.01,70.02,77.03.01.01.01;"The authors show that expression and subcellular localization of AQP4 depend on association with the dystrophin complex through a tSSV-PDZ-mediated interaction with alpha -syntrophin.";"";""
36;AP1 adaptor complex;;Human;Q10567,O43747,O75843,Q9BXS5,Q9Y6Q5,P61966,P56377,Q96PC3;162,164,8906,8907,10053,1174,8905,130340;MI:0018- two hybrid;9733768;14.04,20.09.07,20.09.07.25,20.09.18.09.01,42.09;"This adaptor-related complex participates in a transport step different from that of AP-1. It may function at some trafficking step in the complex pathways between the TGN and the cell surface.";"";""
37;CDH23-harmonin transmembrane complex;;Mouse;Q99PF4,Q9ES64;22295,72088;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;12407180;36.25.01.03,43.03.23,73.03.23,77.03.02.01;"";"";""
38;20S proteasome; proteasome;Mouse;Q9R1P4,P49722,O70435,Q9R1P0,Q9Z2U1,Q9QUM9,Q9Z2U0,O09061,Q9R1P3,Q9R1P1,P99026,O55234,Q60692,P70195;26440,19166,19167,26441,26442,26443,26444,19170,26445,26446,19172,19173,19175,19177;MI:0019- coimmunoprecipitation;10436176;14.07.11,14.13.01.01,32.01,70.03,70.10;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
39;immunoproteasome;20S proteasome | proteasome;Mouse;Q9R1P4,P49722,O70435,Q9R1P0,Q9Z2U1,Q9QUM9,Q9Z2U0,O09061,O35955,Q9R1P3,Q9R1P1,P99026,P28063,P28076;26440,19166,19167,26441,26442,26443,26444,19170,19171,26445,26446,19172,16913,16912;MI:0019- coimmunoprecipitation;10436176;14.07.11,14.13.01.01,32.01,36.25.16.03.05,70.03,70.10;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
40;COP9 signalosome complex (Gps1, Cops1, Cops2, Cops3, Cops4, Cops5, Cops6, Cops7a, Cops7b, Cops8) ; signalosome | COP9 complex | CSN complex;Mouse;P61202,O88543,O88544,O35864,O88545,Q9CZ04,Q8BV13,Q8VBV7,Q99LD4;12848,26572,26891,26754,26893,26894,26895,108679,209318;MI:0019- coimmunoprecipitation;9707402;14.13.01,16.01,70.03,70.10;"";"";""
41;Mi-2/NuRD-MTA2 complex;;Human;P41182,Q13547,O95983,O94776,Q9BTC8;604,3065,53615,9219,57504;MI:0019- coimmunoprecipitation;15454082;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,43.03.07.02.01.01,70.10,77.03.05.03;"";"";""
42;CASK-MINT-VELI tripartite complex;;Rat;O35430,Q62915,(Q9Z250,Q9Z252,Q792I0);83589,29647,(85327,60377,60442);MI:0019- coimmunoprecipitation | MI:0096- pull down;9753324;14.10,20.09.16.09.05,34.03.01,34.07,70.06,77.03.01.01.01;"This complex acts as a nucleation site for the assembly of proteins involved in synaptic vesicle exocytosis and synaptic junctions.";"";""
43;Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN variant);;Human;Q96BI3,Q92542,P49768,Q9NZ42;51107,23385,5663,55851;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;12740439;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.";"Gamma-secretase is causally implicated in Alzheimer's disease.";""
44;CASK-MINT complex;;Mouse;Q8BMF2,O70589;319924,12361;MI:0019- coimmunoprecipitation | MI:0096- pull down;9753324;14.10,20.09.16.09.05,77.03.01.01.01;"The interaction between CASK and Mint1 was resistant to salt concentrations of up to 3 M NaCl, indicating that binding is not purely electrostatic (PMID:9753324).";"";""
45;Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN variant);;Human;Q96BI3,Q92542,P49768,Q9NZ42;51107,23385,5663,55851;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;15274632;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.";"Gamma-secretase is causally implicated in Alzheimer's disease.";""
46;AP2 adaptor complex;;Mammalia;P17427,P63010,P84092,P62743;11772,163,116563,232910;MI:0004- affinity chromatography technologies | MI:0114- x-ray crystallography;12086608;14.04,14.10,20.09.07,20.09.18.09.01,42.09;"";"";""
47;DNA polymerase alpha-primase complex;;Mouse;P33609,P33611,P20664,P33610;18968,18969,19075,19076;MI:0027- cosedimentation;8463324;10.01.03,70.10;"In growing mouse FM3A cells, the transcripts of the four subunits are present throughout the cell cycle and increase slightly prior to the S phase.";"";""
48;RGS7-Gbeta5-Galphaq complex;;Mammalia;P21279,P62881,O46470;14682,14697,281452;MI:0055- fluorescent resonance energy transfer;12670932;30.01.05.05;"";"";"For the FRET experiments the authors used murine Gbeta5, bovine RGS7, and murine Galphaq."
49;DNMT3B complex;;Human;Q9UBC3,Q13547,O95239,Q96ST3,O60264,O95347,Q9NTJ3;1789,3065,24137,25942,8467,10592,10051;MI:0019- coimmunoprecipitation;15148359;10.01.09.01,10.01.09.05,10.03.01.01.11,10.03.04.05,42.10.03,70.10.03;"";"";""
50;Rab5 GDP/GTP exchange factor complex;;Mouse;O35551,Q9JM13;54189,56715;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;9323142;20.09.18.09.01;"This complex is essential for endocytic membrane fusion.";"";""
51;CCT micro-complex;;Mouse;P11983,P80314,P80318,P80315,P80316,P80317,P80313,P42932;21454,12461,12462,12464,12465,12466,12468,12469;MI:0029- cosedimentation through density gradients;9250675;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. CCT micro-complexes have mol. wts ranging from 120 to 250 kDa and are present in cells at lower abundance (<5%) as compared with intact CCT. Sequence analysis of the TriC subunits was shown in PMID:2377466, PMID:7953530 and PMID:7890169.";"";""
52;CCT complex (chaperonin containing TCP1 complex); TRiC;Mouse;P11983,P80314,P80318,P80315,P80316,P80317,P80313,P42932;21454,12461,12462,12464,12465,12466,12468,12469;MI:0029- cosedimentation through density gradients | MI:0091- chromatography technologies;9013858;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated. Sequence analysis of the TriC subunits was shown in PMID:9013858, PMID:2377466, PMID:7953530 and PMID:7890169.";"";""
53;Gbeta5-rgs7 complex;;Rat;P62882,P49803;83579,54296;MI:0006- anti bait coimmunoprecipitation;10723068;30.01.05.05,77.03.01.01.01;"The authors demonstrated the presence of the heterodimeric RGS7/Gb5 complex throughout many areas of the adult rat brain, with a role as yet undefined on the dynamics of typical Gbg-mediated neuronal pathway activation/desensitization mechanisms.";"";""
54;SIN3 complex; Histone deacetylase complex;Human;Q13547,Q92769,Q09028,Q16576,O00422,O75446,Q96ST3;3065,3066,5928,5931,10284,8819,25942;MI:0004- affinity chromatography technologies;9150135;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03,70.10;"";"";""
55;HDAC4-ERK1 complex;;Human;P56524,P27361;9759,5595;MI:0007- anti tag coimmunoprecipitation;11114188;10.01.09.05,11.02.03.04,30.01.05.01.03,42.10.03,70.10;"ERK1 activity links the Ras-MAPK signal transduction pathway to a mechanism for chromatin remodeling (i.e., histone deacetylation).";"";""
56;Elongin (SIII) complex;;Rat;P83941,P62870,Q63187;64525,81807,25562;MI:0227- reverse phase chromatography;8244996;11.02.03.01.04,11.02.03.04.01,18.01.07,18.02.01.01,70.10;"The elongin (SIII) complex strongly stimulates the rate of elongation by RNA polymerase II by suppressing transient pausing by polymerase at many sites along the DNA. In mammals, elongin is a trimeric complex. Elongin A is the catalytic subunit. Elongins B and C form a binary complex that is capable of enhancing the transcriptional activity of elongin A.";"";""
57;HDAC4-ERK2 complex;;Human;P56524,P28482;9759,5594;MI:0007- anti tag coimmunoprecipitation;11114188;10.01.09.05,11.02.03.04,30.01.05.01.03,42.10.03,70.10;"";"";""
58;SMRT complex;;Human;Q13227,O15379,Q9Y618,O60907,Q9BZK7;2874,8841,9612,6907,79718;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;12628926;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"IR10, a subunit of the N-CoR complex, does not associate with SMRT (NCOR2).";"";""
59;AP3 adapter complex;;Human;O00203,Q13367,O14617,Q9Y2T2,P53677,Q92572,P59780;8546,8120,8943,26985,10947,1176,10239;MI:0019- coimmunoprecipitation;9151686;14.04,20.09.07.06,20.09.18.09.01,70.25;"";"";""
60;Interferon-stimulated gene factor 3 transcription complex ISGF3;;Human;Q00978,P42224,P52630;10379,6772,6773;MI:0004- affinity chromatography technologies;8943351;11.02.03.04,70.10;"The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA.";"";""
61;Mi2/NuRD complex; Mi2-beta-histone deacetylase complex;Human;Q14839,Q13547,Q92769,O95983,O94776,Q09028,Q16576;1108,3065,3066,53615,9219,5928,5931;MI:0004- affinity chromatography technologies;9790534;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,70.10;"";"Dermatomyositis, cancer (PMID:9790534)";""
62;MeCP1 complex; Mi2/NuRD-MBD2 complex;Human;Q14839,Q13547,Q92769,Q9UBB5,O95983,O94776,Q09028,Q16576;1108,3065,3066,8932,53615,9219,5928,5931;MI:0096- pull down;10444591;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,16.03.01,42.10.03,70.10;"MeCP1 protein complex represses transcription through preferential binding, remodeling, and deacetylation of methylated nucleosomes. ";"CHD4 is involved in dermatomyositis (PMID:9790534).";""
63;Mitotic 14S cohesin 1 complex;;Human;O60216,Q14683,Q9UQE7,Q8WVM7;5885,8243,9126,10274;MI:0019- coimmunoprecipitation;11076961;10.03.01.01.11,10.03.04.05,42.10.03,70.10.03;"The results suggest that vertebrate cohesins are regulated by a novel prophase pathway which is distinct from the APC pathway that controls cohesins in yeast.";"";""
64;Mitotic 14S cohesin 2 complex;;Human;O60216,Q14683,Q9UQE7,Q8N3U4;5885,8243,9126,10735;MI:0019- coimmunoprecipitation;11076961;10.03.01.01.11,42.10.03,70.10;"";"";""
65;Multiprotein trafficking complex; SAP97-CASK-VELI-MINT1 complex;Rat;O35430,Q62915,Q62696,P52188,Q792I0;83589,29647,25252,117052,60442;MI:0019- coimmunoprecipitation | MI:0096- pull down;14960569;20.01.01.01,20.03.01,34.03,77.03.01.01.01;"This macromolecular complex participates in trafficking and plasma membrane localization of Kir2 channels (PMID:14960569).";"";""
66;TRAP complex; thyroid hormone receptor-associated protein complex;Human;Q15648,Q93074,O60244,Q9Y2X0,Q9NVC6,O75448,P10827,Q9Y2W1;5469,9968,9282,10025,9440,9862,7067,9967;MI:0004- affinity chromatography technologies | MI:0047- far western blotting;8710870;11.02.03.04.01,18.02.07,30.01.09.08,30.01.11,70.10;"The human thyroid hormone receptor-associated protein (TRAP) complex is a coactivator for nuclear receptors. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
67;AP4 adaptor complex;;Human;Q9Y6B7,Q9UPM8,O00189,Q9Y587;10717,23431,9179,11154;MI:0019- coimmunoprecipitation | MI:0019- coimmunoprecipitation;10436028;14.04,16.01,20.09.07.06,20.09.18.09.01,42.09,70.08,70.09;"Adaptor protein complexes (APs) function as vesicle coat components in different membrane traffic pathways.";"";""
68;BCDX2 complex; RAD51B-RAD51C-RAD51D-XRCC2 complex;Human;O43502,O15315,O75771,O43543;5889,5890,5892,7516;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation | MI:0027- cosedimentation;15141025;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
69;ApoB RNA editing enzyme complex;;Rat;Q923K9,P38483,Q99PF5;170912,25383,171137;MI:0004- affinity chromatography technologies;10781591;11.06.03.01,16.03.03,77.03.11.07;"In rat liver, ASP is apparently associated with KSRP, which may confer stability to the editing enzyme-complex with its substrate apoB RNA serving as an additional auxiliary component.";"";""
70;CLIC4 complex;;Rat;P60711,P07335,Q9Z0W7,P39052,P68370,P62260,P63102;81822,24264,83718,25751,64158,29753,25578;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes | MI:0096- pull down;11563969;20.01.01.07,20.03.01.01,34.01,42.27.03;"";"";""
71;MRN complex (MRE11-RAD50-NBS1 complex);;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0006- anti bait coimmunoprecipitation;10612394;01.03.16.03,10.01.05.01,10.03.01.03,32.01.09,70.10;"The implication of hMre11/hRad50/p95 protein complex in NBS reveals a direct molecular link between DSB repair and cell cycle checkpoint functions.";"Rad50-MRE11-p95 protein complex is involved in Nijmegen breakage syndrome.";""
72;R/M complex (RAD50-MRE11 complex);;Human;P49959,Q92878;4361,10111;MI:0071- molecular sieving;9651580;01.03.16.03,10.01.05.01,16.03.01,32.01.09,42.10.03,70.10;"Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre11 is in a complex with Rad50.";"";""
73;MRN complex (MRE11-RAD50-NBN complex);;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0071- molecular sieving | MI:0413- electrophoretic mobility shift assay;10346816;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"On nonhairpin DNA ends, ATP controls a switch in endonuclease specificity that allows Mre11/Rad50/Nbs1 to cleave a 3'-protruding strand at a double-/single-strand transition.";"";""
74;TRPC1-Homer3-IP3R complex;;Mammalia;Q9Z2X5,Q14643,P48995;29548,3708,7220;MI:0019- coimmunoprecipitation;14505576;20.01.01.01,20.03.01.01,30.05.02.30;"The authors demonstrate that the adaptor protein, termed Homer, facilitates a physical association between TRPC1 and the IP(3)R that is required for the TRP channel to respond to signals.";"";""
75;TSC1-TSC2 complex;;Human;Q92574,P49815;7248,7249;MI:0007- anti tag coimmunoprecipitation;14651849;12.07,14.07.03;"TSC1 and TSC2 form a functional complex and inhibit the phosphorylation of S6K and 4EBP1, two key regulators of translation.";"";""
76;Cytoplasmic dynein complex;;Rat;P63036,P38650,Q63100,Q62871,Q9QXU8,Q9JJ79,P63170,P62628,Q9Z336;65028,29489,29564,116659,252902,65209,58945,170714,83462;MI:0004- affinity chromatography technologies | MI:0027- cosedimentation | MI:0019- coimmunoprecipitation;9790665;02.45.11,16.01,20.09.14,20.09.18.09.01;"Cytoplasmic dynein  is involved in functions as diverse as spindle-pole organization and nuclear migration during mitosis, the positioning and functioning of the endoplasmic reticulum, the Golgi apparatus, and the nucleus, and also the minus-end-directed transport of vesicles, including endosomes and lysosomes, along microtubules and retrograde axonal transport in neurons (PMID:16440056).";"";""
77;nNos-Capon-Dexras1 complex;;Mouse;Q9Z0J4,Q9D3A8,O35626;18125,70729,19416;MI:0004- affinity chromatography technologies;11086993;30.01.09.01,70.03,77.03.01.01.01;"The authors describe that CAPON enhances nNOS-mediated activation of Dexras1 through the ternary complex whereby CAPON links nNOS to Dexras1.";"";""
78;nNos-Capon-Dexras1 complex;;Rat;P29476,O54960,Q9JKF8;24598,192363,64455;MI:0096- pull down;11086993;30.01.09.01,70.03,77.03.01.01.01;"The authors describe that CAPON enhances nNOS-mediated activation of Dexras1 through the ternary complex whereby CAPON links nNOS to Dexras1.";"";""
79;nNos-Capon-Syn1 complex;;Rat;P29476,O54960,P09951;24598,192363,24949;MI:0096- pull down;11867766;30.01.09.01,77.03.01.01.01;"CAPON has  been found to function as an adapter protein linking nNOS to specific targets such as Dexras1 and synapsins. The results suggest a mechanism for specific actions of NO at presynaptic sites.";"";""
80;Ubiquitin E3 ligase (Skp1A, Skp2, Cul1, Rbx1);Cul1-Rbx1-Skp1-Fbox protein Skp2 SCF ubiquitin ligase complex;Human;Q13616,P62877,P63208,Q13309;8454,9978,6500,6502;MI:0114- x-ray crystallography;11961546;14.07.05,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
81;Ubiquitin E3 ligase (SKP1A, FBXW8, CUL7, RBX1);Cul7-Rbx1-Skp1-F-Fbx29 complex;Human;Q14999,Q8N3Y1,P62877,P63208;9820,26259,9978,6500;MI:0004- affinity chromatography technologies;12481031;14.07.05;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
82;Ubiquitin E3 ligase (Vhl, Tceb1, Tceb2, Cul2, Rbx1);VHL tumor suppressor complex;Rat;Q9D4H8,Q498D8,P83941,P62870,Q64259;71745,300084,64525,81807,24874;MI:0071- molecular sieving | MI:0091- chromatography technologies;10213691;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";"Since Cul2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
83;Tubulin:stathmin complex;;Bovine;Q3T0C7,P81948,Q6B856;616317,777775,281555;MI:0114- x-ray crystallography;11030624;10.03,42.04.05;"";"";""
84;Nucleic acid channel complex; NACh;Rat;O88989,P70581;24551,245922;MI:0091- chromatography technologies;11805283;20.01.17,20.03.01,70.02;"";"";"NACh is a heteromultimeric complex of at least two proteins."
85;Tubulin:stathmin complex;;Bovine;Q3T0C7,P81948,Q6B856;616317,777775,281555;MI:0107- surface plasmon resonance | MI:0071- molecular sieving;9312110;10.03,42.04.05;"The stathmin interacts directly with tubulin, with a maximum affinity of 0.5 µM around pH 6.5. This interaction leads to formation of a 217-kDa complex consisting of the association of one stathmin with two tubulin heterodimer molecules.";"";""
86;NUMAC complex (nucleosomal methylation activator complex); CARM1-associated complex;Human;P60709,O14497,Q86X55,Q96KG9,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3;60,8289,10498,57410,6597,6598,6599,6601,6602,6605;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;14729568;10.01.09.05,11.02.03.04.01,14.07.09,16.03.01,30.01.09.08,30.01.11,42.10.03,70.10;"In the NUMAC complex, the methylase, CARM1, acquires the ability to covalently modify nucleosomal histones.";"";""
87;Nup 107-160 subcomplex;NPC subcomplex;Human;P57740,Q8WUM0,Q12769,Q8NFH4,Q8NFH3,Q9BW27,P52948,P55735,Q96EE3;57122,55746,23279,79023,348995,79902,4928,6396,81929;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;15146057;20.01.10,20.03.01.05,20.09.01,70.10.04;"All trafficking of macromolecules between the cytoplasm and the nucleus occurs through nuclear pore complexes (NPCs), which are supramolecular assemblies at points of fusion between the inner and outer nuclear membranes. NPCs are composed of an eightfold symmetric spoke-ring complex, cytoplasmic fibers, and a nuclear basket.";"";""
88;SNARE complex (Scfd1, Sec22b, Stx5, Bet1, Gosr2, Gosr1);;Rat;Q62896,Q62931,O35165,Q62991,Q4KM74,Q08851;29631,94189,64154,54350,310710,65134;MI:0019- coimmunoprecipitation | MI:0027- cosedimentation;9094723;20.09.07.03,20.09.07.05,20.09.07.25,20.09.07.27,20.09.16.09.05,70.07,70.08;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
89;Sec6/8 exocyst complex;;Human;Q9NV70,Q96KP1,O60645,Q96A65,O00471,Q8TAG9,Q9UPT5,Q8IYI6;55763,55770,11336,60412,10640,54536,23265,149371;MI:0004- affinity chromatography technologies;11493706;20.01.10,20.09.16.09.03;"";"";""
91;FA complex (Fanconi anemia complex), cytoplasmic;;Human;O15360,Q00597,Q9NPI8,O15287;2175,2176,2188,2189;MI:0004- affinity chromatography technologies;15082718;14.07.05,32.01.09,70.03;"";"FA complex is involved in Fanconi anemia (FA) disease.";""
92;CD28-transactivation complex;;Human;P10747,P19338;940,4691;MI:0004- affinity chromatography technologies;12324461;11.02.03.01.01,11.02.03.04,70.10;"";"";""
93;Anaphase-promoting complex; APC | cyclosome;Human;Q9H1A4,Q9UJX6,Q9UJX5,Q9UJX4,Q9UJX3,Q13042,Q9UJX2,P30260;64682,29882,29945,51433,51434,8881,8697,996;MI:0019- coimmunoprecipitation;9469815;10.03.01,14.07.05,16.01,70.10;"The initiation of anaphase and exit from mitosis depend on a multi-subunit ubiquitination complex called the anaphase-promoting complex (APC)1 or cyclosome. The APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26 S proteasome is essential for the initiation of sister chromatid separation at the metaphase-anaphase transition. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B.";"";""
94;ATP-utilizing chromatin assembly and remodeling factor (hACF) complex;;Human;Q9NRL2,O60264;11177,8467;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;10747848;10.01.09.05,11.02.03.04,42.10.03,70.10;"The hACF complex also possesses ATP-dependent nucleosome remodeling and spacing activities.";"";""
95;Ku antigen-NARG1 complex; OCFRE-binding complex;Human;Q9BXJ9,P13010,P12956;80155,7520,2547;MI:0004- affinity chromatography technologies;12145306;11.02.03.04,16.03.01,73.03.17;"This complex regulates osteocalcin gene expression.";"";""
96;Anaphase-promoting complex; APC | cyclosome;Human;Q9H1A4,Q9UM13,Q9UJX6,Q9UJX5,Q9UJX4,Q9UJX3,Q13042,Q9UJX2,P30260;64682,10393,29882,29945,51433,51434,8881,8697,996;MI:0019- coimmunoprecipitation;10318877;10.03.01,14.07.05,16.01,70.10;"The initiation of anaphase and exit from mitosis depend on a multi-subunit ubiquitination complex called the anaphase-promoting complex (APC)1 or cyclosome. The APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26 S proteasome is essential for the initiation of sister chromatid separation at the metaphase-anaphase transition. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B.";"";""
97;Anaphase-promoting complex; APC | cyclosome;Mouse;P53995,Q8K2H6,Q8BZQ7,Q91W96,Q8BTZ4,Q9WVM3,Q3V036,Q8R349,Q8BGZ4;17222,68999,99152,52206,59008,56317,381580,69957,52563;MI:0019- coimmunoprecipitation;10318877;10.03.01,14.07.05,16.01,70.10;"The initiation of anaphase and exit from mitosis depend on a multi-subunit ubiquitination complex called the anaphase-promoting complex (APC)1 or cyclosome. The APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26 S proteasome is essential for the initiation of sister chromatid separation at the metaphase-anaphase transition. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B.";"";""
98;p300-MDM2-p53 protein complex;;Human;Q09472,Q00987,P04637;2033,4193,7157;MI:0091- chromatography technologies;11070080;11.02.03.04,18.02.01,70.10;"";"";""
100;hNURF complex;;Human;Q12830,Q09028,Q16576,P28370;2186,5928,5931,6594;MI:0071- molecular sieving | MI:0226- ion exchange chromatography;14609955;10.01.09.05,11.02.03.04,41.05.13,42.10.03,43.03.13,70.10;"NURF is a member of the ISWI-containing chromatin remodeling complexes.";"";""
101;Nucleolar remodeling complex (NoRC complex);;Mouse;Q91YE5,Q91ZW3;116848,93762;MI:0004- affinity chromatography technologies;11532953;10.01.09.05,11.02.01,42.10.03,70.10;"NoRC induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. This complex may serve a role in the regulation of the rDNA locus.";"";""
102;Meiotic cohesin complex;;Mouse;Q8C5S7,Q920F6,Q9CW03,P70281;56739,140557,13006,20962;MI:0019- coimmunoprecipitation;12759374;10.03.02.01,10.03.02.03,42.10.03,70.10,77.03.15.07;"";"";""
103;RNA polymerase II holoenzyme complex;;Human;P18074,P19447,Q00403,P29083,P29084,P35269,P13984,P32780,Q13888,Q13889,Q92759,P24928,P30876,P19387,O15514,P19388,P61218,P62487,P52434,P36954,P52435,P53803,P62875,P20226;2068,2071,2959,2960,2961,2962,2963,2965,2966,2967,2968,5430,5431,5432,5433,5434,5435,5436,5437,5438,5439,5440,5441,6908;MI:0004- affinity chromatography technologies;9305922;11.02.03.01,16.03.01,70.10;"";"";""
104;RNA polymerase II core complex;;Human;P24928,P30876,P19387,O15514,P19388,P61218,P62487,P52434,P36954,P52435,P53803,P62875;5430,5431,5432,5433,5434,5435,5436,5437,5438,5439,5440,5441;MI:0004- affinity chromatography technologies;9852112;11.02.03.01,16.03.01,70.10;"";"";""
105;Polycomb repressive complex 2 (PRC 2);;Human;O75530,Q15910,Q09028,Q16576,Q15022;8726,2146,5928,5931,23512;MI:0096- pull down | MI:0069- mass spectrometry studies of complexes;12435631;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.09,42.10.03,70.10;"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. They are methylating histones at lysine residues. PRC4 methylates preferentially the histone H1b isoform, whereas PRC2 methylated preferentially the histone H1d isoform. The PRC3 complex exclusively targets methylation of histone H3-K27, and the activity is repressed in the presence of histone H1. PRC2 also methylates histone H3-K27 but in the presence of histone H1, PRC2 methylates both H3-K27 and H1-K26.";"PRC complexes are overexpressed in breast, colon, and prostate cancers.";""
106;Srf-myogenin-E12 complex;;Mouse;P12979,Q9JM73,P15806;17928,20807,21423;MI:0004- affinity chromatography technologies | MI:0437- protein tri hybrid;8617811;11.02.03.04,43.03,45.03.12;"The formation of this complex could be one of the means by which SRF activity is deviated from proliferative to differentiating genes upon muscle cell terminal differentiation.";"";""
107;TFIIH transcription factor complex;;Human;P51946,P50613,P18074,P19447,P32780,Q13888,Q13889,Q92759,P51948;902,1022,2068,2071,2965,2966,2967,2968,4331;MI:0004- affinity chromatography technologies;9852112;01.04,10.01.05.01,10.03,11.02.03.01,11.02.03.04,18.01.01,18.02.01,70.10;"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair.";"";""
108;ApoB mRNA editing enzyme complex;;Rat;Q923K9,P38483,Q99PF5;170912,25383,171137;MI:0004- affinity chromatography technologies;10781591;11.06.03.01,16.03.03,77.03.11.07;"";"";""
109;Fertilin complex (Adam1b, Adam2);;Mouse;Q8R534,Q60718;280667,11495;MI:0019- coimmunoprecipitation;15194697;20.01.10;"The formation of the heterodimeric protein complex between the ADAM1b and ADAM2 precursors in TGC may be essential for the localization of the mature forms of these two ADAMs on the sperm surface.";"";""
112;Prefoldin complex;;Human;O60925,Q9UHV9,Q9NQP4,Q99471,O15212,P61758;5201,5202,5203,5204,10471,7411;MI:0413- electrophoretic mobility shift assay | MI:0040- electron microscopy | MI:0071- molecular sieving;12456645;14.01,42.04;"";"";""
114;SNAPc (small nuclear RNA-activating protein) complex; PTF;Human;Q16533,Q13487,Q92966,Q5SXM2,O75971;6617,6618,6619,6621,10302;MI:0019- coimmunoprecipitation;11056176;11.02.03.04,16.01,16.03.01,18.01.07,18.02.09,70.10;"Additional information about the constituents of the SNAPc complex is given in PMID:7715707 and PMID:9732265.";"";""
115;Polycomb repressive complex 1 (PRC1, hPRC-H);;Human;P35226,Q14781,O00257,Q9HC52,P08107,P78364,Q8IXK0,Q8NDX5,Q06587,Q99496,Q96GD3,O60264;648,84733,8535,57332,3303,1911,1912,80012,6015,6045,22955,8467;MI:0004- affinity chromatography technologies;12167701;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.09,42.10.03,70.10;"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones. hPRC-H apparently represents not a single complex but rather a mixture of highly related complexes, here exemplified by the M33F and Bmi1F M2 eluates. The identified beta-tubulin may be a contaminant, it needs more characterization.";"";""
116;Polycomb repressive complex 1 (PRC1, hPRC-H);;Human;P35226,Q14781,O00257,Q9HC52,P08107,P78364,Q8IXK0,Q8NDX5,Q06587,Q99496,Q96GD3,O60264,P25490;648,84733,8535,57332,3303,1911,1912,80012,6015,6045,22955,8467,7528;MI:0004- affinity chromatography technologies;12167701;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.09,42.10.03,70.10;"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones. hPRC-H apparently represents not a single complex but rather a mixture of highly related complexes, here exemplified by the Hi-Trap S eluate. The identified beta-tubulin may be a contaminant, it needs more characterization.";"";""
117;GPR56-CD81-Galphaq/11-Gbeta complex;;Human;P60033,Q9Y653,(P29992,P50148),(P62873,P62879,P16520,Q9HAV0);975,9289,(2767,2776),(2782,2783,2784,59345);MI:0019- coimmunoprecipitation;15004227;30.01.05.05.03;"The central role of CD81 (and CD9 when present) suggests possible scaffolding functions for CD81 and CD9 in GPR56 signaling.";"";""
118;GPI-GnT activity complex;;Human;P37287,Q92535,Q14442,Q9BRB3;5277,5279,5283,9091;MI:0004- affinity chromatography technologies;9463366;01.06.02.01,70.07;"This protein complex has GPI-GlcNAc transferase (GPI-GnT) activity in vitro.";"";""
120;Lymphotoxin beta receptor complex;;Human;P01374,Q06643,P36941;4049,4050,4055;MI:0019- coimmunoprecipitation;9122217;30.05,40.10.02;"The binding of heterotrimeric lymphotoxin, LT alpha1 beta2, to the LTbeta receptor (LTbeta R), a member of the tumor necrosis factor receptor (TNFR) superfamily, induces nuclear factor kappaB (NF-kappaB) activation and cell death in HT29 adenocarcinoma cells.";"";""
122;MCM complex;;Mouse;P97310,P25206,P49717,P49718,P97311,Q61881;17216,17215,17217,17218,17219,17220;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;12614612;10.01.03,10.03.02,16.19.03,70.10.03;"";"";""
123;Rnase/Mrp complex;;Human;Q99575,O95707,Q969H6,O75817,O95059,Q9H633,Q9BUL9,P78346,P78345,O75818;10940,10775,51367,10248,11102,79897,54913,10556,10557,10799;MI:0096- pull down;15096576;01.03.16.01,11.04.01,16.03.03,70.10;"RNase MRP is involved in the processing of pre-rRNA and the generation of RNA primers for mitochondrial DNA replication.";"";""
124;RGS9-GNB5-GNAT1-R9AP complex;;Bovine;P04695,O46469,Q8MJG0;281794,281453,282338;MI:0006- anti bait coimmunoprecipitation;12119397;30.01.05.05,34.11.01,70.02,77.03.02.02;"";"";"At the time of annotation, the additional member  GNB5 (Gbeta5) of the protein complex was not found in the UniProt database."
126;CCT micro-complex;;Human;P17987,P78371,P49368,P50991,P48643,P40227,Q99832,P50990;6950,10576,7203,10575,22948,908,10574,10694;MI:0029- cosedimentation through density gradients | MI:0047- far western blotting;9250675;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. CCT micro-complexes have mol. wts ranging from 120 to 250 kDa and are present in cells at lower abundance (<5%) as compared with intact CCT.";"";""
127;NDC80 kinetochore complex;;Human;O14777,Q9BZD4,Q8NBT2,Q9HBM1;10403,83540,147841,57405;MI:0019- coimmunoprecipitation;14699129;10.03.01.01,10.03.04.05,70.10.04;"Components of the conserved NDC80 complex are required for chromosome congression, and their disruption results in mitotic arrest accompanied by multiple spindle aberrations. hSPC25 is an essential kinetochore component that plays a significant role in proper execution of mitotic events.";"";""
128;ORC complex (origin recognition complex);;Mouse;Q9Z1N2,Q60862,Q9JK30,O88708,Q9WUV0,Q9WUJ8;18392,18393,50793,26428,26429,56452;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;12614612;10.01.03.03,16.19.03,70.10.03;"";"";""
129;PIDDsome complex;;Human;P42575,P78560,Q9HB75;835,8738,55367;MI:0019- coimmunoprecipitation;15073321;40.10.02.02.02,40.10.02.03;"";"PIDDsome is involved in caspase-2 dependent TSA-induced cell death in prostate cancer cell lines (PMID:17110788).";""
130;Gamma-secretase complex (Aph1a, Psen1, Psenen, Ncstn); presenilin complex;Mouse;Q8BVF7,P57716,P49769,Q9CQR7;226548,59287,19164,66340;MI:0413- electrophoretic mobility shift assay;14717705;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,34.05,40.10.02.01,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin.";"";"Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes."
131;Skeletal muscle sarcoglycan complex SGC, alpha-beta-gamma-delta;;Mouse;P82350,P82349,P82347,P82348;20391,24051,24052,24053;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;9864373;14.10,36.25.09.03,45.03.12.01,70.02,75.03.12.01;"";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
132;CCT complex (chaperonin containing TCP1 complex); TRiC;Mouse;P11983,P80314,P80318,P80315,P80316,P80317,P80313,P42932;21454,12461,12462,12464,12465,12466,12468,12469;MI:0019- coimmunoprecipitation | MI:0047- far western blotting | MI:0040- electron microscopy;10604479;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol.";"";""
136;Troponin complex;;Rabbit;P02586,P02643,P02641;100009341,100009581,0;MI:0091- chromatography technologies;12395950;16.17.01,36.25.09,45.03.12,70.04.03;"";"";""
138;Telosome complex; telomere-associated protein complex;Human;Q96AP0,Q9NUX5,P54274,Q15554,Q9NYB0,Q9BSI4;65057,25913,7013,7014,54386,26277;MI:0071- molecular sieving;15383534;14.10,16.03.01,42.10.03,70.10;"TIN2 binds TRF2 directly, thereby tethering TRF2 to the TRF1 complex. This complex is responsible for telomere maintenance.";"";""
139;SDH-mABC1-PIC-ANT-ATPase complex;;Rat;Q5RKI8,P15999,Q920L2,P21913,P16036,(Q05962,Q09073);362302,65262,157074,298596,245959,(85333,25176);MI:0027- cosedimentation | MI:0019- coimmunoprecipitation;15284438;20.01.01.01,20.03.01.01,70.16.05;"The complex constitutes the mitochondrial ATP-sensitive K(+) channel.";"";""
140;E-box sequence-binding complex; Bex2 protein complex;Human;Q9BXY8,Q86U70,P25791,Q02577;84707,8861,4005,4808;MI:0019- coimmunoprecipitation;16314316;11.02.03.04,41.05.13,70.10;"This complex may help to understand the molecular mechanisms by which hBex2 plays a role in transcriptional regulation in the brain during neurodevelopment.";"";""
141;Sos1-Abi1-Eps8 complex;;Mouse;Q8CBW3,Q08509,Q62245;11308,13860,20662;MI:0019- coimmunoprecipitation;10499589;30.01.05.05.01;"The authors  propose a model in which Eps8 mediates the transfer of signals between Ras and Rac, by forming a complex with E3b1 and Sos1.";"";""
142;CD147-gamma-secretase complex (APH-1a, PS-1, PEN-2, NCT variant);;Human;Q96BI3,P35613,Q92542,P49768,Q9NZ42;51107,682,23385,5663,55851;MI:0019- coimmunoprecipitation;15890777;14.07.11,30.01.05.03,70.02,70.08;"CD147 in gamma-secretase complex down-modulates the production of amyloid beta-peptides.";"";""
143;APP-FE65-LRP complex;;Human;O00213,P05067,Q07954;322,351,4035;MI:0019- coimmunoprecipitation | MI:0096- pull down;15115822;14.07.11;"";"";""
144;Gamma-BAR-AP1 complex;;Human;Q10567,O43747,O75843,Q9BXS5,Q9Y6Q5,P61966,P56377,Q96PC3,Q63HQ0;162,164,8906,8907,10053,1174,8905,130340,55435;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;15775984;14.04,18.01,20.09.07,20.09.07.25,20.09.18.09.01,42.09;"The isolation of AP1 adaptor complex was described in PMID:9733768.";"";""
145;CCT:PFD complex;;Mammalia;Q32L40,Q3ZBH0,Q3T0K2,Q2T9X2,Q3T115,Q3MHL7,Q2NKZ1,Q3ZCI9,O60925,Q9UHV9,Q9NQP4,Q99471,O15212,P61758;512043,505313,504735,613336,533784,521540,514355,281047,5201,5202,5203,5204,10471,7411;MI:0040- electron microscopy | MI:0028- cosedimentation in solution | MI:0226- ion exchange chromatography;12456645;14.01,16.01,16.19.03,70.03;"The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Three-dimensional reconstruction of the CCT:PFD complex based on cryoelectron microscopy reveals that PFD binds to each of the two CCT rings.";"";""
146;Src-dynamin-synapsin complex;;Mouse;P05480,O88935,(P39053,P39054);20779,20964,(13429,13430);MI:0047- far western blotting;9539797;20.09.16.09.05,77.03.01.01.01;"The SH3 domain of Src, but not that of the splice variant N-Src, bound to three proteins from mouse synaptosomes or PC12 cells: dynamin, synapsin Ia, and synapsin Ib. Src may play a regulatory role in membrane traffic events that are particularly critical in the neuron.";"";""
147;Src-dynamin-synapsin complex;;Rat;P21575,Q9WUD9,P09951;140694,83805,24949;MI:0006- anti bait coimmunoprecipitation;9539797;20.09.16.09.05;"The SH3 domain of Src, but not that of the splice variant N-Src, bound to three proteins from mouse synaptosomes or PC12 cells: dynamin, synapsin Ia, and synapsin Ib. Src may play a regulatory role in membrane traffic events that are particularly critical in the neuron.";"";""
148;Src-dynamin-synapsin-alpha-adaptin complex;;Rat;P18484,P21575,Q9WUD9,P09951;81637,140694,83805,24949;MI:0006- anti bait coimmunoprecipitation;9539797;20.09.16.09.05;"The identification of a complex containing Src, dynamin, and alpha-adaptin indicates that Src may play a more general role in membrane traffic as well.";"";""
149;PBAF complex (Polybromo- and BAF containing complex); SWI/SNF complex B;Human;Q68CP9,Q86U86,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3,(P60709,P63261),(O96019,O94805);196528,55193,6597,6598,6599,6601,6602,6605,(60,71),(86,51412);MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;11078522;10.01.09.05,11.02.03.04.01,16.03.01,30.01.09.08,30.01.11,42.10.03,70.10;"";"";"At the time of annotation, the additional member BAF240 of the protein complex was not found in the UniProt database."
150;CCT complex (chaperonin containing TCP1 complex), testis specific; TRiC;Bovine;Q32L40,Q3ZBH0,Q3T0K2,Q2T9X2,Q3T115,Q3T084,Q2NKZ1,Q3ZCI9;512043,505313,504735,613336,533784,538090,514355,281047;MI:0027- cosedimentation | MI:0091- chromatography technologies;12456645;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated.";"";""
152;TFIIE complex;;Human;P29083,P29084;2960,2961;MI:0019- coimmunoprecipitation;9836642;11.02.03.01.01,11.02.03.04,70.10;"";"";""
153;TFIIF complex (transcription factor IIF);;Human;P35269,P13984;2962,2963;MI:0027- cosedimentation;9836642;11.02.03.01.01,16.17.07,16.19.03,70.10;"TFIIF facilitates activator-dependent transcription initiation on chromatin templates.";"";""
154;Src1-Ep300-Crebbp complex;;Mouse;P45481,Q8BJ14,P70365;12914,328572,17977;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;8855229;11.02.03.04.01,18.02.07,30.05.02;"";"";""
155;TFIID complex;;Human;P21675,Q12962,Q15544,Q6P1X5,O00268,Q15542,P49848,Q16594,P20226;6872,6881,6882,6873,6874,6877,6878,6880,6908;MI:0019- coimmunoprecipitation;9836642;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"";"";""
156;Retrotranslocation complex;;Human;Q9BUN8,P57678,Q86TM6;79139,50628,84447;MI:0019- coimmunoprecipitation;16186510;20.01.10;"";"";""
157;Condensin I complex; canonical condensin complex;Human;Q15021,Q9BPX3,Q15003,O95347,Q9NTJ3;9918,64151,23397,10592,10051;MI:0019- coimmunoprecipitation;10958694;10.03.01.01,10.03.04.03,42.10.03,70.10;"";"";""
158;ATP synthasome; ATP synthase-PIC-ANC complex;Rat;P15999,P10719,P35435,P35434,P29418,P19511,Q06645,Q06646,Q71S46,P31399,P29419,P21571,Q06647,P05504,P11608,P16036,Q09073;65262,171374,116550,245965,245958,171375,29754,171082,114630,641434,140608,94271,192241,26197,26196,245959,25176;MI:0047- far western blotting | MI:0027- cosedimentation | MI:0020- transmission electron microscopy | MI:0410- electron tomography;12560333;02.11,02.13.03,02.45.15;"";"";"Two additional members of complex have been described as ATP synthase g chain and ATP synthase f chain."
159;Condensin I-PARP-1-XRCC1 complex;;Human;Q15021,Q9BPX3,Q15003,P09874,O95347,Q9NTJ3,P18887;9918,64151,23397,142,10592,10051,7515;MI:0006- anti bait coimmunoprecipitation;16543152;10.01.05.01,32.01.09,70.10;"The association between PARP-1 and XRCC1 was enhanced in response to DNA damage.";"";""
160;Condensin II;;Human;P42695,Q86XI2,Q6IBW4,O95347,Q9NTJ3;23310,54892,29781,10592,10051;MI:0006- anti bait coimmunoprecipitation;14532007;10.03.01.01,10.03.04.03,42.10.03,70.10;"";"";""
161;SWAP complex;;Mouse;P09405,Q61937,P11103,Q6A028;17975,18148,11545,20947;MI:0004- affinity chromatography technologies;9642267;10.01.05.03.03,36.25.16.03.01,70.10,73.03.07.02.01.01;"SWAP complex has recombination activity and is specific for switching B-cells and prefers S-region substrates. S regions, several kilobase pairs in length, contain short, G-rich repetitive sequence elements, often arranged in tandem arrays (PMID:9642267).";"";""
162;Conserved oligomeric Golgi (COG) complex;;Human;Q8WTW3,Q14746,Q96JB2,Q9H9E3,Q9UP83,Q9Y2V7,P83436,Q96MW5;9382,22796,83548,25839,10466,57511,91949,84342;MI:0040- electron microscopy | MI:0047- far western blotting | MI:0069- mass spectrometry studies of complexes;11980916;14.07.02,20.09.07.05,42.08,70.08;"";"Deficiencies in COG1, COG7, COG8 cause a novel group of Cogenital Disorders of Glycosylation II (PMID:17904886).";""
163;Cohesin-SA2 complex;;Human;O60216,Q14683,Q9UQE7,Q8N3U4;5885,8243,9126,10735;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;10931856;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"";"";""
164;Cohesin-SA1 complex;;Human;O60216,Q14683,Q9UQE7,Q8WVM7;5885,8243,9126,10274;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;10931856;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"In HeLa cell extracts, the ratio between the hSA1-containing complex (h-cohesin SA1) and the hSA2-containing complex (h-cohesin SA2) is about 1:3.";"";""
165;Cohesin-SA1 complex;;Human;O60216,Q14683,Q9UQE7,Q8WVM7;5885,8243,9126,10274;MI:0004- affinity chromatography technologies;11250156;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"The cohesin complex binds directly to double-stranded DNA and induces the formation of large protein-DNA aggregates.";"";""
166;Cohesin-SA2 complex;;Human;O60216,Q14683,Q9UQE7,Q8N3U4;5885,8243,9126,10735;MI:0004- affinity chromatography technologies;11250156;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"The cohesin complex binds directly to double-stranded DNA and induces the formation of large protein-DNA aggregates.";"";""
167;Condensin I complex; canonical condensin complex;Human;Q15021,Q9BPX3,Q15003,O95347,Q9NTJ3;9918,64151,23397,10592,10051;MI:0004- affinity chromatography technologies;11250156;10.03.01.01,10.03.04.03,42.10.03,70.10;"";"";""
168;Protein-sorting complex (Stam2, Hgs, Eps15);;Mouse;P42567,Q99LI8,O88811;13858,15239,56324;MI:0019- coimmunoprecipitation;12551915;14.04;"Hrs, Eps15, and STAM proteins function in a multivalent complex that sorts ubiquitinated proteins into the multivesicular body pathway.";"";""
169;Protein-sorting complex (Stam1, Hgs, Eps15);;Mammalia;P42567,Q99LI8,Q92783;13858,15239,8027;MI:0019- coimmunoprecipitation;12551915;14.04;"Hrs, Eps15, and STAM proteins function in a multivalent complex that sorts ubiquitinated proteins into the multivesicular body pathway.";"";""
170;Ric-8A G(i) alpha-1 subunit complex;;Rat;P10824,Q80ZG1;25686,293614;MI:0018- two hybrid | MI:0027- cosedimentation;12509430;18.02.03;"";"";""
171;Ric-8A G(i) alpha-2 subunit complex;;Rat;P04897,Q80ZG1;81664,293614;MI:0018- two hybrid | MI:0027- cosedimentation;12509430;18.02.03;"";"";""
172;Ric-8A G(o) alpha-1 subunit complex;;Rat;P59215,Q80ZG1;50664,293614;MI:0018- two hybrid | MI:0027- cosedimentation;12509430;18.02.03;"";"";""
173;MRN complex (MRE11-RAD50-NBN complex); RAD50-MRE11-p95 complex;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0004- affinity chromatography technologies;9705271;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"MRN complex possesses manganese-dependent single-stranded DNA endonuclease and 3' to 5' exonuclease activities, important for recombination, repair, and genomic stability.";"Nibrin is mutated in Nijmegen breakage syndrome.";""
174;Ric-8A G(o) alpha-2 subunit complex;;Rat;P59215,Q80ZG1;50664,293614;MI:0018- two hybrid | MI:0027- cosedimentation;12509430;18.02.03;"";"";""
175;Ric-8A G(q) alpha subunit complex;;Rat;P82471,Q80ZG1;81666,293614;MI:0018- two hybrid | MI:0027- cosedimentation;12509430;18.02.03;"";"";""
176;Ric-8A G alpha 13 complex;;Rat;Q6Q7Y5,Q80ZG1;303634,293614;MI:0018- two hybrid | MI:0027- cosedimentation;12509430;18.02.03;"";"";""
177;OGT-TRAK1-TRAK2 complex;;Human;O15294,Q9UPV9,O60296;8473,22906,66008;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;12435728;14.07.09,30.05.02.24.04;"O-GlcNAc, OGT, and GRIF-1 could be involved in GABA signaling. GRIF-1 would function as an adaptor/scaffolding protein, bridging OGT to GABAA receptor in this model.";"";""
178;Respiratory chain complex I (holoenzyme), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3);Human;P03886,P03891,P03897,P03901,P03915,P03923,O15239,O95299,Q86Y39,Q9UI09,Q9P0J0,O43678,O95167,O00483,Q16718,P56556,O95182,P51970,Q16795,O14561,O75438,O96000,Q9NX14,O95178,O43676,O95168,O43674,O95139,P17568,O95169,Q9Y6M9,O43677,O95298,P28331,O75306,O75489,O43181,O43920,O75380,O75251,O00217,P49821,P19404,P56181;4535,4536,4537,4539,4540,4541,4694,4705,126328,55967,51079,4695,4696,4697,4698,4700,4701,4702,4704,4706,4707,4716,54539,4708,4709,4710,4711,4712,4713,4714,4715,4717,4718,4719,4720,4722,4724,4725,4726,374291,4728,4723,4729,4731;MI:0006- anti bait coimmunoprecipitation;12611891;02.11.05,02.13.03,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
179;Nephrin multiprotein complex;;Rat;Q62915,B5DFH1,O88382,Q9R044,Q9WUX0,P16086,(Q9Z1P2,Q9QXQ0);29647,361598,113970,64563,305614,64159,(81634,63836);MI:0096- pull down | MI:0051- fluorescence technologies | MI:0069- mass spectrometry studies of complexes;15994232;34.07.01,42.06,43.03;"";"";""
180;PNUTS-PP1 complex;;Human;P62136,Q96QC0;5499,5514;MI:0019- coimmunoprecipitation;12574161;18.02.01.02;"";"";""
181;26S proteasome;;Human;P25786,P25787,P25788,P25789,P28066,P60900,O14818,P20618,P49721,P49720,P28070,P28074,P28072,Q99436,P62191,P35998,P17980,P43686,P62195,P62333,Q9UNM6,P55036;5682,5683,5684,5685,5686,5687,5688,5689,5690,5691,5692,5693,5694,5695,5700,5701,5702,5704,5705,5706,5719,5710;MI:0019- coimmunoprecipitation;11812135;14.13.01.01,16.01,32.01,70.03,70.10;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
182;Synaptotagmin-sodium channel complex (Syt1-Scn1a-Scn1b);;Rat;P04774,Q00954,P21707;81574,29686,25716;MI:0006- anti bait coimmunoprecipitation;10737807;20.01.01.01,20.03.01.01,20.09.16.09.03,34.03,70.02;"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.";"";""
183;Synaptotagmin-sodium channel complex (Syt2-Scn1a-Scn1b);;Rat;P04774,Q00954,P29101;81574,29686,24805;MI:0006- anti bait coimmunoprecipitation;10737807;20.01.01.01,20.03.01.01,20.09.16.09.03,34.03,70.02;"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.";"";""
184;Synaptotagmin-sodium channel complex  (Syt1-Scn2a-Scn1b);;Rat;Q00954,P04775,P21707;29686,24766,25716;MI:0006- anti bait coimmunoprecipitation;10737807;20.01.01.01,20.03.01.01,20.09.16.09.03,34.03,70.02;"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.";"";""
185;Synaptotagmin-sodium channel complex (Syt2-Scn2a-Scn1b);;Rat;Q00954,P04775,P29101;29686,24766,24805;MI:0006- anti bait coimmunoprecipitation;10737807;20.01.01.01,20.03.01.01,20.09.16.09.03,34.03,70.02;"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.";"";""
186;Wave-2 complex;;Human;Q8IZP0,Q8WUW1,Q7L576,Q9Y2A7,Q9Y6W5;10006,55845,23191,10787,10163;MI:0029- cosedimentation through density gradients | MI:0091- chromatography technologies;15070726;30.01.05.05.01,34.05.01,42.04.03,70.04.03;"Proteins are only present in the complexed form, with the exception of Hspc (C3orf10). The complex is organized around a core of Nap and Abi. Sra is a peripheral subunit recruited on the Nap side, whereas the Wave and Hspc subunits are recruited on the Abi side of the core.";"";""
187;Wave-2 complex (Rac-activated);;Mouse;Q8CBW3,Q7TMB8,P28660,Q8BPG5,Q8BH43;11308,20430,50884,19353,242687;MI:0019- coimmunoprecipitation | MI:0096- pull down;14765121;30.01.05.05.01,34.05,42.04.03,70.04.03;"The complex is constitutively assembled in the presence and absence of active Rac in vivo. The authors show that Sra-1 and Nap1 colocalize with Abi-1 and WAVE2 at the interface between the lamellipodial actin meshwork and the membrane. These proteins form stable complexes in vivo that can be immunoprecipitated from resting cells, upon Rac activation by AlF treatment and upon overexpression of constitutively active Rac.";"";""
188;Wave-2 complex;;Mouse;Q8CBW3,Q7TMB8,P28660,Q8BH43;11308,20430,50884,242687;MI:0019- coimmunoprecipitation | MI:0096- pull down;14765121;30.01.05.05.01,34.05,42.04.03,70.04.03;"The complex is constitutively assembled in the presence and absence of active Rac in vivo. The authors show that Sra-1 and Nap1 colocalize with Abi-1 and WAVE2 at the interface between the lamellipodial actin meshwork and the membrane. These proteins form stable complexes in vivo that can be immunoprecipitated from resting cells, upon Rac activation by AlF treatment and upon overexpression of constitutively active Rac.";"";""
189;BAF complex; SWI/SNF complex A;Human;P51531,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3,(P60709,P63261),(O96019,O94805),(O14497,Q8NFD5);6595,6597,6598,6599,6601,6602,6605,(60,71),(86,51412),(8289,57492);MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;11078522;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10;"";"";"At the time of annotation, the additional member BAF110 of the protein complex was not found in the UniProt database."
190;Mitotic checkpoint complex (MCC); APC/C inhibitory factor;Human;O60566,O43684,Q12834,Q13257;701,9184,991,4085;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;11535616;10.03.01.03;"MCC inhibitory activity is 3,000-fold greater than that of recombinant MAD2, MCC is not generated from kinetochores, as it is also present and active in interphase cells.";"";""
191;20S proteasome;;Human;P25786,P25787,P25788,P25789,P28066,P60900,O14818,P20618,P49721,P49720,P28070,P28074,P28072,Q99436;5682,5683,5684,5685,5686,5687,5688,5689,5690,5691,5692,5693,5694,5695;MI:0029- cosedimentation through density gradients;7811265;14.07.11,14.13.01.01,32.01,70.03,70.10;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
192;PA28-20S proteasome;;Human;P25786,P25787,P25788,P25789,P28066,P60900,O14818,P20618,P49721,P49720,P28070,P28074,P28072,Q99436,Q06323,Q9UL46;5682,5683,5684,5685,5686,5687,5688,5689,5690,5691,5692,5693,5694,5695,5720,5721;MI:0029- cosedimentation through density gradients;11676531;14.07.11,14.13.01.01,32.01,70.03,70.10;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
193;PA700-20S-PA28 complex; proteasome;Human;P25786,P25787,P25788,P25789,P28066,P60900,O14818,P20618,P49721,P49720,P28070,P28074,P28072,Q99436,P62191,P35998,P17980,P43686,P62195,P62333,Q99460,O75832,O00231,O00232,Q9UNM6,O00487,Q13200,O43242,P55036,Q16401,Q15008,P51665,P48556,O00233,Q06323,Q9UL46;5682,5683,5684,5685,5686,5687,5688,5689,5690,5691,5692,5693,5694,5695,5700,5701,5702,5704,5705,5706,5707,5716,5717,5718,5719,10213,5708,5709,5710,5711,9861,5713,5714,5715,5720,5721;MI:0029- cosedimentation through density gradients;11676531;14.13.01.01,16.01,18.01.07,18.02.01.01.03;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
194;PA28gamma-20S proteasome;;Human;P25786,P25787,P25788,P25789,P28066,P60900,O14818,P20618,P49721,P49720,P28070,P28074,P28072,Q99436,P61289;5682,5683,5684,5685,5686,5687,5688,5689,5690,5691,5692,5693,5694,5695,10197;MI:0029- cosedimentation through density gradients;7811265;14.07.11,14.13.01.01,32.01,70.03,70.10;"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.";"";""
195;Ubiquitin E3 ligase (Lrrc41, Tceb1, Tceb2, Cul5, Rbx1);Muf1-Elongin BC-Cul5-Rbx1 complex;Rat;Q9JJ31,Q5M9H1,Q498D8,P83941,P62870;64624,362566,300084,64525,81807;MI:0019- coimmunoprecipitation;11384984;14.07.05,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
196;Ubiquitin E3 ligase (Vhl, Tceb1, Tceb2, Cul5, Rbx1);VHL-Elongin BC-Cul5-Rbx1 complex;Rat;Q9JJ31,Q498D8,P83941,P62870,Q64259;64624,300084,64525,81807,24874;MI:0019- coimmunoprecipitation;11384984;14.07.05;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
197;Ubiquitin E3 ligase (Vhl, Tceb1, Tceb2, Cul2, Rbx1);VHL-Elongin BC-Cul2-Rbx1 complex;Rat;Q9D4H8,Q498D8,P83941,P62870,Q64259;71745,300084,64525,81807,24874;MI:0019- coimmunoprecipitation;11384984;14.07.05;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";"Since Cul2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
198;Ubiquitin E3 ligase (Tceb1, Tceb2, Tceb3, Cul5, Rbx1);Elongin A-Elongin BC-Cul5-Rbx1 complex;Rat;Q9JJ31,Q498D8,P83941,P62870,Q63187;64624,300084,64525,81807,25562;MI:0019- coimmunoprecipitation;11384984;14.07.05;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
199;Ubiquitin E3 ligase (Socs1, Tceb1, Tceb2, Cul5, Rbx1);Socs1-Elongin BC-Cul5-Rbx1 complex;Rat;Q9JJ31,Q498D8,Q9QX78,P83941,P62870;64624,300084,252971,64525,81807;MI:0019- coimmunoprecipitation;11384984;14.07.05;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
200;Ubiquitin E3 ligase (Wsb1, Tceb1, Tceb2, Cul5, Rbx1);Wsb1-Elongin BC-Cul5-Rbx1 complex;Rat;Q9JJ31,Q498D8,P83941,P62870,Q4KM78;64624,300084,64525,81807,303336;MI:0019- coimmunoprecipitation;11384984;14.07.05,14.13.01.01,16.01,30.05.02.16,70.07;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
201;HUIC complex; BRCA1-BARD1 complex;Human;Q99728,P38398;580,672;MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients;11504724;10.03.01.02,10.03.01.03,70.10;"The HUIC complex has been isolated after treating cells with hydroxyurea.";"BRCA1 is involved in breast cancer.";""
202;BRCA1-RAD50-MRE11-NBS1 complex;;Human;P38398,P49959,O60934,Q92878;672,4361,4683,10111;MI:0004- affinity chromatography technologies | MI:0007- anti tag coimmunoprecipitation;11504724;10.01.05.01,32.01.09,70.10;"";"BRCA1 is involved in breast cancer.";""
203;Ubiquitin E3 ligase (Med8, Tceb1, Tceb2, Cul2, Rbx1);Med8-Elongin BC-Cul2-Rbx1 complex;Rat;Q9D4H8,Q9D7W5,Q498D8,P83941,P62870;71745,80509,300084,64525,81807;MI:0019- coimmunoprecipitation;12149480;14.07.05,16.01,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. ";"";"Since Cul2 and Med8 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
204;Ubiquitin E3 ligase (Asb2, Tceb1, Tceb2, Cul5, Rbx1);Asb2-Elongin BC-Cul5-Rbx1 complex;Rat;Q5U2S6,Q9JJ31,Q498D8,P83941,P62870;299266,64624,300084,64525,81807;MI:0019- coimmunoprecipitation;15590664;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. ";"Results suggest that Asb2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate.";""
205;Ubiquitin E3 ligase (VHL, TCEB1, TCEB2, CUL2, RBX1);VHL-Elongin BC-CUL2-RBX1 complex;Human;Q13617,P62877,Q15369,Q15370,P40337;8453,9978,6921,6923,7428;MI:0028- cosedimentation in solution;10535940;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
206;DNA ligase IV-XRCC4 complex;;Human;P49917,Q13426;3981,7518;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;9259561;10.01.05.01,10.01.05.03.03,16.03.01,70.10.03;"XRCC4 serves as a molecular bridge to target DNA ligase IV to a DNA double-strand break.";"";""
207;Ubiquitin E3 ligase (ASB2, TCEB1, TCEB2, CUL5, RNF7); Asb2-Elongin BC-Cul5-Rbx2 complex;Human;Q96Q27,Q93034,Q9UBF6,Q15369,Q15370;51676,8065,9616,6921,6923;MI:0028- cosedimentation in solution;16325183;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. ";"";"The presence of Elongin BC was predicted by the authors but has not been shown experimentally."
208;Ubiquitin E3 ligase (ASB1, TCEB1, TCEB2, CUL5, RNF7); Asb1-Elongin BC-Cul5-Rbx2 complex;Human;Q9Y576,Q93034,Q9UBF6,Q15369,Q15370;51665,8065,9616,6921,6923;MI:0028- cosedimentation in solution;16325183;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";"The presence of Elongin BC was predicted by the authors but has not been shown experimentally."
209;Ubiquitin E3 ligase (ASB6, TCEB1, TCEB2, CUL5, RNF7); Asb6-Elongin BC-Cul5-Rbx2 complex;Human;Q9NWX5,Q93034,Q9UBF6,Q15369,Q15370;140459,8065,9616,6921,6923;MI:0028- cosedimentation in solution;16325183;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";"The presence of Elongin BC was predicted by the authors but has not been shown experimentally."
210;Ubiquitin E3 ligase (ASB7, TCEB1, TCEB2, CUL5, RNF7); Asb7-Elongin BC-Cul5-Rbx2 complex;Human;Q9H672,Q93034,Q9UBF6,Q15369,Q15370;140460,8065,9616,6921,6923;MI:0028- cosedimentation in solution;16325183;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";"The presence of Elongin BC was predicted by the authors but has not been shown experimentally."
211;Ubiquitin E3 ligase (ASB12, TCEB1, TCEB2, CUL5, RNF7); Asb12-Elongin BC-Cul5-Rbx2 complex;Human;Q8WXK4,Q93034,Q9UBF6,Q15369,Q15370;142689,8065,9616,6921,6923;MI:0028- cosedimentation in solution;16325183;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";"The presence of Elongin BC was predicted by the authors but has not been shown experimentally."
212;DNA ligase III-XRCC1 complex;;Human;P49916,P18887;3980,7515;MI:0004- affinity chromatography technologies;7760816;10.01.05.01,70.10;"";"";""
213;DNA ligase IV-XRCC1 complex;;Human;P49917,P18887;3981,7515;MI:0004- affinity chromatography technologies;7760816;10.01.05.01,70.10;"";"";""
214;Ubiquitin E3 ligase (WSB1, TCEB1, TCEB2, CUL5, RBX1);WSB1-Elongin BC-CUL5-RBX1 complex;Human;Q93034,P62877,Q15369,Q15370,Q9Y6I7;8065,9978,6921,6923,26118;MI:0019- coimmunoprecipitation;15965468;14.07.05,14.13.01.01,16.01,30.05.02.16,70.07;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. WSB-1 is a Hedgehog-inducible ubiquitin ligase that modulates thyroid hormone activation and PTHrP secretion in the developing growth plate.";"";""
216;PDZK1-NaPiIIa-MAP17 complex;;Mouse;Q9JIL4,Q9CQH0,Q60825;59020,67182,20505;MI:0018- two hybrid;12837682;20.01.01;"";"";""
217;CRSP complex;cofactor required for Sp1;Human;Q15648,O60244,Q9NVC6,Q9ULK4,O75448,O95402,Q6P2C8,O43513;5469,9282,9440,9439,9862,9441,9442,9443;MI:0029- cosedimentation through density gradients | MI:0226- ion exchange chromatography;10377381;11.02.03.04.01,16.01,70.10;"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"Information about the 85kD component CRSP5 of the protein complex is not available in databases."
218;CRSP complex; cofactor required for Sp1;Human;Q15648,O60244,Q9NVC6,Q9ULK4,O75448,O95402,Q6P2C8,O43513;5469,9282,9440,9439,9862,9441,9442,9443;MI:0029- cosedimentation through density gradients | MI:0226- ion exchange chromatography;9989412;11.02.03.04.01,16.01,70.10;"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"At the time of annotation, the additional 85kD component CRSP5 of the protein complex was not found in the UniProt database. "
219;CAND1-CUL1-RBX1 complex;;Human;Q86VP6,Q13616,P62877;55832,8454,9978;MI:0007- anti tag coimmunoprecipitation;15537541;16.01,18.01.07,18.02.01;"Cand1 forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 protein-ubiquitin ligase complex.";"";""
220;ARF-Mule complex; ARF-BP1-ARF-NPM1 complex;Human;Q8N726,Q7Z6Z7,P06748;1029,10075,4869;MI:0007- anti tag coimmunoprecipitation;15989956;16.01,70.10;"ARF is an inhibitor of the ARF-BP1 protein-ubiquitin ligase.";"";""
221;CAND1-CUL2-RBX1 complex;;Human;Q86VP6,Q13617,P62877;55832,8453,9978;MI:0007- anti tag coimmunoprecipitation;12609982;16.01,18.01.07,18.02.01;"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.";"";""
222;CAND1-CUL3-RBX1 complex;;Human;Q86VP6,Q13618,P62877;55832,8452,9978;MI:0007- anti tag coimmunoprecipitation;12609982;16.01,18.01.07,18.02.01;"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.";"";""
223;CAND1-CUL4A-RBX1 complex;;Human;Q86VP6,Q13619,P62877;55832,8451,9978;MI:0007- anti tag coimmunoprecipitation;12609982;16.01,18.01.07,18.02.01;"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.";"";""
224;CAND1-CUL4B-RBX1 complex;;Human;Q86VP6,Q13620,P62877;55832,8450,9978;MI:0007- anti tag coimmunoprecipitation;12609982;16.01,18.01.07,18.02.01;"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.";"";""
226;Ubiquitin E3 ligase (SKP1A, SKP2, CUL1);SKP1-SKP2-CUL1 complex;Human;Q13616,P63208,Q13309;8454,6500,6502;MI:0007- anti tag coimmunoprecipitation;12609982;14.07.05,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
227;Ubiquitin E3 ligase (SKP1A, BTRC, CUL1);Skp1-Btrc-Cul1 complex;Human;Q9Y297,Q13616,P63208;8945,8454,6500;MI:0007- anti tag coimmunoprecipitation;9990852;14.07.05,14.13.01.01,16.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
228;SMCC complex; SRB/MED-containing cofactor complex;Human;P24863,P49336,Q15648,O60244,Q13503,O75448,Q9Y3C7,O75586;892,1024,5469,9282,9412,9862,51003,10001;MI:0007- anti tag coimmunoprecipitation;10024883;11.02.03.04.01,11.02.03.04.03,16.01,18.01.07,18.02.09,70.10;"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
229;NAT complex;;Human;P24863,P49336,Q9BTT4,O60244,Q13503,Q9ULK4,O75586;892,1024,84246,9282,9412,9439,10001;MI:0019- coimmunoprecipitation;9734358;11.02.03.04.03,16.01,70.10;"A complex, NAT, that represses activation of transcription by RNAPII has been isolated. The NAT complex is composed of approximately 20 polypeptides and includes a subset of the Srb polypeptides, hSrb7, hSrb10, and hSrb11, as well as hRgr1 and hMed6. The presence of hSrb10, hSrb11, and hRgr1 in a complex that functions to down-regulate transcription is consistent with studies in yeast demonstrating that Srb8-Srb11, as well as Rgr1, function as negative regulators of transcription in vivo. It has been suggested that the NAT complex is a subcomplex of the RNAPII holoenzyme and its function and regulation is through the RNAPII holoenzyme. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
230;Mediator complex; Mediator of transcriptional regulation;Human;P24863,Q9BWU1,P49336,Q15648,Q9BTT4,Q9P086,Q93074,Q9UHV7,Q71F56,O60244,Q96RN5,Q9Y2X0,Q9NVC6,Q9BUE0,Q9H944,Q13503,Q15528,Q9ULK4,O75448,Q71SY5,O95402,Q6P2C8,Q9H204,Q9NX70,Q96HR3,Q9Y3C7,Q9NPJ6,O75586,O43513,Q96G25,Q9NWA0,A0JLT2;892,23097,1024,5469,84246,400569,9968,9969,23389,9282,51586,10025,9440,54797,9477,9412,6837,9439,9862,81857,9441,9442,80306,55588,90390,51003,29079,10001,9443,112950,55090,219541;MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;15175163;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10;"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
232;ARC complex; activator-recruited cofactor;Human;Q9UKU7,Q15648,Q93074,Q9UHV7,O60244,Q96RN5,Q9NVC6,Q9ULK4,O75448,Q71SY5,O95402,Q9NPJ6,O75586,O43513,Q96G25;27034,5469,9968,9969,9282,51586,9440,9439,9862,81857,9441,29079,10001,9443,112950;MI:0004- affinity chromatography technologies;10235267;11.02.03.04.01,16.01,18.01.07,18.02.09,30.01,70.10;"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors. According to authors, the ARC complex is probably identical to the DRIP complex.";"";""
234;HuCHRAC complex;;Human;Q9NRL2,Q9NRG0,Q9NRF9,O60264;11177,54108,54107,8467;MI:0226- ion exchange chromatography;10880450;10.01.09.05,16.01,16.03.01,16.19.03,70.10;"HuCHRAC is a member of the ISWI-containing chromatin remodelling complexes. The polyclonal antibodies against ISWI do not discriminate between hSNF2L and hSNF2H.";"";""
235;WICH complex; WSTF-ISWI chromatin remodeling complex;Mouse;Q9Z277,Q91ZW3;22385,93762;MI:0096- pull down;11980720;10.01.09.05,16.01,16.03.01,70.10.03;"WICH is a member of the ISWI-containing chromatin remodelling complexes.";"";""
236;WICH complex; WSTF-ISWI chromatin remodeling complex;Human;Q9UIG0,O60264;9031,8467;MI:0096- pull down;11980720;10.01.09.05,16.01,16.03.01,16.19.03,70.10.03;"WICH is a member of the ISWI-containing chromatin remodelling complexes.";"";""
237;Ags3-Lkb1-Gnai3 complex;;Rat;P08753,Q9R080;25643,246254;MI:0096- pull down;12719437;30.01.05.05;"";"";"At the time of annotation, the additional member Lkb1 (Stk11) of the protein complex was not found in the UniProt database."
238;SWI-SNF chromatin remodeling-related-BRCA1 complex;;Human;O96019,P38398,P51531,P51532,Q12824,Q92922,Q8TAQ2,Q92925,Q969G3,(O14497,Q8NFD5);86,672,6595,6597,6598,6599,6601,6603,6605,(8289,57492);MI:0071- molecular sieving | MI:0004- affinity chromatography technologies;10943845;10.01.09.05,11.02.03.04,42.10.03,70.10;"BRCA1 interacts directly with BRG1.";"BRCA1 gene is involved in breast and ovarian cancers.";""
239;Sin3-Hdac1-Sds3 complex;;Mouse;O09106,Q62141,Q8BR65;433759,20467,71954;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;11909966;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,70.10;"";"";""
240;BRCA1-CTIP-ZBRK1 repressor complex;;Human;P38398,Q99708,Q9GZX5;672,5932,59348;MI:0006- anti bait coimmunoprecipitation;16843262;11.02.03.04.03,16.03.01,70.10;"";"BRCA1 is involved in breast cancer.";""
241;BLOC-3 (biogenesis of lysosome-related organelles complex 3);;Human;Q92902,Q9NQG7;3257,89781;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients | MI:0071- molecular sieving;12756248;42.22,42.25;"The results demonstrate that the HPS1 and HPS4 proteins are components of a cytosolic complex that is involved in the biogenesis of lysosomal-related organelles by a mechanism distinct from that operated by AP-3 complex.";"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome (PMID:15030569).";""
242;BRCA1-BACH1 complex;;Human;P38398,Q9BX63;672,83990;MI:0006- anti bait coimmunoprecipitation;11301010;10.01.05.01,70.10;"An intact BRCA1 C-terminal region is necessary for the interaction with BACH1. ";"BRCA1 is involved in breast cancer.";""
243;RalBP1-CDC2-CCNB1 complex;;Human;P14635,P06493,Q15311;891,983,10928;MI:0019- coimmunoprecipitation | MI:0096- pull down;12775724;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"The complex was only detected in mitotic cell extracts. The authors show that RLIP76 associates with a catalytically active cyclinB·p34cdc2(cdk1) complex.";"";""
244;BRAFT complex; BLM complex I;Human;P54132,O15360,Q00597,Q9HB96,Q9NPI8,O15287,Q9NW38,P40692,Q9H9A7,P27694,P15927,P35244,Q13472;641,2175,2176,2178,2188,2189,55120,4292,80010,6117,6118,6119,7156;MI:0006- anti bait coimmunoprecipitation;12724401;10.01.02,10.01.05.01,32.01.09,70.10;"";"BRAFT complex is involved in Fanconi Anemia (FA) and Bloom Syndrome (BS).";"The BRAFT complex contains several other proteins of unknown function, called FAAPs or BLAPs. FAAP 43 has been identified as FANCL/PHF9 in a following paper (PMID:12973351)."
245;FA core complex (Fanconi anemia core complex);;Human;Q0VG06,O15360,Q8NB91,Q00597,Q9HB96,Q9NPI8,O15287,Q9NW38,Q9H9A7;80233,2175,2187,2176,2178,2188,2189,55120,80010;MI:0006- anti bait coimmunoprecipitation;12724401;14.07.05,32.01.09,70.10;"";"FA complex is involved in Fanconi anemia (FA) disease.";"FANCB and FANCL have been designated as FAAP90 and FAAP43. RMI1 has been designated as FAAP75."
246;BLM complex III; BLM-CIII complex;Human;P54132,P40692,Q9H9A7,Q13472;641,4292,80010,7156;MI:0006- anti bait coimmunoprecipitation;12724401;10.01.02,10.01.05.01,32.01.09,70.10;" ";"BLM complex III is involved in Bloom syndrome (BS).";"Another subunit of the complex was found in the analysis, which has not been further characterized: BLAPp100."
247;RalBP1-CCNB1-AP2A-NUMB-EPN1 complex;;Human;P14635,Q9Y6I3,P49757,Q15311,(O95782,O94973);891,29924,8650,10928,(160,161);MI:0019- coimmunoprecipitation;12775724;10.03.01.01,20.09.18.09.01,70.10;"RLIP, an effector of the RAL GTPases, is important for the mitotic cdk1 to facilitate the phosphorylation of Epsin.";"";""
248;BRAFT complex;;Human;P54132,O15360,Q00597,Q9HB96,Q9NPI8,O15287,Q9NW38,P27694,P15927,P35244,Q13472;641,2175,2176,2178,2188,2189,55120,6117,6118,6119,7156;MI:0006- anti bait coimmunoprecipitation;12973351;10.01.02,10.01.05.01,14.07.05,32.01.09,70.10;"";"";"FANCL/PHF9 (formerly called FAAP 43) is a newly identified component of the BRAFT complex."
249;Caspase-2-TRAF2-RIP1 complex;;Mouse;P29594,Q62172,P39429;12366,19765,22030;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving;15590671;30.01.05.01.03,30.01.05.01.04;"This complex activates NF-kappaB and p38 MAPK through the caspase recruitment domain of caspase-2 independently of its proteolytic activity.";"";""
251;BCDX2 complex; RAD51B-RAD51C-RAD51D-XRCC2 complex;Human;O43502,O15315,O75771,O43543;5889,5890,5892,7516;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;11751635;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"BCDX2 binds specifically to nicks in duplex DNA (PMID:11751635).";"";""
252;RAD51C-XRCC3 complex;;Human;O43502,O43542;5889,7517;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;11751635;01.04,10.01.05.01,10.01.05.03,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
253;RAD51C-XRCC3 complex;;Human;O43502,O43542;5889,7517;MI:0004- affinity chromatography technologies;15037616;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"The authors postulate that XRCC3 regulates the dissociation and formation of Rad51C-XRCC3 complex through ATP binding and hydrolysis.";"";""
254;TBPIP/HOP2-MND1 complex;;Human;Q9BWT6,Q9P2W1;84057,29893;MI:0004- affinity chromatography technologies;16407260;10.01.05.03.01,10.03.02,10.03.04,16.03.01,18.01.07,18.02.01,70.10;"The complex ensures proper pairing between homologous chromosomes.";"";""
255;TBPIP/HOP2-Mnd1 complex;;Mouse;Q8K396,O35047;76915,19183;MI:0004- affinity chromatography technologies;15834424;10.01.05.03.01,10.03.02,10.03.04,16.01,16.03.01,18.01.07,18.02.01,70.10;"The complex ensures proper pairing between homologous chromosomes.";"";""
256;RAD51B-RAD51C complex;;Human;O43502,O15315;5889,5890;MI:0006- anti bait coimmunoprecipitation;11751636;10.01.05.01,10.01.05.03,16.03.01,16.19.03,70.10;"";"";""
257;Hop2-Mnd1 complex;;Mouse;Q8K396,O35047;76915,19183;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;16675459;10.01.05.03.01,10.03.02.01,16.01,16.03.01,18.01.07,18.02.01,70.10;"Only the heterodimeric complex, but not the individual proteins, can stimulate strand invasion by Dmc1.";"";""
258;BCDX2 complex; RAD51B-RAD51C-RAD51D-XRCC2 complex;Human;O43502,O15315,O75771,O43543;5889,5890,5892,7516;MI:0007- anti tag coimmunoprecipitation;11842113;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
259;RAD51C-XRCC3 complex;;Human;O43502,O43542;5889,7517;MI:0007- anti tag coimmunoprecipitation;11842113;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
260;RAD51B-RAD51C complex;;Human;O43502,O15315;5889,5890;MI:0006- anti bait coimmunoprecipitation;11744692;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
261;RAD51B-RAD51C-RAD51D-XRCC2-XRCC3 complex;;Human;O43502,O15315,O75771,O43543,O43542;5889,5890,5892,7516,7517;MI:0006- anti bait coimmunoprecipitation;11744692;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
262;RAD51L3-XRCC2 complex;;Human;O75771,O43543;5892,7516;MI:0096- pull down;10871607;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10;"";"";""
263;R/M complex (RAD50-MRE11 complex);;Human;P49959,Q92878;4361,10111;MI:0004- affinity chromatography technologies | MI:0428- imaging techniques;11741547;01.03.16.03,10.01.05.01,16.03.01,32.01.09,42.10.03,70.10;"R/M consists of two highly flexible intramolecular coiled coils emanating from a central globular DNA binding domain.";"";""
264;R/M complex (RAD50-MRE11 complex);;Human;P49959,Q92878;4361,10111;MI:0428- imaging techniques;15165861;01.03.16.03,10.01.05.01,16.03.01,32.01.09,42.10.03,70.10;"Human Rad50-Mre11 complexes are predominantly heterotetramers.";"";""
265;ATR-ATRIP complex;;Human;Q13535,Q8WXE1;545,84126;MI:0091- chromatography technologies | MI:0071- molecular sieving;14724280;10.03.01.03,16.03.01,32.01.09,70.10;"ATR and ATRIP associate with chromatin in vivo, and they exist as a large molecular weight complex that can bind single-stranded (ss)DNA cellulose in vitro. Neither ATR nor ATRIP are able to bind DNA individually, nor do they bind DNA in a cooperative manner.";"";""
266;RAD17-RFC complex;;Human;O75943,P35250,P40938,P35249,P40937;5884,5982,5983,5984,5985;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;11572977;01.04,10.03.01.03,16.03.01,16.19.03,32.01.09,70.10;"RFCp38 is necessary for the association of RAD17 with the core complex RFCp36-p37-p40 to form the RAD17-RFC complex. The ATPase activity of RAD17-RFC complex is stimulated by DNA.";"";""
267;Checkpoint 9-1-1 complex;;Human;O60921,O60671,Q99638;3364,5810,5883;MI:0004- affinity chromatography technologies;11572977;10.01.05.01,10.03.01.03,32.01.09,70.10;"";"";""
268;Checkpoint Rad complex; RAD17-RFC-9-1-1 complex;Human;O60921,O60671,O75943,Q99638,P35250,P40938,P35249,P40937;3364,5810,5884,5883,5982,5983,5984,5985;MI:0004- affinity chromatography technologies | MI:0071- molecular sieving;11572977;10.03.01.03,32.01.09,70.10;"Checkpoint Rad complex has been detected in an in vitro system.";"";""
270;RAD17-RFC complex;;Human;O75943,P35250,P40938,P35249,P40937;5884,5982,5983,5984,5985;MI:0004- affinity chromatography technologies | MI:0040- electron microscopy;11907025;01.04,10.03.01.03,16.03.01,16.19.03,32.01.09,70.10;"RAD17 makes a heteropentameric complex with the four RFC subunits with a deep groove or cleft and is similar to the RFC clamp loader.";"";""
271;Checkpoint 9-1-1 complex;;Human;O60921,O60671,Q99638;3364,5810,5883;MI:0004- affinity chromatography technologies | MI:0040- electron microscopy;11907025;10.01.05.01,10.03.01.03,32.01.09,70.10;"The checkpoint 9-1-1 complex makes a trimeric ring structure reminiscent of the PCNA ring.";"";""
272;Dysbindin-pallidin-muted-beta-dystrobrevin complex;;Mouse;O70585,Q91WZ8,Q8R015,Q9R0C0;13528,94245,17828,18457;MI:0019- coimmunoprecipitation;12923531;42.25;"";"Dtnbp1 is involved in Hermansky-Pudlak syndrome type 7 (HPS-7).";""
274;RAD17-RFC-9-1-1 checkpoint supercomplex;;Human;O60921,O60671,O75943,Q99638,P35250,P40938,P35249,P40937;3364,5810,5884,5883,5982,5983,5984,5985;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients | MI:0040- electron microscopy;12578958;10.03.01.03,16.03.01,32.01.09,70.10;"Rad17-RFC complex binds to nicked circular, gapped and primed DNA and recruits the 9-1-1 complex in an ATP-dependent manner. The interaction is mediated mainly by binding of Rad9 to Rad17.";"";""
275;Checkpoint 9-1-1 complex;;Human;O60921,O60671,Q99638;3364,5810,5883;MI:0071- molecular sieving;11340080;10.01.05.01,10.03.01.03,32.01.09,70.10;"";"";""
276;Checkpoint 9-1-1 complex;;Human;O60921,O60671,Q99638;3364,5810,5883;MI:0006- anti bait coimmunoprecipitation;9872989;10.01.05.01,10.03.01.03,32.01.09,70.10;"";"";""
277;RFC complex;;Human;P35251,P35250,P40938,P35249,P40937;5981,5982,5983,5984,5985;MI:0006- anti bait coimmunoprecipitation;8692848;01.04,10.01.03,16.03.01,16.19.03,70.10;"The subunits of the RFC complex have been reconstituted in an in vitro experiment. The Rfc complex works as a clamp loader.";"";""
278;RFC core complex;;Human;P35250,P35249,P40937;5982,5984,5985;MI:0006- anti bait coimmunoprecipitation;8692848;01.04,10.01.03,16.03.01,16.19.03,70.10;"The subunits of the RFC complex have been reconstituted in an in vitro experiment.";"";""
279;RFC complex (activator A 1 complex);;Human;P35251,P35250,P40938,P35249,P40937;5981,5982,5983,5984,5985;MI:0029- cosedimentation through density gradients;1670772;01.04,10.01.03,16.03.01,16.19.03,70.10;"Activator 1 (A1) is a multiprotein complex which is essential for proliferating cell nuclear antigen (PCNA)-dependent DNA polymerase delta (pol delta) activity and efficient in vitro DNA synthesis in the SV40 dipolymerase replication system (PMID:1670772).";"";""
280;HMGB1-HMGB2-HSC70-ERP60-GAPDH complex;;Human;P04406,P09429,P26583,P11142,P30101;2597,3146,3148,3312,2923;MI:0413- electrophoretic mobility shift assay;12517784;10.01.05.01,16.03.01,32.01.09,70.10;"The protein/DNA complex was isolated from human leukemia cells deficient in components of the mismatch repair system (Nalm6). This complex detects changes in DNA structure caused by incorporation of nonnatural nucleosides and is a determinant of cell sensitivity to such DNA modifying chemotherapy. The authors show that murine fibroblasts deficient in one component of the complex, Hmgb1, are 10-fold more resistant to thiopurine treatment than their wild-type counterparts.";"";""
281;NELF complex (Negative elongation factor complex);;Human;Q8WX92,P18615,Q8IXH7,Q9H3P2;25920,7936,51497,7469;MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients | MI:0071- molecular sieving;10199401;11.02.03.01.04,11.02.03.04.03,16.03.03,18.01.07,18.02.09,70.10;"NELF cooperates with DSIF and strongly represses POLII elongation.";"";""
282;SNF2h-cohesin-NuRD complex; ISWI (SNF2h)-containing chromatin remodeling complex;Human;Q9NRL2,Q12873,Q13547,Q92769,Q9UBB5,O95983,Q13330,O94776,O60216,Q09028,Q16576,O60264,Q14683,Q9UQE7,Q8WVM7,Q8N3U4;11177,1107,3065,3066,8932,53615,9112,9219,5885,5928,5931,8467,8243,9126,10274,10735;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;12198550;10.01.09.05,16.03.01,42.10.03,70.10.03;"The association of the complex with chromatin can be regulated by the state of DNA methylation.";"";""
283;Sin3 complex; Histone deacetylase complex;Human;Q13547,Q92769,Q09028,Q16576,O00422,O75446,Q96ST3;3065,3066,5928,5931,10284,8819,25942;MI:0004- affinity chromatography technologies;9651585;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03;"";"";""
284;CRSP complex; Cofactor required for Sp1;Human;Q15648,O60244,Q96RN5,Q9NVC6,Q13503,Q9ULK4,O75448,Q71SY5,O95402,O75586,O43513;5469,9282,51586,9440,9412,9439,9862,81857,9441,10001,9443;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;11834832;11.02.03.04.01,16.01,70.10.03;"The activator-recruited cofactor ARC consists of the two distinct multisubunit complexes ARC-L and CRSP. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"Information about four small protein subunits of the protein complex was not available in the article."
285;PCNA-MLH1-PMS1 complex;;Human;P40692,P12004,P54277;4292,5111,5378;MI:0107- surface plasmon resonance;16303135;10.01.03,10.01.05.01,70.10;"The authors show that PCNA interacts with MSH2-MSH6 with a higher affinity than with MLH1-PMS1. PCNA acts as a scaffold for consecutive protein-protein interactions.";"";""
286;PCNA-MSH2-MSH6 complex;;Human;P43246,P52701,P12004;4436,2956,5111;MI:0107- surface plasmon resonance;16303135;10.01.03,10.01.05.01,70.10;"The authors show that PCNA interacts with MSH2-MSH6 with a higher affinity than with MLH1-PMS1.";"";""
287;ARC-L complex;;Human;P24863,P49336,Q15648,Q93074,Q9UHV7,O60244,Q96RN5,Q9NVC6,Q13503,Q9ULK4,O75448,Q71SY5,O75586,O43513;892,1024,5469,9968,9969,9282,51586,9440,9412,9439,9862,81857,10001,9443;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;11834832;16.01,18.01.07,18.02.09,70.10.03;"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. The activator-recruited cofactor ARC consists of the two distinct multisubunit complexes ARC-L and CRSP- Information about four small components of the protein complex is not available in the article. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
288;ARC complex; activator-recruited cofactor;Human;P24863,P49336,Q15648,Q93074,Q9UHV7,O60244,Q96RN5,Q9NVC6,Q13503,Q9ULK4,O75448,Q71SY5,O95402,O75586,O43513;892,1024,5469,9968,9969,9282,51586,9440,9412,9439,9862,81857,9441,10001,9443;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;11834832;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10.03;"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. The activator-recruited cofactor ARC consists of the two distinct multisubunit complexes ARC-L and CRSP. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"Information about four small components of the protein complex is not available in the article."
289;PCNA-MSH2-MSH6 complex;;Human;P43246,P52701,P12004;4436,2956,5111;MI:0096- pull down | MI:0004- affinity chromatography technologies;11005803;10.01.05.01,70.10;"PCNA binds to MSH2-MSH6 complex.";"";""
290;MSH2-MLH1-PMS2-PCNA DNA-repair initiation complex;;Human;P40692,P43246,P12004,P54278;4292,4436,5111,5395;MI:0006- anti bait coimmunoprecipitation;9469823;10.01.05.01,16.03.01,32.01.09,70.10;"Formation of the initiation complex is ATP-dependent.";"";""
291;MSH2-MLH1-PMS2 DNA-repair initiation complex;;Human;P40692,P43246,P54278;4292,4436,5395;MI:0006- anti bait coimmunoprecipitation;9469823;10.01.05.01,16.03.01,70.10;"Formation of the initiation complex is ATP-dependent.";"";""
292;MutL-alpha complex; MLH1-PMS2 complex;Human;P40692,P54278;4292,5395;MI:0029- cosedimentation through density gradients;7892206;10.01.05.01,16.03.01,32.01.09,70.10;"";"";""
293;PCNA-DNA polymerase delta complex;;Mouse;P17918,P52431,O35654,Q9EQ28,Q9CWP8;18538,18971,18972,67967,69745;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;10219083;10.01.03,10.01.05.01,70.10;"Pold4 (=p66) is not absolutely necessary for polymerase activity.";"";""
294;DNA polymerase delta complex;;Mouse;P52431,O35654,Q9EQ28,Q9CWP8;18971,18972,67967,69745;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;10219083;10.01.03,70.10;"Pold4 (=p66) is not absolutely necessary for polymerase activity.";"";""
295;PCNA-DNA ligase complex;;Mouse;P37913,P17918,O35654,Q9EQ28;16881,18538,18972,67967;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;10219083;10.01.03,10.01.05.01,70.10;"";"";""
296;Pcna-Msh2-Msh6 complex;;Mouse;P43247,P54276,P17918;17685,17688,18538;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;10219083;10.01.05.01,70.10;"";"";""
297;PCNA-DNA polymerase delta complex;;Human;P12004,P28340,P49005,Q15054,Q9HCU8;5111,5424,5425,10714,57804;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;11328591;10.01.03,10.01.05.01,70.10;"PPLD3 stabilizes the polymerase delta complex and increases the affinity of polymerase delta for PCNA.";"";""
298;VEGF transcriptional complex;;Human;P27695,Q16665,P40763,(Q99966,Q99967,Q96RK1);328,3091,6774,(4435,10370,163732);MI:0019- coimmunoprecipitation;15735682;11.02.03.04,70.10;"";"This complex regulates Src-dependent hypoxia-induced expression of VEGF in pancreatic and prostate carcinomas.";""
299;IRF3-CBP complex;;Human;Q14653,(Q99966,Q99967,Q96RK1);3661,(4435,10370,163732);MI:0114- x-ray crystallography | MI:0019- coimmunoprecipitation;16154084;11.02.03.04,18.02.09;"The crystal structure of IRF-3 in complex with CBP reveals that CBP interacts with a hydrophobic surface on IRF-3, which in latent IRF-3 is covered by its autoinhibitory elements.";"";""
300;PC2 complex;;Human;Q9BTT4,O60244,Q9Y2X0,Q9NVC6,Q9H944,Q13503,O75448,Q6P2C8,Q9Y3C7,O75586,O43513,Q9Y2W1;84246,9282,10025,9440,9477,9412,9862,9442,51003,10001,9443,9967;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;10882111;11.02.03.04.01,16.01,70.10;"According to the authors, PC2 is a submodule of TRAP/SMCC. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
301;SMCC complex;SRB/MED-containing cofactor complex;Human;P24863,P49336,Q15648,Q9BTT4,Q93074,Q9UHV7,O60244,Q9Y2X0,Q9NVC6,Q9H944,Q13503,O75448,Q6P2C8,Q9Y3C7,O75586,O43513,Q9Y2W1;892,1024,5469,84246,9968,9969,9282,10025,9440,9477,9412,9862,9442,51003,10001,9443,9967;MI:0007- anti tag coimmunoprecipitation;10882111;11.02.03.04,16.01,70.10;"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
302;INO80 chromatin remodeling complex; INO80 complex;Human;O96019,Q9H9F9,Q9H981,Q6PI98,Q8NBZ0,Q53TQ3,Q9ULG1,Q96EZ8,Q6P4R8,Q9Y265,Q9Y230,P15923,Q9C086;86,79913,93973,125476,283899,54891,54617,10445,4798,8607,10856,6929,83444;MI:0007- anti tag coimmunoprecipitation;16230350;10.01.09.05,16.03.01,16.19.03,42.10.03,70.10.03;"INO80 complex exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding.";"";""
304;SRCAP-associated chromatin remodeling complex;;Human;O96019,Q9GZN1,Q96CJ1,P0C0S5,Q9Y265,Q9Y230,Q6ZRS2,Q15906,O95619,O43257;86,64431,55840,3015,8607,10856,10847,6944,8089,10467;MI:0007- anti tag coimmunoprecipitation;15647280;10.01.09.05,11.02.03.04.01,42.10.03,70.10;"";"";""
305;40S ribosomal subunit, cytoplasmic; small ribosomal subunit, cytoplasmic;Human;P62861,P46783,P62280,P25398,P62277,P62263,P62841,P62244,P62249,P08708,P62269,P39019,P15880,P60866,P63220,P62266,P62847,P62851,P62854,P42677,P62979,P62857,P62273,P23396,P61247,P62701,P46782,P62753,P62081,P62241,P46781,P08865,(P22090,Q8TD47);2197,6204,6205,6206,6207,6208,6209,6210,6217,6218,6222,6223,6187,6224,6227,6228,6229,6230,6231,6232,6233,6234,6235,6188,6189,6191,6193,6194,6201,6202,6203,3921,(6192,140032);MI:0363- inferred by author;14681386;12,70.03;"";"";""
306;Ribosome, cytoplasmic;;Human;P62861,P27635,P62906,P62913,P30050,P26373,P40429,P50914,P61313,P18621,Q07020,Q02543,P84098,P46778,P35268,P62829,P62750,P83731,P61254,P61353,P46776,P46779,P47914,P39023,P62888,P62899,P62910,P49207,P42766,P18077,Q9Y3U8,P83881,P61927,P61513,P63173,P62891,P36578,P62945,P46777,Q02878,P18124,P62424,P62917,P32969,P05388,P05386,P05387,P46783,P62280,P25398,P62277,P62263,P62841,P62244,P62249,P08708,P62269,P39019,P15880,P60866,P63220,P62266,P62847,P62851,P62854,P42677,P62979,P62857,P62273,P23396,P61247,P62701,P46782,P62753,P62081,P62241,P46781,P08865,P62987,(P22090,Q8TD47);2197,6134,4736,6135,6136,6137,23521,9045,6138,6139,6141,6142,6143,6144,6146,9349,6147,6152,6154,6155,6157,6158,6159,6122,6156,6160,6161,6164,11224,6165,25873,6173,6167,6168,6169,6170,6124,6171,6125,6128,6129,6130,6132,6133,6175,6176,6181,6204,6205,6206,6207,6208,6209,6210,6217,6218,6222,6223,6187,6224,6227,6228,6229,6230,6231,6232,6233,6234,6235,6188,6189,6191,6193,6194,6201,6202,6203,3921,7311,(6192,140032);MI:0363- inferred by author;14681386;12,70.03;"";"";""
307;Epithelial utrophin-associated protein complex;;Mammalia;O70585,Q61235,O08614;13528,20650,22288;MI:0019- coimmunoprecipitation;10209032;70.02,75.03.09;"The complex is restricted to the basolateral cell surface of epithelial cells. The authors suggest that this complex in the MDCK cell line may be involved in the generation or maintenance of cell polarity and the formation of signaling complexes in epithelia.";"";""
308;60S ribosomal subunit, cytoplasmic; large ribosomal subunit, cytoplasmic;Human;P27635,P62906,P62913,P30050,P26373,P40429,P50914,P61313,P18621,Q07020,Q02543,P84098,P46778,P35268,P62829,P62750,P83731,P61254,P61353,P46776,P46779,P47914,P39023,P62888,P62899,P62910,P49207,P42766,P18077,Q9Y3U8,P83881,P61927,P61513,P63173,P62891,P36578,P62945,P46777,Q02878,P18124,P62424,P62917,P32969,P05388,P05386,P05387,P62987;6134,4736,6135,6136,6137,23521,9045,6138,6139,6141,6142,6143,6144,6146,9349,6147,6152,6154,6155,6157,6158,6159,6122,6156,6160,6161,6164,11224,6165,25873,6173,6167,6168,6169,6170,6124,6171,6125,6128,6129,6130,6132,6133,6175,6176,6181,7311;MI:0363- inferred by author;14681386;12,70.03;"";"";""
309;RC complex;;Bovine;P33609,Q58D13,P28339,P49004,P20664,P33610,P35601,Q9WUK4,Q2TBV1,Q3UI84,Q9D0F6;18968,514793,281990,281991,19075,19076,19687,19718,515602,106344,72151;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving | MI:0226- ion exchange chromatography;8639537;10.01.03.03,10.01.03.05,16.03.01,70.10;"ATP is required for the stability of the RC complex. PCNA is required to stabilize the RC complex to a DNA primer-end.";"";"Since several bovine proteins were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were taken."
310;Cell cycle kinase complex CDC2;;Human;P14635,O95067,P24385,P06493,P38936,P12004;891,9133,595,983,1026,5111;MI:0006- anti bait coimmunoprecipitation;7903056;10.03.01.01;"";"";""
311;Cell cycle kinase complex CDK2;;Human;P24385,P24941,P38936,P12004;595,1017,1026,5111;MI:0006- anti bait coimmunoprecipitation;7903056;10.03.01.01;"";"";""
312;Cell cycle kinase complex CDK4;;Human;P24385,P11802,P38936,P12004;595,1019,1026,5111;MI:0006- anti bait coimmunoprecipitation;7903056;10.03.01.01;"";"";""
313;Cell cycle kinase complex CDK5;;Human;P24385,P30281,Q00535,P38936,P12004;595,896,1020,1026,5111;MI:0006- anti bait coimmunoprecipitation;7903056;10.03.01.01,14.07.03;"";"";""
314;PCNA-p21 complex;;Human;P38936,P12004;1026,5111;MI:0114- x-ray crystallography;8861913;10.03.01.03,70.10;"";"";""
315;28S ribosomal subunit, mitochondrial; Small ribosomal subunit, mitochondrial;Human;P51398,P82664,P82912,O15235,O60783,P82914,Q9Y3D3,Q9Y2R5,Q9NVS2,Q9Y676,Q9Y3D5,Q9Y399,P82921,P82650,Q9Y3D9,Q96EL2,P82663,Q9BYN8,Q92552,Q9Y2Q9,Q9NP92,Q92665,Q9Y291,P82930,P82673,P82909,P82675,P82932,Q9Y2R9,P82933;7818,55173,64963,6183,63931,64960,51021,51373,55168,28973,51023,51116,54460,56945,51649,64951,64432,64949,23107,28957,10884,10240,51650,65993,60488,92259,64969,64968,51081,64965;MI:0363- inferred by author;14681386;12,70.16.07;"With the exception of MRPS12, all proteins of the small ribosomal subunit from ribosomes of Bos taurus were identified in a proteomic approach (PMID:11279123).";"";""
316;Dystrophin associated complex DPC (Dmd, Dtnb), brain-derived;;Rat;P84060,(Q7TPH2,Q7TPH3,Q7TPH4);362715,(24907,24907,24907);MI:0019- coimmunoprecipitation;10545507;34.03.01,42.06,77.03.01.01.01;"The authors demonstrate that beta-dystrobrevin is part of a neuronal DPC-like complex and suggest that it may be involved in the compound phenotype of cognitive dysfunction in DMD patients.";"Dmd is involved in DUCHENNE muscular dystrophy (DMD).";""
317;Brain-derived dystrobrevin-syntrophin complex;;Mouse;P11531,Q9D2N4,O70585,(Q61234,Q99L88,Q61235,Q925E1,Q925E0);13405,13527,13528,(20648,20649,20650,71096,268534);MI:0019- coimmunoprecipitation;10545507;34.03.01,36.25.03,70.02,77.03.01.01.01;"";"";"The mouse dystrophin was described as Dp71, the authors differentiate between alpha-dystrobrevin 1 and alpha-dystrobrevin 2."
318;Muscle-derived dystrobrevin-syntrophin complex;;Mouse;Q9D2N4,(Q61234,Q99L88,Q61235,Q925E1,Q925E0);13527,(20648,20649,20650,71096,268534);MI:0019- coimmunoprecipitation;10545507;36.25.09,75.03.12;"";"";"The authors differentiate between alpha-dystrobrevin 1 and alpha-dystrobrevin 2."
320;55S ribosome, mitochondrial;;Human;P51398,P83111,Q9BYD6,Q7Z7H8,Q9Y3B7,P52815,Q9BYD1,Q6P1L8,Q9P015,Q9NX20,Q9NRX2,Q9H0U6,P49406,Q5T653,Q9BYC9,Q7Z2W9,Q9NWU5,Q16540,Q96A35,Q9P0M9,Q13084,P09001,Q8TCC3,Q9BYC8,O75394,Q9BQ48,Q9NZE8,Q9P0J6,Q9BZE1,Q96DV4,Q9NYK5,Q9BYD3,Q9NQ50,Q8IXM3,Q6FID1,Q8N983,Q9H9J2,Q9BRJ2,Q9H2W6,Q9HD33,Q96GC5,Q13405,Q8N5N7,Q4U2R6,Q86TS9,Q96EL3,Q6P161,Q7Z7F7,Q9BYD2,P82664,P82912,O15235,O60783,P82914,Q9Y3D3,Q9Y2R5,Q9NVS2,Q9Y676,Q9Y3D5,Q9Y399,P82921,P82650,Q9Y3D9,Q96EL2,P82663,Q9BYN8,Q92552,Q9Y2Q9,Q9NP92,Q92665,Q9Y291,P82930,P82673,P82909,P82675,P82932,Q9Y2R9,P82933;7818,114294,65008,124995,65003,6182,28998,64928,29088,54948,63875,29074,9801,51069,55052,219927,29093,6150,79590,51264,10573,11222,51263,64983,9553,64981,51318,64979,51253,64978,54148,51073,64976,64975,28977,84545,65080,84311,26589,57129,51642,740,54534,51258,122704,116540,116541,128308,65005,55173,64963,6183,63931,64960,51021,51373,55168,28973,51023,51116,54460,56945,51649,64951,64432,64949,23107,28957,10884,10240,51650,65993,60488,92259,64969,64968,51081,64965;MI:0363- inferred by author;14681386;12,70.16.07;"";"";""
321;p27-cyclinD2-Cdk4 complex;;Mammalia;P30280,P30285,P46529;12444,12567,0;MI:0006- anti bait coimmunoprecipitation;9325318;10.03.01.02,18.02,70.10;"p27 inhibits kinase activity of cyclinD2-CDK4.";"";"Since Ccnd2 and Cdk4 from mink were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were taken."
322;DNA-PK-Ku complex; DNA-PK-Ku70-Ku80 complex;Human;P78527,P13010,P12956;5591,7520,2547;MI:0040- electron microscopy | MI:0029- cosedimentation through density gradients;16713581;11.02.03,14.07.03,16.03.01,18.01.01,18.02.01.01,70.10;"For assembly of the DNA-PK-Ku70-Ku80 complex presence of DNA is necessary. DNA-bound Ku directs the recruitment of the catalytic subunit DNA-Pk via a small helical domain at the C-terminus of Ku80.";"";""
323;28S ribosomal subunit, mitochondrial; Small ribosomal subunit, mitochondrial;Bovine;P82922,P82670,P82911,Q6B860,P82913,P82915,P82916,P82919,P82918,P82917,P82923,P82920,P82649,Q2NL27,Q2M2T7,P82669,Q3SZ86,Q32PI8,P82928,P82924,P82925,P82927,P82926,P82929,Q2YDF6,P82908,Q2KID9,P82931,Q3T040,Q58DQ5;504320,515885,509816,445421,0,510899,508143,614102,510824,613561,505681,614343,532044,515228,617466,533011,516004,514740,535290,516084,534185,614148,523435,618357,513438,613835,512469,615431,509115,519302;MI:0028- cosedimentation in solution | MI:0029- cosedimentation through density gradients;11279123;12,70.16.07;"";"";"MRPS12 could not be identified in this study."
324;39S ribosomal subunit, mitochondrial; Large ribosomal subunit, mitochondrial;Human;P83111,Q9BYD6,Q7Z7H8,Q9Y3B7,P52815,Q9BYD1,Q6P1L8,Q9P015,Q9NX20,Q9NRX2,Q9H0U6,P49406,Q5T653,Q9BYC9,Q7Z2W9,Q9NWU5,Q16540,Q96A35,Q9P0M9,Q13084,P09001,Q8TCC3,Q9BYC8,O75394,Q9BQ48,Q9NZE8,Q9P0J6,Q9BZE1,Q96DV4,Q9NYK5,Q9BYD3,Q9NQ50,Q8IXM3,Q6FID1,Q8N983,Q9H9J2,Q9BRJ2,Q9H2W6,Q9HD33,Q96GC5,Q13405,Q8N5N7,Q4U2R6,Q86TS9,Q96EL3,Q6P161,Q7Z7F7,Q9BYD2;114294,65008,124995,65003,6182,28998,64928,29088,54948,63875,29074,9801,51069,55052,219927,29093,6150,79590,51264,10573,11222,51263,64983,9553,64981,51318,64979,51253,64978,54148,51073,64976,64975,28977,84545,65080,84311,26589,57129,51642,740,54534,51258,122704,116540,116541,128308,65005;MI:0363- inferred by author;14681386;12,70.16.07;"With the exception of MRPL36 and MRPL42, all proteins of the large ribosomal subunit from ribosomes of Bos taurus were identified in a proteomic approach (PMID:11551941). ";"";"At the time of annotation, about half of the bovine subunits were not found in the UniProt database."
325;Skeletal muscle sarcoglycan complex SGC, beta-gamma-delta-zeta;;Mouse;P82349,P82347,P82348,Q8BX51;24051,24052,24053,244431;MI:0019- coimmunoprecipitation;12189167;36.25.09.03,45.03.12.01,75.03.12.01;"The authors demonstrate that zeta-sarcoglycan is an integral component of the sarcoglycan complex and, as such, is important in the pathogenesis of muscular dystrophy.";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
326;Smooth muscle sarcoglycan complex SGC, beta-delta-zeta;;Mouse;P82349,P82347,Q8BX51;24051,24052,244431;MI:0019- coimmunoprecipitation;12189167;36.25.09.01,45.03.12.02,70.02,75.03.12.02;"The authors demonstrate that zeta-sarcoglycan was found as a component of the vascular smooth muscle sarcoglycan complex. They propose that vasospasm, as it occurs in sarcoglycan-deficient muscle, may not be related to disruption of the vascular smooth muscle sarcoglycan complex.";"";""
328;Ku antigen complex; Ku70-Ku80 complex | Ku complex;Human;P13010,P12956;7520,2547;MI:0029- cosedimentation through density gradients | MI:0091- chromatography technologies;16713581;10.01.05.01,16.03.01,32.01.09,70.10;"In the absence of added DNA Ku70-Ku80 copurify without DNA-PKcs.";"";""
329;Skeletal muscle sarcoglycan complex SGC, alpha-beta-gamma-delta;;Mouse;P82350,P82349,P82347,P82348;20391,24051,24052,24053;MI:0019- coimmunoprecipitation;10862711;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"The authors show that mice lacking delta-sarcoglycan developed muscular dystrophy and cardiomyopathy similar to mice lacking gamma-sarcoglycan. ";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
330;PSF-p54(nrb) complex;;Human;Q15233,P23246;4841,6421;MI:0091- chromatography technologies;15590677;10.01.05.01,16.01,16.03.01,32.01.09,70.10;"PSF-p54(nrb) complex probably works as a dimeric complex.";"";""
331;MRN complex (MRE11-RAD50-NBN complex);;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0091- chromatography technologies;12917393;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"";"";""
332;Skeletal muscle sarcoglycan complex SGC, alpha-beta-epsilon-gamma;;Mouse;P82350,P82349,O70258,P82348;20391,24051,20392,24053;MI:0019- coimmunoprecipitation;10608889;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"Mutations in any of the four genes encoding sarcoglycans cause a deficiency in all sarcoglycans in the sarcolemma and produce one of four types of limb-girdle muscular dystrophy.";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
5856;AK2-FADD-caspase-10 (AFAC10) complex;;Human;P54819,Q92851,Q13158;204,843,8772;MI:0096- pull down | MI:0071- molecular sieving;17952061;40.10.02.03.02;"AFAC10 complexes are detected in cells undergoing intrinsic cell death and AK2 promotes the association of caspase-10 with FADD. AK2 mediates a novel intrinsic apoptotic pathway that may be involved in tumorigenesis.";"";""
333;Skeletal muscle sarcoglycan complex SGC, alpha-beta-gamma-delta;;Mouse;P82350,P82349,P82347,P82348;20391,24051,24052,24053;MI:0019- coimmunoprecipitation;10608889;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"Complex also isolated in C2C12 cells- epsilon-sarcoglycan was undetectable in anti-alpha-sarcoglycan isolates and vice versa. Mutations in any of the four genes encoding sarcoglycans cause a deficiency in all sarcoglycans in the sarcolemma and produce one of four types of limb-girdle muscular dystrophy.";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
334;Skeletal muscle sarcoglycan complex SGC, epsilon-beta-gamma-delta;;Mouse;P82349,P82347,O70258,P82348;24051,24052,20392,24053;MI:0019- coimmunoprecipitation;10608889;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"Complex also isolated in C2C12 cells- epsilon-sarcoglycan was undetectable in anti-alpha-sarcoglycan isolates and vice versa. Mutations in any of the four genes encoding sarcoglycans cause a deficiency in all sarcoglycans in the sarcolemma and produce one of four types of limb-girdle muscular dystrophy.";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
335;p54(nrb)-PSF-matrin3 complex;;Human;P43243,Q15233,P23246;9782,4841,6421;MI:0030- cross-linking studies;11525732;16.03.03,20.01.21,70.10;"This complex binds specifically to inosine-containing RNAs and anchors hyperedited RNAs to the nuclear matrix.";"";""
336;DNA ligase IV-XRCC4-AHNK complex; AHNAK-LX complex;Human;Q09666,P49917,Q13426;79026,3981,7518;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;15177040;10.01.05.01,10.01.05.03.03,16.03.01,70.10;"AHNAK stimulates the double-stranded ligation activity of DNA ligase IV-XRCC4 complex.";"";""
337;Dystrophin-sarcoglycan-syntrophin complex, skeletal muscle;;Mouse;P11531,P82350,P82349,P82347,P82348,(Q61234,Q99L88,Q61235,Q925E1,Q925E0);13405,20391,24051,24052,24053,(20648,20649,20650,71096,268534);MI:0019- coimmunoprecipitation;9864373;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"The authors show  that delta -sarcoglycan can be cross-linked to the dystroglycan complex and of the four sarcoglycans, only beta -, gamma -, and delta -sarcoglycan contain intramolecular disulfide bonds.";"DMD, SGCB, SGCG and SGCD are involved in muscular dystrophy  and cardiomyopathy (PMID:15117830).";""
338;40S ribosomal subunit, cytoplasmic; small ribosomal subunit, cytoplasmic;Human;P62861,P46783,P62280,P25398,P62277,P62263,P62841,P62244,P62249,P08708,P62269,P39019,P15880,P60866,P63220,P62266,P62847,P62851,P62854,P62979,P62857,P62273,P23396,P61247,P62701,P46782,P62753,P62081,P62241,P46781,P08865;2197,6204,6205,6206,6207,6208,6209,6210,6217,6218,6222,6223,6187,6224,6227,6228,6229,6230,6231,6233,6234,6235,6188,6189,6191,6193,6194,6201,6202,6203,3921;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;15883184;12,70.03;"";"";"RPS27 was not detected in this study. RPS4Y1 and RPSY2 could not be detected, since HeLa cells were used, which contain no Y chromosome."
339;Smooth muscle dystroglycan complex;;Rabbit;Q28646,Q28685,Q28635,P82347,O70258,P82352,O08614;100009214,100009278,100009208,24052,20392,100008714,22288;MI:0029- cosedimentation through density gradients;10473626;36.25.09.01,45.03.12.02,70.02,75.03.12.02,77.03.09.01;"The authors demonstrate that the presence of the sarcoglycans and sarcospan in lung reflects association with dystroglycan in the smooth muscle within lung, and they show that epithelial dystroglycan is not associated with any of the known sarcoglycans and can be separated from the smooth muscle dystroglycan complex.";"DAG1, SGCB, SGCG and SGCD are involved in muscular dystrophy (Duchenne muscular dystrophy DMD, the milder Becker muscular dystrophy BMD) and cardiomyopathy (PMID:15117830).";"Since Sgce, Sgcd and Utrn from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
340;Dystrophin-glycoprotein complex DGC, skeletal muscle;;Rabbit;Q28646,Q28685,P11531,Q28686,Q28635,P82347,Q28626,P82352;100009214,100009278,13405,100009178,100009208,24052,100009179,100008714;MI:0226- ion exchange chromatography;9395445;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"These proteins provide a physical connection between the extracellular matrix and the intracellular cytoskeleton of muscle cells.";"DGC complex is involved in several forms of muscular dystrophy (Duchenne muscular dystrophy DMD, the milder Becker muscular dystrophy BMD) and cardiomyopathy (PMID:15117830).";"Since Sgcd and Dmd from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
341;Dystrophin-glycoprotein complex DGC, skeletal muscle;;Rabbit;Q28646,Q28685,P11531,Q28686,Q28635,P82347,P82352;100009214,100009278,13405,100009178,100009208,24052,100008714;MI:0029- cosedimentation through density gradients;10189375;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"";"DMD, DAG1, SGCB, SGCG and SGCD are involved in muscular dystrophy (Duchenne muscular dystrophy DMD, the milder Becker muscular dystrophy BMD)  and cardiomyopathy (PMID:15117830).";"Since Sgcd and Dmd from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
342;Skeletal muscle sarcoglycan-sarcospan complex SG-SPN;;Rabbit;Q28646,Q28686,Q28635,P82347,P82352;100009214,100009178,100009208,24052,100008714;MI:0029- cosedimentation through density gradients;10189375;36.25.09.03,45.03.12.01,70.02,75.03.12.01;"The authors demonstrate that assembly of the SG subcomplex is a prerequisite for targeting SPN to the sarcolemma and that the SG- SPN subcomplex functions to stabilize alpha -dystroglycan to the muscle plasma membrane.";"SGCB, SGCG and SGCD are involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";"Since Sgcd from rabbit was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
343;Sarcoglycan-sarcospan complex SG-SPN;;Human;Q16586,Q16585,Q92629,Q13326,Q14714;6442,6443,6444,6445,8082;MI:0019- coimmunoprecipitation;10189375;36.25.09.03,45.03.12,70.02;"The authors demonstrate that assembly of the SG subcomplex is a prerequisite for targeting SPN to the sarcolemma and that the SG- SPN subcomplex functions to stabilize alpha -dystroglycan to the muscle plasma membrane.";"SGCB, SGCG and SGCD are involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
344;DNA ligase IV-XRCC4 complex (LX complex);;Human;P49917,Q13426;3981,7518;MI:0114- x-ray crystallography;11702069;10.01.05.01,10.01.05.03.03,16.03.01,70.10;"";"";""
345;DNA ligase IV-XRCC4 complex (LX complex);;Human;P49917,Q13426;3981,7518;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;9242410;10.01.05.01,10.01.05.03.03,16.03.01,70.10.03;"";"";""
346;Sarcoglycan-sarcospan-dystroglycan complex;;Mouse;Q62165,P82350,P82349,P82347,P82348,Q62147;13138,20391,24051,24052,24053,16651;MI:0091- chromatography technologies;10767327;36.25.09,45.03.12,75.03.12;"";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
347;Sarcoglycan-sarcospan-complex SG-SPN;;Mouse;P82350,P82349,P82347,P82348,Q62147;20391,24051,24052,24053,16651;MI:0091- chromatography technologies;10767327;36.25.09,45.03.12,70.02,75.03.12;"";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
348;DNA ligase IV-XRCC4 complex;;Mammalia;P49917,Q13426;3981,7518;MI:0404- comigration in non denaturing gel electrophoresis | MI:0007- anti tag coimmunoprecipitation | MI:0030- cross-linking studies | MI:0071- molecular sieving;10945980;10.01.05.01,10.01.05.03.03,16.03.01,70.10;"Cross-linking experiments suggest that an XRCC4·XRCC4 dimer interface forms the core of the tetramer, and that the DNL IV polypeptides are in contact with XRCC4 but not with one another.";"";""
349;Sarcoglycan-sarcospan-syntrophin-dystrobrevin complex;;Mouse;P82350,P82349,P82347,P82348,Q61234,Q99L88,Q62147,(Q9D2N4,O70585);20391,24051,24052,24053,20648,20649,16651,(13527,13528);MI:0091- chromatography technologies | MI:0019- coimmunoprecipitation;10767327;36.25.09,45.03.12,70.02,75.03.12;"The authors consider that the sarcoglycan-sarcospan complex is linked to the signaling protein neuronal nitric oxide synthase via alpha-syntrophin associated with dystrobrevin.";"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
350;DNA ligase IV-XRCC4-PNK complex;;Human;P49917,Q96T60,Q13426;3981,11284,7518;MI:0007- anti tag coimmunoprecipitation;15385968;10.01.05.01,70.10.03;"Interaction of PNK with XRCC4 is dependent on the phosphothreonine-binding activity of the FHA domain.";"";""
351;Spliceosome; U2-type spliceosome;Human;Q9UKV3,O60306,Q13838,O75934,Q9BRD0,P41223,Q9Y6A4,Q8WUQ7,Q9BQ61,O95400,O60508,Q99459,Q14011,Q16630,Q9NYV4,Q9BZJ0,O95232,Q8WYA6,Q9P013,Q9HCG8,Q92841,Q9BUQ8,O00571,Q9UJV9,Q7L014,P17844,Q96DF8,O43143,O60231,Q92620,Q14562,Q08211,O75937,Q15029,P38919,Q4ZG51,Q9Y5B6,O43719,O00425,Q13123,Q9ULR0,Q69YN4,Q9Y333,P62310,Q9Y4Z0,P62312,Q9UK45,P61326,P55081,Q9HCE1,Q09161,P52298,P55769,O43809,P11940,O43660,Q9UNP9,O43447,Q9Y3C6,Q13356,Q9H2H8,O15355,Q96BP3,Q99633,Q9UMS4,O43395,Q8WWY3,O43172,O75400,Q13523,O94906,Q6P2Q9,Q9UHX1,Q96T37,Q96I25,Q9NW64,P49756,Q14498,Q9Y5S9,Q15287,O43290,Q15637,Q15459,Q15428,Q12874,O75533,Q9Y3B4,Q13435,Q15393,Q15427,Q07955,Q05519,Q01130,P84103,Q08170,Q13243,Q16629,P42285,O95391,O75940,Q2TAY7,O75643,Q8WVK2,Q96DI7,P08621,P09012,P09661,P14678,P08579,P09234,P62314,P62316,P62318,P62304,P62306,P62308,Q13573,Q96T58,O15042,Q8IYB3,Q9UQ35,Q9BXP5,Q13247,Q13242,O95926,O14776,Q9UBB9,Q96FV9,Q8NI27,Q96J01,Q86V81,Q13769,Q86W42,Q6I9Y2,P62995,P83876,Q01081,P26368,Q53GS9,Q9Y2W2,Q15007,Q9HCS7,O43670;22985,9716,7919,10286,84811,8896,29105,58509,79002,10421,51362,988,1153,11052,51755,51340,51747,56259,51503,57703,10521,9416,1654,51428,9879,1655,8220,1665,8449,9785,1659,1660,22826,9343,9775,55660,94104,27336,10643,3550,57461,25962,57819,27258,25804,11157,51690,4116,4236,4343,4686,22916,4809,11051,26986,5356,10450,10465,51645,23759,53938,5496,23398,8559,27339,9129,26121,9128,55660,8899,24148,10594,22827,64783,84991,55696,58517,9584,9939,10921,9092,7536,10291,8175,10946,23451,51639,10992,23450,10262,6426,9295,6427,6428,6429,6430,6432,23517,10569,10285,55234,23020,11017,9410,6625,6626,6627,6628,6629,6631,6632,6633,6634,6635,6636,6637,22938,23013,23350,10250,23524,51593,6431,8683,25949,10915,24144,9984,57187,84321,10189,8563,79228,80145,6434,10907,7307,11338,10713,51729,9589,56949,7756;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving | MI:0069- mass spectrometry studies of complexes;12226669;11.04.03.01,16.03.03,70.10;"In eukaryotes, the removal of introns from nascent transcripts is mediated by a highly dynamic, macromolecular machine called the spliceosome.";"";""
352;DNA ligase IV-XRCC4 complex;;Human;P49917,Q13426;3981,7518;MI:0004- affinity chromatography technologies;10854421;10.01.05.01,10.01.05.03.03,16.03.01,70.10.03;"";"";""
353;DNA ligase IV-condensin complex;;Human;P49917,O95347,Q9NTJ3;3981,10592,10051;MI:0428- imaging techniques | MI:0402- chromatin immunoprecipitation assays | MI:0019- coimmunoprecipitation;12589063;10.01.05.01,10.03,70.10.03;"DNA ligase IV interacts with SMC2L1 protein.";"";""
354;DNA ligase IV-XRCC4 complex;;Human;P49917,Q13426;3981,7518;MI:0428- imaging techniques | MI:0402- chromatin immunoprecipitation assays;12589063;10.01.05.01,10.01.05.03.03,16.03.01,70.10.03;"XRCC4 and DNA ligase IV do not colocalize during mitosis.";"";""
355;DNA-PK-Ku antigen complex;;Human;P78527,P13010,P12956;5591,7520,2547;MI:0091- chromatography technologies;1465419;11.02.03,14.07.03,16.03.01,18.01.01,18.02.01.01,70.10;"Ku antigen activates DNA-PK that phosphorylates the C-terminal domain of RNA polymerase II.";"";""
356;DNA-PK-Ku antigen complex;;Human;P78527,P13010,P12956;5591,7520,2547;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;8422676;11.02.03,14.07.03,16.03.01,18.01.01,18.02.01.01,70.10;"DNA-PK is directed to the DNA by interaction with Ku antigen.";"";""
357;DNA-PK-Ku antigen complex;;Human;P78527,P13010,P12956;5591,7520,2547;MI:0029- cosedimentation through density gradients;8486698;11.02.03,14.07.03,16.03.01,18.01.01,18.02.01.01,70.10;"Ku antigen activates DNA-PK that phosphorylates the C-terminal domain of RNA polymerase II.";"";""
358;DNA ligase IV-Xrcc4-DNA-protein kinase complex;;Mouse;Q8BTF7,P97313,Q924T3;319583,19090,108138;MI:0007- anti tag coimmunoprecipitation;15194694;10.01.05.01,10.01.05.03.03,14.07.03,70.10.03;"DNA ligase IV in complex with XRCC4 can be phosphorylated by DNA-protein kinase.";"";""
359;DNA ligase IV-XRCC4-XLF complex;;Human;P49917,Q9H9Q4,Q13426;3981,79840,7518;MI:0007- anti tag coimmunoprecipitation;16439205;10.01.05.01,70.10;"";"";""
360;Artemis-DNA-PK complex;;Human;Q96SD1,P78527;64421,5591;MI:0006- anti bait coimmunoprecipitation;16857680;01.03.16.03,10.01.05.01,10.01.05.03.03,16.03.01,32.01.09,70.10;"DNA-PKcs is necessary for the loading of Artemis on damaged chromatin. Ku-mediated assembly of DNA-PK on DNA ends is responsible for a dissociation of the DNA-PKcs·Artemis complex.";"";""
361;Artemis-DNA-PK complex;;Human;Q96SD1,P78527;64421,5591;MI:0007- anti tag coimmunoprecipitation;11955432;01.03.01,10.01.05.01,10.01.05.03.03,16.03.01,32.01.09,70.10;"Upon complex formation, DNA-PKcs phosphorylates Artemis, and Artemis acquires endonucleolytic activity on 5' and 3' overhangs, as well as hairpins. Finally, the Artemis:DNA-PKcs complex can open hairpins generated by the RAG complex.";"";""
362;DNA ligase III-XRCC1-PNK-DNA-pol III multiprotein complex;;Human;P49916,Q96T60,P06746,P18887;3980,11284,5423,7515;MI:0006- anti bait coimmunoprecipitation;11163244;10.01.05.01,32.01.09,70.10;"";"";""
363;DNA ligase III-XRCC1 complex;;Human;P49916,P18887;3980,7515;MI:0004- affinity chromatography technologies;15141024;10.01.05.01,70.10;"";"";""
364;RC-1 complex (recombination complex 1);;Bovine;P97386,Q9WVF7,O54956,O97593,Q8CG48;16882,18973,18974,282370,14211;MI:0071- molecular sieving;8392064;01.03.16.03,10.01.05.01,10.01.05.03,70.10;"";"";"Since several bovine proteins were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
365;DNA ligase III-XRCC1 complex;;Human;P49916,P18887;3980,7515;MI:0071- molecular sieving;16060670;10.01.05.01,70.10;"DNA polymerase beta promotes recruitment of the XRCC1-Lig3 complex to sites of base excision repair. However Pol-beta is not stably complexed with the XRCC1-Lig3 heterodimer.";"";""
366;Rag1-Rag2 protein-DNA complex;;Mouse;P15919,P21784;19373,19374;MI:0006- anti bait coimmunoprecipitation;9094713;10.01.05.03.03,16.03.01,70.10;"Rag1 and Rag2 proteins form a stable complex only in presence of DNA.";"";""
367;Rag1-Rag2-Ku70-Ku80 protein-DNA complex;;Mouse;P63158,P15919,P21784,P27641,P23475;15289,19373,19374,22596,14375;MI:0006- anti bait coimmunoprecipitation;9094713;10.01.05.03.03,16.03.01,70.10;"A stable complex is formed only in the presence of DNA and Rag1/2.";"";""
368;ERCC1-ERCC4-MSH2 complex;;Human;P07992,Q92889,P43246;2067,2072,4436;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;14706347;01.03.16.03,10.01.05.01,32.01.09,70.10;"";"ERCC4 is involved in xeroderma pigmentosum group F.";""
369;MSH2-MSH6-PMS2-MLH1 complex; MMR complex 2;Human;P40692,P43246,P52701,P54278;4292,4436,2956,5395;MI:0031- protein cross-linking with a bifunctional reagent | MI:0006- anti bait coimmunoprecipitation;10748159;10.01.05.01,16.03.01,32.01.09,70.10;"The protein complex specifically binds to mismatched DNA. Interactions occur without addition of ATP.";"";""
370;MSH2-MSH6-PMS1-MLH1 complex; MMR complex 1;Human;P40692,P43246,P52701,P54277;4292,4436,2956,5378;MI:0031- protein cross-linking with a bifunctional reagent | MI:0006- anti bait coimmunoprecipitation;10748159;10.01.05.01,16.03.01,32.01.09,70.10;"The protein complex specifically binds to mismatched DNA. Interactions occur without addition of ATP.";"";""
371;Structure-specific endonulease complex; ERCC1-XPF complex;Mammalia;P07992,Q9QYM7;2067,0;MI:0004- affinity chromatography technologies | MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients;8797827;10.01.05.01,32.01.09,70.10;"This complex is a structure-specific endonuclease responsible for the 5' incision during repair.";"ERCC4 is involved in xeroderma pigmentosum group F.";""
372;F0F1 ATP synthase, mitochondrial;;Rat;P15999,P10719,P35435,P35434,P29418,P19511,P31399,P29419,P21571,P56135,Q03344,Q6PDU7,P05504,P11608,(Q06645,Q06646,Q71S46);65262,171374,116550,245965,245958,171375,641434,140608,94271,57423,25392,300677,26197,26196,(29754,171082,114630);MI:0028- cosedimentation in solution;10887193;01.03.01,01.04,02.45.15,16.01,70.16.05;"";"";"Since Atp5j2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
373;Vacuolar ATPase;;Bovine;P40682,P81134,Q29466,P23956,P61420,P81103,P31404,P21282,P39942,P11019,Q28029,P79251,(P31407,P31408);327687,513520,286768,550622,282148,338075,282147,338089,404152,287017,282405,281641,(338059,338082);MI:0028- cosedimentation in solution | MI:0276- blue native page;9556572;01.03.01.01,16.01,20.01.01.01,20.03.22,20.09.07,70.02;"This ATPase was isolated from bovine chromaffin granules.";"";""
374;MSH2-MSH6 complex; MutS-alpha complex;Human;P43246,P52701;4436,2956;MI:0006- anti bait coimmunoprecipitation | MI:0031- protein cross-linking with a bifunctional reagent;8942985;10.01.05.01,16.03.01,32.01.09,70.10;"";"";""
375;MSH2-MSH3 complex; MutS-beta complex;Human;P43246,P20585;4436,4437;MI:0006- anti bait coimmunoprecipitation | MI:0031- protein cross-linking with a bifunctional reagent;8942985;10.01.05.01,16.03.01,32.01.09,70.10;"";"";""
376;PCNA-MutS-alpha-MutL-alpha-DNA complex; PCNA-MSH2-MSH6-MLH1-PMS2 complex;Human;P40692,P43246,P52701,P12004,P54278;4292,4436,2956,5111,5395;MI:0031- protein cross-linking with a bifunctional reagent | MI:0019- coimmunoprecipitation;16204460;10.01.05.01,16.03.01,32.01.09,70.10;"MutS-alpha, consisting of MSH2 and MSH6 proteins, and PCNA bind to DNA to form an initial complex. MutL-alpha, consisting of MLH1 and PMS2, binds to the complex when the DNA is damaged.";"";""
377;PCNA-MutS-alpha-DNA initial complex; PCNA-MSH2-MSH6 complex;Human;P43246,P52701,P12004;4436,2956,5111;MI:0031- protein cross-linking with a bifunctional reagent | MI:0019- coimmunoprecipitation;16204460;10.01.05.01,16.03.01,70.10;"MutS-alpha, consisting of MSH2 and MSH6 proteins, and PCNA bind to DNA to form an initial complex. MutL-alpha, consisting of MLH1 and PMS2, binds to the complex when the DNA is damaged.";"";""
378;MutS-beta complex; MSH2-MSH3 complex;Human;P43246,P20585;4436,4437;MI:0019- coimmunoprecipitation;8805365;10.01.05.01,16.03.01,32.01.09,70.10;"";"";""
379;MutL-alpha complex; MLH1-PMS2 complex;Human;P40692,P54278;4292,5395;MI:0006- anti bait coimmunoprecipitation;10748105;10.01.05.01,16.03.01,32.01.09,70.10;"Normal levels of hMLH1 protein appear to be important in maintaining normal levels of hPMS1 and hPMS2 proteins, suggesting that PMS proteins are unstable in the absence of hMLH1.";"";""
380;MutL-beta complex; MLH1-PMS1 complex;Human;P40692,P54277;4292,5378;MI:0006- anti bait coimmunoprecipitation;10748105;10.01.05.01,16.03.01,32.01.09,70.10;"The results provide evidence for the association of hPMS1 with hMLH1 as a heterodimer in human epithelial cancer cells. Normal levels of hMLH1 protein appear to be important in maintaining normal levels of hPMS1 and hPMS2 proteins, suggesting that PMS proteins are unstable in the absence of hMLH1.";"";""
381;Respiratory chain complex I, mitochondrial; NADH dehydrogenase (EC 1.6.5.3);Mouse;Q91WP8,Q9MD59,Q9MD82,P03888,P03911,Q99LC3,Q7TMF3,Q9ERS2,Q9CQ75,Q9CQ91,Q62425,Q9CPP6,Q9CQZ5,Q9Z1P6,Q9DCJ5,Q9DC69,Q9CR21,Q9DCS9,O09111,Q9CQZ6,Q9CQC7,Q9CQH3,Q3UIU2,Q9CR61,Q9D6J5,Q9CQJ8,Q9CQ54,Q91VD9,Q91WD5,Q9DCT2,Q9CXZ1,Q99LY9,P52503,Q9DC70,Q8K3J1,Q91YT0,Q9D6J6;78330,17717,17721,17716,17719,67273,66414,67184,17991,66091,17992,68202,67130,66416,68375,66108,70316,68342,104130,66495,68194,66046,230075,66916,67264,66218,68197,227197,226646,68349,17993,595136,407785,75406,225887,17995,72900;MI:0029- cosedimentation through density gradients;15591592;02.11.05,02.13.03,20.01.15,70.16.05,77.03.01.01.01;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
382;Respiratory chain complex I, mitochondrial; NADH dehydrogenase (EC 1.6.5.3);Mouse;Q91WP8,Q9MD82,P03888,P03899,P03911,O35683,Q99LC3,Q9D8B4,Q7TMF3,Q9ERS2,Q9CQ75,Q9CQ91,Q62425,Q9CPP6,Q9CQZ5,Q9Z1P6,Q9DCJ5,Q9DC69,Q9CR21,Q9DCS9,O09111,Q9CPU2,Q9CQZ6,Q9CQC7,Q9CQH3,Q3UIU2,Q9CR61,Q9D6J5,Q9CQJ8,Q9CQ54,Q91VD9,Q91WD5,Q9DCT2,Q9CXZ1,Q99LY9,P52503,Q9DC70,Q8K3J1,Q91YT0,Q9D6J6;78330,17721,17716,17718,17719,54405,67273,69875,66414,67184,17991,66091,17992,68202,67130,66416,68375,66108,70316,68342,104130,68198,66495,68194,66046,230075,66916,67264,66218,68197,227197,226646,68349,17993,595136,407785,75406,225887,17995,72900;MI:0006- anti bait coimmunoprecipitation;15591592;02.11.05,02.13.03,20.01.15,70.16.05,77.03.01.01.01;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
384;Caveolar macromolecular signaling complex;;Mouse;P97490,P18762,Q01815,P51637,P63094,Q76MZ3,P31324;11514,11555,12288,12391,14683,51792,19088;MI:0006- anti bait coimmunoprecipitation;16648270;30.05.02.24,36.25.09.03,70.02,75.03.12.03;"Anti-Ca(v)1.2 used for coimmunoprecipitation. The authors didn't differentiate between the different types of adenylate cyclases, Adcy8 was chosen due to its molecular weight, complex isolated from ventricular myocytes.";"";""
385;Caveolar macromolecular signaling complex, using anti-Cav-3;;Mouse;P97490,P18762,Q01815,P51637,P63094,Q76MZ3,P31324,(Q61018,P08752,Q9DC51);11514,11555,12288,12391,14683,51792,19088,(14677,14678,14679);MI:0006- anti bait coimmunoprecipitation;16648270;30.05.02.24,36.25.09.03,70.02,75.03.12.03;"";"";"The authors didn't differentiate between the different types of adenylate cyclases, Adcy8 was chosen due to its molecular weight, complex isolated from ventricular myocytes."
386;Ubiquitin E3 ligase (UBADC1, RNF123);KPC complex |KPC1-KPC2 ubiquitin-protein ligase;Human;Q5XPI4,Q9BSL1;63891,10422;MI:0007- anti tag coimmunoprecipitation;15531880;14.07.05,14.13.01.01,16.01,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The cyclin-dependent kinase inhibitor p27(Kip1) is degraded at the G0-G1 transition of the cell cycle by the ubiquitin-proteasome pathway. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. The nuclear export of p27(Kip1) by CRM1 seems to be necessary for KPC-mediated proteolysis.";"";""
387;MCM complex;;Human;P49736,P25205,P33991,P33992,Q14566,P33993;4171,4172,4173,4174,4175,4176;MI:0226- ion exchange chromatography;8798650;10.01.02,10.01.03,16.19.03,70.10.03;"";"The MCM proteins are highly expressed in malignant human cancer cells and pre-cancerous cells undergoing malignant transformation (PMID:16101384).";""
388;Respiratory chain complex I, mitochondrial; NADH dehydrogenase (EC 1.6.5.3);Bovine;P03887,P03892,P03898,P03910,P03902,P03920,P03924,Q02377,P34942,Q8HXG6,O97725,Q95KV7,Q02370,Q02371,Q01321,P23935,Q02366,Q05752,P42029,P34943,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369,Q02376,Q02827,P15690,P17694,P23709,Q02375,Q02379,P23934,P42026,P42028,P25708,P04394,P25712;0,0,3283884,3283886,3283885,0,3283888,327673,338060,326346,281742,338084,327698,338064,327704,327714,327670,338063,327710,404188,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660,282289,338046,288380,327697,287327,327680,338057,327691,338079,287027,287014,282290,327717;MI:0227- reverse phase chromatography;12381726;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
389;ORC complex (origin recognition complex);;Human;Q13415,Q13416,Q9UBD5,O43929,O43913,Q9Y5N6;4998,4999,23595,5000,5001,23594;MI:0007- anti tag coimmunoprecipitation;16549788;10.01.03.03,16.19.03,70.10.03;"Orc6 is only weakly associated with the ORC complex.";"";""
390;Ubiquitin E3 ligase (SKP1A, FBXW2, CUL1);SCF(hFBW2) E3 complex;Human;Q13616,Q9UKT8,P63208;8454,26190,6500;MI:0007- anti tag coimmunoprecipitation;15640526;14.07.05,14.13.01.01,16.01,47.03.21.03.06,70.03;"The GCM proteins GCMa/1 and GCMb/2 are novel zinc-containing transcription factors critical for glial cell differentiation in fly and for placental as well as parathyroid gland development in mouse. Experiments identify the SCF(hFBW2) E3 complex as the key machinery that targets hGCMa to the ubiquitin-proteasome degradation system.";"";""
391;Ubiquitin E3 ligase (DDB1, CUL4A, RBX1);Ddb1-Cul4a-Roc1 complex;Human;Q13619,Q16531,P62877;8451,1642,9978;MI:0007- anti tag coimmunoprecipitation;16964240;14.07.05,16.01,32.01.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
392;Succinyl-CoA synthetase, GDP-forming; succinyl-CoA ligase;Pig;O19069,P53590;399539,397026;MI:0027- cosedimentation;8401211;01.03.01,01.05.08,16.01,16.19.05,70.16;"";"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).";""
393;Succinyl-CoA synthetase, GDP-forming;succinyl-CoA ligase;Human;P53597,Q96I99;8802,8801;MI:0027- cosedimentation;15234968;01.03.01,01.05.08,16.01,16.19.05,70.16;"";"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).";""
394;Succinyl-CoA synthetase, ADP-forming;succinyl-CoA ligase;Human;Q9P2R7,P53597;8803,8802;MI:0027- cosedimentation;15234968;01.03.01,01.05.08,16.01,16.19.03,70.16;"";"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).";""
395;Succinyl-CoA synthetase, ADP-forming;succinyl-CoA ligase;Mouse;Q9Z2I9,Q9WUM5;20916,56451;MI:0027- cosedimentation;15234968;01.03.01,01.05.08,16.01,16.19.03,70.16;"";"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).";""
396;Succinyl-CoA synthetase, GDP-forming;succinyl-CoA ligase;Mouse;Q9WUM5,Q9Z2I8;56451,20917;MI:0027- cosedimentation;15234968;01.03.01,01.05.08,16.01,16.19.05,70.16;"";"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).";""
397;Succinyl-CoA synthetase, ADP-forming;succinyl-CoA ligase;Rat;P13086,Q499V7;114597,362404;MI:0027- cosedimentation;15234968;01.03.01,01.05.08,16.01,16.19.03,70.16;"";"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).";""
398;Egasyn-glucuronidase complex;;Mouse;Q64176,P12265;13897,110006;MI:0404- comigration in non denaturing gel electrophoresis;7744842;70.07;"A region including the serpin-like sequence in the glucuronidase propeptide is essential for complex formation with egasyn and ER retention of glucuronidase.";"";""
399;Respiratory chain complex I, mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3);Bovine;P03887,P03892,P03898,P03910,P03902,P03920,P03924,Q02377,P34942,Q8HXG6,O97725,Q95KV7,Q02370,Q02371,Q01321,P23935,Q02366,Q05752,P42029,P34943,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369,Q02376,Q02827,P15690,P17694,P23709,Q02375,Q02379,P23934,P42026,P42028,P25708,P04394,P25712;0,0,3283884,3283886,3283885,0,3283888,327673,338060,326346,281742,338084,327698,338064,327704,327714,327670,338063,327710,404188,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660,282289,338046,288380,327697,287327,327680,338057,327691,338079,287027,287014,282290,327717;MI:0091- chromatography technologies | MI:0071- molecular sieving;12644575;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
400;Respiratory chain complex I (subcomplex I alpha), mitochondrial; NADH:ubiqinone dehydrogenase (EC 1.6.5.3) subcomplex I alpha;Bovine;P03924,Q02377,P34942,Q8HXG6,O97725,Q95KV7,Q02370,Q02371,P23935,Q02366,Q05752,P42029,P34943,P52505,P48305,Q02368,P15690,P17694,P23709,P23934,P42026,P42028,P25708,P04394,P25712;3283888,327673,338060,326346,281742,338084,327698,338064,327714,327670,338063,327710,404188,327702,327706,338065,288380,327697,287327,327691,338079,287027,287014,282290,327717;MI:0091- chromatography technologies | MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients;12644575;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
401;Respiratory chain complex I (subcomplex I lambda), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex I lambda;Bovine;O97725,Q95KV7,Q02370,P23935,Q05752,Q02368,P15690,P17694,P23709,P23934,P42026,P42028,P25708,P04394,P25712;281742,338084,327698,327714,338063,338065,288380,327697,287327,327691,338079,287027,287014,282290,327717;MI:0091- chromatography technologies | MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients;12644575;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Subcomplex I lambda is a fraction of subcomplex I alpha. Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
402;Respiratory chain complex I (subcomplex I beta), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex I beta;Bovine;P03910,P03920,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369;3283886,0,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660;MI:0091- chromatography technologies | MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients;12644575;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
403;Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III | Cytochrome reductase | Ubiquinol:cytochrome c oxidoreductase;Bovine;P00125,P00157,P07552,P00130,P00129,P31800,P23004,P13272,P00126,P13271;512500,3283889,281570,616109,616871,282393,282394,287020,613899,286885;MI:0114- x-ray crystallography;9651245;02.13.03,20.01.10,20.01.15,20.09.04,70.16.05,75.03.12.03;"";"";"The bovine heart mitochondrial cytochrome bc1 complex is a dimer, with each monomer consisting of 11 different subunits. Only 10 subunits are displayed, since subunit V (Rieske iron sulfur protein = P13272) contains subunit IX (=precursor of subunit V, compare PMID:8386158)."
404;Isocitrate dehydrogenase, cytoplasmic;;Human;O75874;3417;MI:0096- pull down;15173171;01.05.02,01.07.04,16.21.07,70.03,70.19;"Isocitrate dehydrogenases (IDHs) catalyze the oxidative decarboxylation of isocitrate to alpha-ketoglutarate. The isocitrate dehydrogenase complex appears as homodimer.";"";""
405;Glucosidase 2;;Rat;Q14697,P14314;23193,5589;MI:0028- cosedimentation in solution | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;8910335;14.04,14.07,16.01,70.07;"";"";"Since Ganab and Prkcsh from rat were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
406;N-acetylglucosamine-1-phosphotransferase;;Bovine;Q3T906,Q58CS8;79158,508713;MI:0071- molecular sieving | MI:0226- ion exchange chromatography | MI:0019- coimmunoprecipitation;8940155;14.04,14.07.03,16.01,70.25;"";"";"Since bovine GNPTAB was not available in the UniProt database at the time of annotation, the orthologous human protein was used."
407;Guanylyl cyclase, soluble (GUCY1A2, GUCY1B3);;Human;P33402,Q02153;2977,2983;MI:0028- cosedimentation in solution;1683630;01.03.10,16.01,70.03;"Two soluble guanylyl cyclase complexes were found in mammals.  The GUCY1A3-GUCY1B3 complex exhibits higher guanylyl cyclase activity than the GUCY1A2-GUCY1B3 complex.";"";""
408;Guanylyl cyclase, soluble (GUCY1A3, GUCY1B3);;Human;Q02108,Q02153;2982,2983;MI:0028- cosedimentation in solution;1683630;01.03.10,16.01,70.03;"Two soluble guanylyl cyclase complexes were found in mammals.  The GUCY1A3-GUCY1B3 complex exhibits higher guanylyl cyclase activity than the GUCY1A2-GUCY1B3 complex.";"";""
409;Gamma-glutamylcysteine synthetase;;Rat;P19468,P48508;25283,29739;MI:0028- cosedimentation in solution;1967255;01.01.03.02,01.01.09.03,01.03.01,16.01;"";"";""
413;(ER)-localized multiprotein complex, Ig heavy chains associated;;Mouse;Q9JLK7,Q99KV1,P08113,P20029,Q9JKR6,P09103,P08003,P24369,Q9ESP1,Q6P5E4;29867,67838,22027,14828,12282,18453,12304,19035,64136,320011;MI:0031- protein cross-linking with a bifunctional reagent | MI:0096- pull down;12475965;14.01,32.01.07,70.07;"Complex isolated in mouse lymphoma cell lines Ag8(8). The assembly of the chaperones with each other is not dependent on the presence of unassembled, unfolded heavy chains but rather that unassembled heavy chains may bind to this preformed ER chaperone network.";"";""
414;(ER)-localized multiprotein complex, in absence of Ig heavy chains;;Mouse;Q9JLK7,P08113,P20029,Q9JKR6,P09103,P08003,P24369,Q9ESP1,Q6P5E4;29867,22027,14828,12282,18453,12304,19035,64136,320011;MI:0031- protein cross-linking with a bifunctional reagent | MI:0096- pull down | MI:0019- coimmunoprecipitation;12475965;14.01,32.01.07,70.07;"The assembly of the chaperones with each other is not dependent on the presence of unassembled, unfolded heavy chains but rather that unassembled heavy chains may bind to this preformed ER chaperone network.";"";""
415;EXO1-MLH1-PMS2 complex;;Human;Q9UQ84,P40692,P54278;9156,4292,5395;MI:0006- anti bait coimmunoprecipitation;11427529;01.03.16,10.01.05.01,32.01.09,70.10;"The authors propose  the involvement of hExoI as a downstream effector in MMR (DNA mismatch repair) and/or DNA recombination.";"";""
416;Nitric oxide synthase-dystrophin complex, skeletal muscle;;Mouse;P11531,Q9Z0J4;13405,18125;MI:0004- affinity chromatography technologies | MI:0096- pull down | MI:0019- coimmunoprecipitation;7545544;30.01.09.01,36.25.09,70.02,75.03.12.01;"The authors describe that  aberrant regulation of nNOS may contribute to preferential degeneration of fast-twitch muscle fibers in DMD.";"DMD is  involved in muscular dystrophy (Duchenne muscular dystrophy).";""
417;COX-2-Cav-3 complex;;Rat;P51638,P35355;29161,29527;MI:0019- coimmunoprecipitation | MI:0096- pull down;16479074;18.02.01,70.02,73.03.19,75.03.06;"Chondrocytes were stimulated with Cd.";"";""
418;H/ACA ribonucleoprotein complex;;Rat;P40615,Q6AYA1,Q9CRB2,Q9CQS2;170944,499709,52530,66181;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;12446766;01.03.10,11.06.01,16.01,70.10.07;"NAP57, GAR1, NHP2, and NOP10, and a snoRNA were apparently sufficient for site-specific pseudouridylation of synthetic rRNA substrates. Except for physiological concentration of salt, no exogenous factors were required for catalysis. The box H/ACA snoRNPs associated with phosphorylated but not dephosphorylated Nopp140 and were active in rRNA pseudouridylation independently of their Nopp140 association.";"";"Since Nhp2 and Nop10 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
419;Farnesyltransferase;;Human;P49354,P49356;2339,2342;MI:0114- x-ray crystallography;11687658;14.07.01,16.01;"";"";""
420;SAP97-Cav-3-Kv1.5 complex;;Mammalia;P51637,Q811D0,P19024;12391,13383,25470;MI:0096- pull down;15277200;14.10,18.02.10,70.02,75.03.12.03;"The results show that a scaffolding complex containing Cav-3 and SAP97 can recruit Kv1.5 by means of multiple protein-protein interactions.";"";""
5850;p65-p65 Nf(kappa)B complex, Il-1-beta induced;;Rat;Q7TQN4;309165;MI:0412- electrophoretic mobility supershift assay;16556731;11.02.03.04.01,16.03.01,30.01.05.01.04;"The results suggest that in INS-1E (beta cell line) cells the cytokines IL-1-beta or TNF-alpha induce a complex preferentially constituted by p65 homodimers, with a minor contribution by the p65/p50 heterodimer. The results further show that cytokine induced NF(kappa)B activation in insulin-producing cells is more intense and sustained than in fibroblasts.";"In pancreatic beta cells the cytokine induced p65-p65 Nf(kappa)B complex is involved in Diabetes mellitus, type I.";""
421;SAP97-Cav-3-Kv1.5 complex;;Rat;P51638,Q62696,P19024;29161,25252,25470;MI:0019- coimmunoprecipitation;15277200;14.10,18.02.10,70.02,75.03.12.03;"The results show that a scaffolding complex containing Cav-3 and SAP97 can recruit Kv1.5 by means of multiple protein-protein interactions.";"";""
422;Beta-dystroglycan-caveolin-3 complex;;Human;P56539,Q14118;859,1605;MI:0096- pull down | MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;10988290;14.10,70.02,75.03.12;"Caveolin-3 can effectively block the interaction of dystrophin with beta -dystroglycan. ";"DAG1 is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).";""
423;EXO1-MLH1-PMS2 complex;;Human;Q9UQ84,P40692,P54278;9156,4292,5395;MI:0096- pull down;14676842;01.03.16,10.01.05.01,32.01.09,70.10;"EXO1 plays a role in events at the replication sites as well as a functional role in the DNA mismatch repair and/or recombination processes.";"";""
424;EXO1-MLH1-PCNA complex;;Human;Q9UQ84,P40692,P12004;9156,4292,5111;MI:0663- confocal microscopy;14676842;01.03.16,10.01.05.01,32.01.09,70.10;"EXO1 plays a role in events at the replication sites as well as a functional role in the DNA mismatch repair and/or recombination processes.";"";""
425;MSH4-MSH5-GPS2 complex;;Human;Q13227,O15457,O43196;2874,4438,4439;MI:0437- protein tri hybrid | MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down;16122992;10.01.05.01,10.01.05.03.01,32.01.09;"The association with GPS2 is mediated through the interface of hMSH4-hMSH5 complex and the N-terminal region of GPS2.";"";""
426;Meprin A;PABA peptide hydrolase;Human;Q16819,Q16820;4224,4225;MI:0019- coimmunoprecipitation;8262185;14.13.01,16.01,70.02;"";"";""
427;Tripeptidyl peptidase;TPPII;Mouse;Q64514;22019;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;9974389;14.13.01,70.03;"TPPII is a homomeric high molecular-weight protease with an estimated mass between 5 and 9 MD. The particle is larger than the 26S proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like endoproteolytic cleavage.";"";""
428;Molybdopterin synthase;;Human;O96007,O96033;4338,4338;MI:0071- molecular sieving;12732628;01.07.01,16.01;"Molybdenum cofactor (Moco)1 biosynthesis is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is essential for the activity of sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase in humans. MOCS2A and MOCS2B are encoded on a single bicistronic mRNA.";"Human Moco deficiency leads to the pleiotropic loss of all three of these molybdoenzymes and usually progresses to death at an early age.";""
429;Phosphatidylinositol 3-kinase complex (PIK3C3, PIK3R4);;Human;Q8NEB9,Q99570;5289,30849;MI:0019- coimmunoprecipitation;7628435;14.04,14.07.03,16.01,16.17.09,16.19.03,30.05.01,70.02;"The homologous Vps34p-Vps15p complex in yeast mediates protein trafficking.";"";""
430;18S U11/U12 snRNP;;Human;Q9BV90,Q6IEG0,O43143,Q8N8D1,Q6P2Q9,Q96LT9,O75533,Q9Y3B4,Q13435,Q15393,Q15427,Q9BWJ5,P14678,P62314,P62316,P62318,P62304,P62306,P62308,Q16560,P67809,Q8TBF4,Q9UDW3,Q15696;79622,154007,1665,10081,10594,55599,23451,51639,10992,23450,10262,83443,6628,6632,6633,6634,6635,6636,6637,11066,4904,85437,55954,8233;MI:0069- mass spectrometry studies of complexes | MI:0029- cosedimentation through density gradients;15146077;11.04.03,70.10;"U12-type spliceosomes excise U12-type introns, which comprise less than 1% of all human introns.";"";""
431;MSH2-MSH6-PMS2-MLH1 complex; MutS(alpha)-MutL(alpha)-heteroduplex complex;Human;P40692,P43246,P52701,P54278;4292,4436,2956,5395;MI:0107- surface plasmon resonance;11441019;10.01.05.01,16.03.01,16.19.03,32.01.09,70.10;"MutS-alpha-MutL-alpha-heteroduplex complex requires DNA mismatch and ATP hydrolysis.";"";""
432;N-NOS-CHIP-HSP70-1 complex;;Human;P08107,P29475,Q9UNE7;3303,4842,10273;MI:0019- coimmunoprecipitation;15466472;14.13.01.01,70.03;"Cells for analysis were treated with lactacystin, a selective inhibitor of the proteasome. The authors found that CHIP acts to ubiquitylate nNOS and that hsp70 and hsp40 can facilitate this conjugation reaction.";"";""
433;BASC complex (BRCA1-associated genome surveillance complex);;Human;Q13315,P54132,P38398,P40692,P49959,P43246,P52701,O60934,Q92878,P35251,P35250,P35249;472,641,672,4292,4361,4436,2956,4683,10111,5981,5982,5984;MI:0071- molecular sieving | MI:0226- ion exchange chromatography | MI:0019- coimmunoprecipitation;10783165;10.01.05.01,32.01.09,70.10;"The BASC complex may serve as a sensor for DNA damage. ";"BRCA1 is involved in breast cancer.";""
434;BASC (Ab 80) complex (BRCA1-associated genome surveillance complex);;Human;P54132,P38398,P40692,P43246,P52701,P35251,P35250,P35249;641,672,4292,4436,2956,5981,5982,5984;MI:0007- anti tag coimmunoprecipitation;10783165;10.01.05.01,32.01.09,70.10;"For isolation of the BASC complex (Ab 80), polyclonal antibodies against GST-BRCA1 1021-1552 were used.  ";"BRCA1 is involved in breast cancer.";""
435;BASC (Ab 81) complex (BRCA1-associated genome surveillance complex);;Human;Q13315,P38398,P40692,P35251,P35250,P35249;472,672,4292,5981,5982,5984;MI:0071- molecular sieving | MI:0226- ion exchange chromatography | MI:0019- coimmunoprecipitation;10783165;10.01.05.01,32.01.09,70.10;"For isolation of the BASC complex (Ab 81), polyclonal antibodies against GST-BRCA1 1501-1861 were used. ";"BRCA1 is involved in breast cancer.";""
436;BASC (Ab C-20) complex (BRCA1-associated genome surveillance complex);;Human;P38398,P52701,Q92878;672,2956,10111;MI:0007- anti tag coimmunoprecipitation;10783165;10.01.05.01,32.01.09,70.10;"For isolation of the BASC complex (Ab C-20), polyclonal antibodies against the carboxy-terminal epitope of BRCA1 were used. ";"BRCA1 is involved in breast cancer.";""
437;AQP2-binding multiprotein force generator complex;;Rat;Q9QXQ0,Q07936,P48037,P34080,Q68FP1,Q9EQX4,Q62812,P18666,P13832,Q7TQ08,Q6I7S1,P16086,P21107,(P60711,P63259);63836,56611,79125,25386,296654,108897,25745,50685,501203,298975,361710,64159,59069,(81822,287876);MI:0004- affinity chromatography technologies;15823548;14.04,20.03.01,34.01,70.02,77.03.07.01;"";"";"Since Iba2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. Since Tpm3 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
438;GCN5-TRRAP histone acetyltransferase complex; GCN5-TRRAP-HAT complex;Human;P38398,Q92830,P43246,P52701,O75486,O75528,Q12962,O75529,Q16594,Q9Y4A5;672,2648,4436,2956,8464,10474,6881,27097,6880,8295;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;16260778;10.01.05.01,10.01.09.05,11.02.03.04,32.01.09,42.10.03;"hGCN5/TRRAP HAT complex subclass is required for the multiple functions of BRCA1 (PMID:16260778).";"";""
439;Phosphatidylinositol 3-kinase complex (PIK3CA, PIK3R1);;Bovine;P32871,P23727;282306,282307;MI:0226- ion exchange chromatography | MI:0004- affinity chromatography technologies;8383968;16.01,16.19.03,30.05.01.12,70.02;"Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate phosphatidylinositol 4,5-bisphosphate at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3 ), which, in turn, initiates a vast array of signaling events. PI3Ks are heterodimers, composed of catalytic and regulatory subunits, that are activated by growth factor-receptor tyrosine kinases.";"";""
440;Succinate dehydrogenase complex II (EC 1.3.5.1), mitochondrial; Succinate ubiquinone oxidoreductase;Mouse;Q8K2B3,Q9CQA3,Q9CZB0,Q9CXV1;66945,67680,66052,66925;MI:0069- mass spectrometry studies of complexes | MI:0019- coimmunoprecipitation;16120479;01.05.02.07,02.11.05,16.21.08,20.01.15,70.16.05;"The enzyme complex is a heterotetramer divided into three domains:  SDHA, the catalytic domain- SDHB, the electron transfer subunit- SDHC/SDHD, the dimeric membrane anchor that contains beta-type heme. ";"Paraganglioma syndrome type 4 caused by a mutation in the SDHB gene (PMID:17143317).";""
441;TFTC-type histone acetyl transferase complex;;Human;P03372,Q92830,Q15648,Q93074,Q9UHV7,O60244,Q9Y2X0,Q9NVC6,Q9ULK4,O75448,Q9Y4A5;2099,2648,5469,9968,9969,9282,10025,9440,9439,9862,8295;MI:0091- chromatography technologies | MI:0029- cosedimentation through density gradients | MI:0096- pull down;11931763;10.01.09.05,11.02.03.04,14.07.04,16.01.01,30.01.11,42.10.03,70.10;"This complex is a coactivator of estrogen receptor alpha (ERalpha).";"";""
442;Vacuolar ATPase;;Bovine;P23956,P61420,P31404,P21282,P39942,P11019,Q28029,P79251,O46563,(Q29466,O97681),(P31407,P31408);550622,282148,282147,338089,404152,287017,282405,281641,282657,(286768,338038),(338059,338082);MI:0019- coimmunoprecipitation;15269204;01.03.01.01,16.01,20.01.01.01,20.03.22,20.09.07,70.02;"The complex is found in both the endomembrane system of subcellular organelles and the plasma membrane of certain specialized cells. The function of the V-ATPase is to pump protons across the membrane bilayer, a process powered by hydrolysis of ATP. The V-ATPase is a large, multisubunit complex that can be divided into three domains: a water-soluble V1, which is responsible for binding and hydrolysis of ATP- a membrane embedded V0, which contains the proton translocation pore- and a stalk domain, which functions as a structural and functional connection between the V1 and V0.";"";""
443;BP-SMAD complex;;Human;O14867,P19447,O95452,Q13118,P50539,P17980,O15198,Q15582;571,2071,10804,7071,4601,5702,4093,7045;MI:0019- coimmunoprecipitation;16101586;11.02.03.04.01,70.10;"Homozygous knockout mice for the homeobox protein Msx1 (Hox7) die at birth exhibiting severe abnormalities limited to the craniofacial region, including a complete cleft of the secondary palate. Results suggest that the BP-SMAD complex is required for transcriptional activation of the mouse Msx1 gene.";"";""
444;Signal peptidase complex;;Dog;P67811,P13679,P83362,Q28250,P61008;404004,404003,0,404016,404005;MI:0401- biochemical;8632014;14.04,16.01,20.01.10,70.07;"";"";""
445;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6873,6874,6877,27097,6878,10629,6879,6880,8295;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;10373431;10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,42.10.03,70.10;"";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized. In following publications these proteins were identified as ataxin-7, splicing factor 3B subunit 3 and PAF65A."
446;Succinate dehydrogenase complex II (EC 1.3.5.1), mitochondrial; Succinate ubiquinone oxidoreductase;Bovine;P31039,Q3T189,P35720,Q95123;281480,286840,327696,281481;MI:0069- mass spectrometry studies of complexes | MI:0019- coimmunoprecipitation;16120479;01.05.02.07,02.11.05,16.21.08,20.01.15,70.16.05;"The enzyme complex is a heterotetramer divided into three domains:  SDHA, the catalytic domain- SDHB, the electron transfer subunit- SDHC/SDHD, the dimeric membrane anchor that contains beta-type heme. ";"Paraganglioma syndrome type 4 caused by a mutation in the SDHB gene (PMID:17143317).";""
447;Kir4.1-dystrophin complex, retinal Mueller cells;;Rat;P49655,(Q7TPH2,Q7TPH3,Q7TPH4);29718,(24907,24907,24907);MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"At the time of annotation, the additional member Dp140 of the protein complex was not found in the UniProt database. ";""
448;Kir4.1-alpha-syntrophin complex, retinal Mueller cells;;Rat;P49655,Q498T0;29718,362242;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"";""
449;Kir4.1-beta-dystroglycan complex, retinal Mueller cells;;Rat;Q91XP6,P49655;114489,29718;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"";""
450;Kir4.1-Aqp4 complex, retinal Mueller cells;;Rat;P47863,P49655;25293,29718;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"";""
451;Kir4.1-dystrobrevin complex, retinal Mueller cells;;Rat;P84060,P49655;362715,29718;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"";""
452;Retinal Mueller cells Aqp4-alpha-syntrophin complex;;Rat;P47863,Q498T0;25293,362242;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"";""
453;Retinal Mueller cells Aqp4-beta-dystroglycan complex;;Rat;P47863,Q91XP6;25293,114489;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;16206160;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01,77.03.02.02;"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.";"";""
454;MKP3-CK2alpha complex;;Mouse;Q60737,Q9DBB1;12995,67603;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;15284227;18.02.01,30.01.05.01,43.03.13,47.03.01.01.01;"This complex can include ERK2 protein. CK2 can selectively phosphorylate MKP3, suggesting cross-regulation between CK2alpha and MKP3, as well as a modulation of ERK2-MAPK signaling by CK2alpha via MKP3.";"";""
455;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6873,6874,6877,27097,6878,10629,6879,6880,8295;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;12601814;10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,42.10.03,70.10;"";"";"TAF-II-30, TAF-II-55 and ADA3 were not identified as TFTC subunits in this study."
456;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6873,6874,6877,27097,6878,10629,6879,6880,8295;MI:0006- anti bait coimmunoprecipitation;15115762;10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,42.10.03,70.10;"";"";""
457;Dystrophin-associated glycoprotein complex DGC (Dag1, Dp71f, Sgcd, Snta1), retinal glia cells;;Rat;Q91XP7,P11531,P82347,Q498T0;114489,13405,24052,362242;MI:0019- coimmunoprecipitation;10984432;42.06.03,70.02,73.03.11,77.03.01.01,77.03.02.02;"The results indicate that the DGC could have both structural and signaling functions in retina.";"";"Since Sgcd and Dmd (described as Dp71f) from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
458;Dystrophin-associated glycoprotein complex DGC (Dag1, Dp71f, Utrn), retinal glia cells;;Rat;Q91XP7,P11531,O55147;114489,13405,25600;MI:0019- coimmunoprecipitation;10984432;42.06.03,70.02,73.03.11,77.03.01.01,77.03.02.02;"The results indicate that the DGC could have both structural and signaling functions in retina.";"";"Since Dmd (described as Dp71f) from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
459;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6873,6874,6877,27097,6878,10629,6879,6880,8295;MI:0006- anti bait coimmunoprecipitation;15115762;10.01.05.01,10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,32.01.09,42.10.03,70.10;"";"";""
460;CRB1-MPP5-INADL complex;;Human;P82279,Q8NI35,Q8N3R9;23418,10207,64398;MI:0019- coimmunoprecipitation;11927608;40.01.03,41.05.19,42.06,70.06;"This complex  appears to be evolutionarily conserved and likely plays an important role in protein targeting and cell polarity.";"";""
461;MPP4-MPP5-CRB1 complex;;Human;P82279,Q96JB8,Q8N3R9;23418,58538,64398;MI:0019- coimmunoprecipitation;15914641;34.11.01,77.03.02.02;"This complex is localized in outer limiting membrane.";"";""
462;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6873,6874,6877,27097,6878,10629,6879,6880,8295;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;9603525;10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,42.10.03,70.10;"TFTC complex can replace TFIID in vitro, indicating that multiple preinitiation complexes may play an important role in regulating gene expression.";"";""
463;TFIID-beta complex; TFIID(beta) transcription factor complex;Human;P21675,Q12962,Q15544,Q16514,Q15543,O00268,Q15542,P49848,Q15545,Q16594,P20226;6872,6881,6882,6883,6884,6874,6877,6878,6879,6880,6908;MI:0071- molecular sieving | MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;9603525;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"";"";""
464;InsP3R1-HAP1A-Htt complex;;Rat;P54256,P51111,P29994;29430,29424,25262;MI:0096- pull down | MI:0019- coimmunoprecipitation;12873381;30.01.09.03,77.03.01.01.01;"HAP1A facilitates functional effects of Htt and Htt(exp) on InsP3R1 in planar lipid bilayers (PMID:15379999).";"Htt is involved in Huntington's disease (PMID:15379999).";""
465;InsP3R1-HAP1A-Htt complex;;Mouse;O35668,P42859,P11881;15114,15194,16438;MI:0019- coimmunoprecipitation;12873381;30.01.09.03,77.03.01.01.01;"HAP1A facilitates functional effects of Htt and Htt(exp) on InsP3R1 in planar lipid bilayers (PMID:15379999).";"Htt is involved in Huntington's disease (PMID:15379999).";""
466;Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN);;Human;Q96BI3,Q92542,P49768,Q9NZ42;51107,23385,5663,55851;MI:0019- coimmunoprecipitation;15286082;14.07.11,30.01.05.03,30.05.02.14,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.";"";""
467;Gamma-secretase complex (APH1B, PSEN2, PSENEN, NCSTN);;Human;Q8WW43,Q92542,P49810,Q9NZ42;83464,23385,5664,55851;MI:0019- coimmunoprecipitation;15286082;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenilin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.";"";""
468;Gamma-secretase complex (APH1A, PSEN2, PSENEN, NCSTN);;Human;Q96BI3,Q92542,P49810,Q9NZ42;51107,23385,5664,55851;MI:0019- coimmunoprecipitation;15286082;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.";"";""
469;TFIID-beta complex; TFIID(beta) transcription factor complex;Human;P21675,Q12962,Q15544,Q16514,Q15543,Q6P1X5,O00268,Q15542,P49848,Q15545,Q16594,P20226;6872,6881,6882,6883,6884,6873,6874,6877,6878,6879,6880,6908;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation | MI:0040- electron microscopy | MI:0428- imaging techniques;10591645;11.02.03.01.01,11.02.03.04,70.10;"";"";""
470;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q15543,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6884,6873,6874,6877,27097,6878,10629,6879,6880,8295;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation | MI:0428- imaging techniques | MI:0040- electron microscopy;10591645;10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,42.10.03,70.10;"";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized. In following publications these proteins were identified as ataxin-7, splicing factor 3B subunit 3 and PAF65A."
471;PCAF complex; PCAF histone acetylase-associated complex;Human;Q92831,O75486,O75478,O75528,Q12962,Q16514,O75529,Q9Y6J9,Q16594,Q9Y4A5;8850,8464,6871,10474,6881,6883,27097,10629,6880,8295;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;9674425;10.01.09.05,11.02.03.01,11.02.03.04,14.07.04,42.10.03,70.10;"";"";"PCAF is a complex consisting of more than 20 different proteins. Several proteins have not been characterized in this study."
472;Prolyl 4-hydroxylase (alpha(I)-type);;Human;P13674,P07237;5033,5034;MI:0027- cosedimentation;7753822;14.07.09,16.01,16.17.09,16.21,70.07;"Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens and related proteins.";"";""
473;Prolyl 4-hydroxylase (alpha(II)-type);;Mammalia;Q60716,P07237;18452,5034;MI:0027- cosedimentation;7753822;14.07.09,16.01,16.17.09,16.21,70.07;"Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens and related proteins.";"";""
474;Prolyl 4-hydroxylase (alpha(III)-type);;Human;Q7Z4N8,P07237;283208,5034;MI:0027- cosedimentation;14500733;14.07.09,16.01,16.17.09,16.21,70.07;"Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens and related proteins.";"";""
475;STAGA complex (SPT3-TAF9-GCN5 acetyltransferase complex); STAGA coactivator complex;Human;Q92830,Q15393,O75486,O94864,Q96BN2,O75528,Q12962,Q16514,O75529,Q9Y6J9,Q16594,Q9Y4A5;2648,23450,8464,9913,117143,10474,6881,6883,27097,10629,6880,8295;MI:0004- affinity chromatography technologies | MI:0007- anti tag coimmunoprecipitation;11564863;10.01.09.05,11.02.03.04.01,14.07.04,32.01.09,42.10.03,70.10;"";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized: STAF60, STAF55, STAF46."
476;STAGA complex (SPT3-TAF9-GCN5 acetyltransferase complex); STAGA coactivator complex;Human;O15265,Q92830,Q15393,O75486,O94864,Q96BN2,O75528,Q12962,Q16514,O75529,Q9Y6J9,Q16594,Q9Y4A5;6314,2648,23450,8464,9913,117143,10474,6881,6883,27097,10629,6880,8295;MI:0006- anti bait coimmunoprecipitation;15115762;10.01.09.05,11.02.03.04.01,14.07.04,32.01.09,42.10.03,70.10;"This complex is a coactivator required for transcription of a subset of RNA polymerase II-dependent genes.";"";""
477;PCAF complex; PCAF histone acetylase-associated complex;Human;Q92831,O75486,O75478,O75528,Q12962,Q16514,O75529,Q9Y6J9,Q16594,Q9Y4A5;8850,8464,6871,10474,6881,6883,27097,10629,6880,8295;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;9885574;10.01.09.05,11.02.03.01,11.02.03.04,14.07.04,42.10.03,70.10;"";"";"PCAF is a complex consisting of more than 20 different proteins. Several proteins have not been characterized in this study."
478;STAGA core complex (SPT3-TAF9-GCN5 acetyltransferase complex);;Human;Q92830,O75486,Q16594;2648,8464,6880;MI:0007- anti tag coimmunoprecipitation;9726987;10.01.09.05,11.02.03.04.01,14.07.04,42.10.03,70.10;"";"";""
479;Mupp1-Dlg4-Syngap1-CamkII complex;;Rat;P11275,P08413,P31016,O55164,Q9QUH6;25400,24245,29495,29365,192117;MI:0019- coimmunoprecipitation;15312654;34.03.01,73.03.13;"The SynGAP-alpha-MUPP1-CAMKII complex is a component of the NMDAR supramolecular structure in hippocampal pyramidal neurons. The integrity of this complex is critical for synaptic NMDAR-dependent AMPA receptor trafficking.";"";""
480;TIF-IB complex;;Mouse;P97357,P97358,Q6PDZ2,P29037;21339,21340,21341,21374;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;8414971;11.02.01,11.02.03.01.01,70.10;"TIF-IB complex interacts with the mouse ribosomal gene promoter and nucleates the formation of an initiation complex containing RNA polymerase I.";"";""
482;cRET-Shc-Grb2-Gab2-P85PI3K-Shp2 complex;;Mouse;Q9Z1S8,Q60631,P26450,P35235,P35546,P98083;14389,14784,18708,19247,19713,20416;MI:0019- coimmunoprecipitation;10995764;30.01.09,30.05.01.12;"";"";""
484;TFIID complex;;Human;P21675,Q12962,Q15544,Q16514,Q15543,O00268,Q15542,P49848,Q15545,Q16594,P20226;6872,6881,6882,6883,6884,6874,6877,6878,6879,6880,6908;MI:0004- affinity chromatography technologies;7729427;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"";"";""
485;TFIID complex, B-cell specific;;Human;P21675,Q12962,Q15544,Q16514,Q15543,O00268,Q92750,Q15542,P49848,Q15545,Q16594,P20226;6872,6881,6882,6883,6884,6874,6875,6877,6878,6879,6880,6908;MI:0004- affinity chromatography technologies;8858156;11.02.03.01.01,11.02.03.04,16.03.01,70.10,73.03.07.02.01.01;"TAF-II-105 (TAF4B) is a cell-type specific subunit of TFIID complex. Up to now TAF-II-105 is only found in differentiated B cells. Isolation of TBP and TAF9-TAF13 was not shown in this paper. ";"";""
486;WIP-WASp-actin-myosin-IIa complex;;Human;P62736,P19105,P35579,P60660,P42768,O43516;59,10627,4627,4637,7454,7456;MI:0019- coimmunoprecipitation;16606694;36.25.16.03.03,42.04.03,70.04;"The multiprotein complex is important for NK cell function. Killer cell immunoglobulin-like receptor inhibitory signaling affects proteins involved in cytoskeletal rearrangements. WIP plays a central role in the formation of the complex and in the regulation of NK cell activity.";"";""
487;Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III | Cytochrome reductase | Ubiquinol:cytochrome c oxidoreductase;Bovine;P00125,P00157,P07552,P00130,P00129,P31800,P23004,P13272,P00126,P13271;512500,3283889,281570,616109,616871,282393,282394,287020,613899,286885;MI:0069- mass spectrometry studies of complexes | MI:0019- coimmunoprecipitation;16120479;02.10,02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"";"";"Complex III consists of 11 subunits- displayed just 10 subunits-  reason: Subunit V (Rieske iron sulfur protein) contains subunit IX (= precursor of subunit V), compare PMID:8386158- subunit XI (P07552) could not be experimentally identified."
488;Vezf1-p68RacGap complex;;Mouse;Q8BL80,Q5SXC4;239027,22344;MI:0019- coimmunoprecipitation;14966113;11.02.03.04,30.01,47.03.03.02,70.03,70.10;"";"";""
489;TFIIA complex;;Human;P52655,P52657;2957,2958;MI:0004- affinity chromatography technologies;8224848;11.02.03.01.01,11.02.03.04,70.10;"TFIIA is a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12). ";"";"GTF2A1 encodes both the alpha and beta subunits."
490;TFIIA complex;;Human;P52655,P52657;2957,2958;MI:0091- chromatography technologies;2247058;11.02.03.01.01,11.02.03.04,70.10;"TFIIA is a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12). ";"";"GTF2A1 encodes both the alpha and beta subunits."
492;DA complex; TFIID-TFIIA complex;Human;P52655,P52657,P21675,Q12962,Q15544,Q16514,Q15543,Q6P1X5,Q5VWG9,O00268,Q15542,P49848,Q15545,Q16594,P20226;2957,2958,6872,6881,6882,6883,6884,6873,83860,6874,6877,6878,6879,6880,6908;MI:0091- chromatography technologies;2247058;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"DA is a multiprotein complex consisting of TFIID complex and TFIIA complex.";"";""
493;DAB complex; TFIID-TFIIA-TFIIB complex;Human;P52655,P52657,Q00403,P21675,Q12962,Q15544,Q16514,Q15543,Q6P1X5,Q5VWG9,O00268,Q15542,P49848,Q15545,Q16594,P20226;2957,2958,2959,6872,6881,6882,6883,6884,6873,83860,6874,6877,6878,6879,6880,6908;MI:0091- chromatography technologies;2247058;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"DAB is a multiprotein complex consisting of TFIID complex, TFIIA complex and TFIIB.";"";""
494;Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; complex III | Cytochrome reductase | Ubiquinol:cytochrome c oxidoreductase;Bovine;P00125,P00157,P07552,P00130,P00129,P31800,P23004,P13272,P00126,P13271;512500,3283889,281570,616109,616871,282393,282394,287020,613899,286885;MI:0047- far western blotting;8386158;02.10,02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"";"";"The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex."
495;Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III | Cytochrome reductase | Ubiquinol:cytochrome c oxidoreductase;Mouse;Q9D0M3,P00158,Q9CPX8,Q8R1I1,Q9D855,Q9CZ13,Q9DB77,Q9CR68,P99028,Q9CQ69;66445,17711,66594,66152,67530,22273,67003,66694,66576,22272;MI:0069- mass spectrometry studies of complexes | MI:0019- coimmunoprecipitation;16120479;02.10,02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"";"";"Complex III consists of 11 subunits- displayed just 10 subunits-  reason: Subunit V precursor (Rieske iron sulfur protein) contains subunit IX, compare PMID:8386158- subunit XI (Q9CPX8) could not be experimentally identified."
496;TFIID complex;;Mouse;Q80UV9,Q8K0H5,Q99JX1,Q8VE65,Q8C176,Q91WW6,Q8C092,Q62311,Q9R1C0,Q9EQH4,Q8VI33,P29037;270627,24075,68776,66464,319944,228980,226182,21343,24074,63856,108143,21374;MI:0004- affinity chromatography technologies;10438527;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"";"";""
497;TAF4-TAF12 subcomplex of TFIID complex;;Human;Q16514,O00268;6883,6874;MI:0004- affinity chromatography technologies | MI:0114- x-ray crystallography;12237304;11.02.03.01.01,11.02.03.04,16.01,70.10;"TAF12 forms a histone-like heterodimer with TAF4, rather than homodimerizing as suggested earlier (PMID:8598932).";"";""
498;Ryk-Wny1-Fzd8 complex;;Mouse;Q61091,Q01887,P04426;14370,20187,22408;MI:0019- coimmunoprecipitation;15454084;30.05.02.20;"";"";""
499;Ryk-Wny1 complex;;Mouse;Q01887,P04426;20187,22408;MI:0019- coimmunoprecipitation;15454084;30.05.02.20;"";"";""
500;Ryk-Wnt3a complex;;Mouse;Q01887,P27467;20187,22416;MI:0019- coimmunoprecipitation;15454084;30.05.02.20;"";"";""
501;Ryk-Dvl1 complex;;Mouse;P51141,Q01887;13542,20187;MI:0019- coimmunoprecipitation;15454084;30.05.02.20;"";"";""
502;Kir4.1-dystrophin complex, whole brain lysate;;Mouse;P11531,Q9JM63;13405,16513;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15102837;20.01.01.01,20.03.01.01,70.02,77.03.01.01.01;"";"";"The dystrophin isoform has been described as Dp71."
503;Kir4.1-alpha-1-syntrophin complex, whole brain lysate;;Mouse;Q9JM63,Q61234;16513,20648;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15102837;20.01.01.01,20.03.01.01,70.02,77.03.01.01.01;"The results suggest that Kir4.1 is localized in glial cells by its association with the DGC through a PDZ domain-mediated interaction with alpha-syntrophin and suggest an important role for the DGC in central nervous system physiology.";"";""
504;Kir4.1-beta-dystroglycan complex, whole brain lysate;;Mouse;Q62165,Q9JM63;13138,16513;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15102837;20.01.01.01,20.03.01.01,70.02,77.03.01.01.01;"The dystroglycan subunit has been described as beta-dystroglycan.";"";""
505;Kir4.1-dystrophin complex, cortical astrocytes;;Mouse;P11531,Q9JM63;13405,16513;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15102837;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01;"";"";"The dystrophin isoform has been described as Dp71."
506;Kir4.1-alpha-1-syntrophin complex, cortical astrocytes;;Mouse;Q9JM63,Q61234;16513,20648;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15102837;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01;"The results suggest that Kir4.1 is localized in glial cells by its association with the DGC through a PDZ domain-mediated interaction with alpha-syntrophin and suggest an important role for the DGC in central nervous system physiology.";"";""
507;Kir4.1-beta-dystroglycan complex, cortical astrocytes;;Mouse;Q62165,Q9JM63;13138,16513;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15102837;20.01.01.01,20.03.01.01,70.02,73.03.11,77.03.01.01;"";"";"The dystroglycan subunit has been described as beta-dystroglycan."
508;TFIID complex;;Human;P21675,Q12962,Q15544,Q16514,O00268,Q15542,P49848,Q15545,Q16594,P20226;6872,6881,6882,6883,6874,6877,6878,6879,6880,6908;MI:0006- anti bait coimmunoprecipitation;8663456;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"";"";""
509;TFIID complex;;Human;P21675,Q12962,Q15544,Q16514,Q15543,Q92804,O00268,Q15542,P49848,Q15545,Q16594,P20226;6872,6881,6882,6883,6884,8148,6874,6877,6878,6879,6880,6908;MI:0006- anti bait coimmunoprecipitation;8890175;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"";"";""
510;TFIID subcomplex, testis-specific;;Mouse;Q9D3R9,P29037;74469,21374;MI:0006- anti bait coimmunoprecipitation;12665565;11.02.03.01.01,11.02.03.04,16.03.01,41.05.25,70.10,77.03.15.07;"";"";""
511;TFIID subcomplex, testis-specific;;Mouse;Q80UV9,Q9D3R9;270627,74469;MI:0018- two hybrid;12665565;11.02.03.01.01,11.02.03.04,16.03.01,41.05.25,70.10,77.03.15.07;"";"";""
512;AQP-1 regulatory complex;;Rat;P29975,P35525,P08753,Q63664,P14423;25240,29232,25643,25472,29692;MI:0019- coimmunoprecipitation;14759764;20.01.01,20.03.01,20.09.16,77.03.11.09;"";"";""
513;TFTC complex (TATA-binding protein-free TAF-II-containing complex);;Human;O15265,Q92830,Q15393,O75486,O75528,Q12962,Q16514,Q6P1X5,O00268,Q15542,O75529,P49848,Q9Y6J9,Q15545,Q16594,Q9HBM6,Q9Y4A5;6314,2648,23450,8464,10474,6881,6883,6873,6874,6877,27097,6878,10629,6879,6880,51616,8295;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;15899866;10.01.09.05,11.02.03.01.01,11.02.03.04.01,14.07.04,42.10.03,70.10;"Gene expression profiling revealed that Taf9 and Taf9b control the expression of different sets of genes.";"";""
514;TFIID-beta complex;;Human;P21675,Q12962,Q15544,Q16514,Q15543,O00268,Q15542,P49848,Q15545,Q16594,Q9HBM6,P20226;6872,6881,6882,6883,6884,6874,6877,6878,6879,6880,51616,6908;MI:0071- molecular sieving | MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;15899866;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"Gene expression profiling revealed that Taf9 and Taf9b control the expression of different sets of genes.";"";""
515;Inner medullary AKAP-signaling complex;;Rat;P09217,(P63329,P20651),(P12368,P12369);25522,(24674,24675),(29699,24679);MI:0004- affinity chromatography technologies;11592953;14.04,14.07.03,30.01.05,70.22;"";"";"At the time of annotation, the additional member 90-kDa AKAP of the protein complex was not found in the UniProt database."
516;Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III | Cytochrome reductase | Ubiquinol:cytochrome c oxidoreductase;Rat;Q9D0M3,P00159,A9UMV7,Q8R1I1,B2RYS2,Q68FY0,P32551,P20788,Q5M9I5,Q7TQ16;66445,0,690848,66152,362897,301011,293448,291103,366448,497902;MI:0047- far western blotting;12794875;02.10,02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"";"";"Since the complete protein information from rat was not available in the UniProt database at the time of annotation, some of the orthologous proteins from mouse (Cyc1, Uqcr10) were used."
517;Kinase-scaffold-phosphatase complex, PKA-AKAP79-CaN;;Human;P24588,Q08209,P13861;9495,5530,5576;MI:0055- fluorescent resonance energy transfer;12507994;14.04,14.07.03,14.10,30.05,70.02,70.04;"";"";""
518;AKAP250-PKA-PDE4D complex;;Human;Q02952,Q08499,(P17612,P22694,P22612);9590,5144,(5566,5567,5568);MI:0415- enzymatic studies | MI:0019- coimmunoprecipitation;16642035;14.04,18.01.03,18.02.01,30.01.09.07,70.02;"PDE4D protein isoforms were specified as PDE4D5 and PDE4D3. The authors identified gravin as the AKAP responsible for the localized regulation of cAMP levels by PKA and PDE4 activity.";"";""
519;AMY-1-S-AKAP84-RII-beta complex;;Human;Q92667,Q99417,P31323;8165,26292,5577;MI:0019- coimmunoprecipitation;11483602;30.01.09.07,41.05.25,70.16;"";"";""
520;KCNQ1 macromolecular complex;;Human;Q99996,P51787,(P62136,P62140,P36873),(P17612,P22694,P22612),(P13861,P31323);10142,3784,(5499,5500,5501),(5566,5567,5568),(5576,5577);MI:0096- pull down | MI:0019- coimmunoprecipitation;11799244;20.03.01.01,30.01.09.07,36.25.03.01.05,75.03.12.03;"This complex is required for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel.";"";""
521;Polycystin-1-E-cadherin-beta-catenin complex;;Human;P12830,P35222,P98161;999,1499,5310;MI:0019- coimmunoprecipitation;14718571;42.06.04,45.03.09,47.03.07.01,70.02,70.03,75.03.09;"Complex is disrupted in ADPKD cells. ";"Polycystin-1-E-cadherin-beta-catenin complex is involved in autosomal dominant polycystic kidney disease (ADPKD). The authors suggest that the expression of mutant polycystin-1 in ADPKD cells, which fails to be cell surface-expressed and assemble into multiprotein complexes with E-cadherin, results in altered cell-cell adhesion and polycystin-1 signaling, thereby triggering dedifferentiation.";""
522;Polycystin-1-E-cadherin-beta-catenin-Flotillin-2 complex;;Human;P12830,P35222,Q14254,P98161;999,1499,2319,5310;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;16038619;16.09,42.06.04,45.03.09,47.03.07.01,70.02,75.03.09,77.03.07.01;"The authors conclude that even though the large multiprotein complex formed by polycystin-1, E-cadherin, beta-catenin and flotillin-2 is not associated with typical lipid rafts, it contains cholesterol molecules that mediate interactions between complexed proteins and may represent a specific membrane domain organization. ";"PKD1 is involved in ADPKD (autosomal dominant polycystic kidney disease).";""
523;Yotiao-RII-NR1 complex;;Rat;Q9JHE0,P35439,P12368,P12369;246150,24408,29699,24679;MI:0019- coimmunoprecipitation;10618500;18.02.07,30.01.09.07,73.03.13;"This complex probably promote cAMP-dependent modulation of NMDA receptor activity at synapses.";"";""
525;TIP60 histone acetylase complex;;Human;O96019,Q92993,Q9Y265,Q9Y230,Q9Y4A5;86,10524,8607,10856,8295;MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;10966108;10.01.02,10.01.05.01,10.01.09.05,14.07.04,16.03.01,40.10.02,42.10.03,70.10;"The TIP60 histone acetylase complex plays a role in DNA repair and apoptosis.";"";"Additional unknown members of the TIP60 complex (p160, p150, p100, p70, p57, p40, p31, p29) have been isolated."
526;TRPC3-TRPC4 channel complex, redox-sensitive;;Pig;Q9QZC1,Q9QUQ5;22065,22066;MI:0019- coimmunoprecipitation;16537542;20.01.01.01,20.03.01.01,32.01.01,70.02,77.03.03.02;"Complex analysed in porcine aortic endothelial cells (PAECs). The authors propose TRPC3 and TRPC4 as subunits of native endothelial cation channels that are governed by the cellular redox state.";"";"Since TRPC3 and TRPC4 from pig were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
527;TRPC3-TRPC4 channel complex, redox-sensitive;;Human;Q13507,Q9UBN4;7222,7223;MI:0019- coimmunoprecipitation | MI:0055- fluorescent resonance energy transfer;16537542;20.01.01.01,20.03.01.01,32.01.01,70.02;"Complex analysed in the HEK293 expression system. The authors propose TRPC3 and TRPC4 as subunits of native endothelial cation channels that are governed by the cellular redox state.";"";""
528;NuA4/Tip60 HAT complex;;Human;O96019,Q9H0E9,Q9HAF1,Q9NPF5,Q96L91,Q9H2F5,Q92993,Q9NXR8,Q9UBU8,Q15014,Q9NV56,Q9Y265,Q9Y230,Q9Y4A5,O95619;86,10902,64769,55929,57634,80314,10524,54556,10933,9643,55257,8607,10856,8295,8089;MI:0004- affinity chromatography technologies;12963728;01.04,10.01.02,10.01.05.01,10.01.09.05,14.07.04,16.03.01,42.10.03,70.10;"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.";"";""
529;NuA4/Tip60 HAT complex;;Human;O96019,Q9H0E9,Q9HAF1,Q9NPF5,Q96L91,Q9H2F5,Q92993,Q9NXR8,Q9UBU8,Q15014,Q9NV56,Q9Y265,Q9Y230,Q9Y4A5,Q15906,O95619;86,10902,64769,55929,57634,80314,10524,54556,10933,9643,55257,8607,10856,8295,6944,8089;MI:0007- anti tag coimmunoprecipitation;15647280;01.04,10.01.02,10.01.05.01,10.01.09.05,14.07.04,16.03.01,42.10.03,70.10;"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.";"";""
530;Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV | COX;Bovine;P00423,P00426,P00428,P07471,P00429,P04038,P07470,P13183,P00430,P10175,P00396,P68530,P00415;281090,444878,287012,282200,100270792,782486,338086,327674,327718,615757,0,3283880,0;MI:0024- confirmational text mining;11943460;02.11.05,02.13.03,16.01,20.01.15,70.16.05;"Cytochrome oxidase (COX) is the fourth complex of the mitochondrial respiratory chain. It transfers electrons from ferrocytochrome c to molecular oxygen.";"";""
531;XPA-ERCC1-ERCC4 complex;;Human;P07992,Q92889,P23025;2067,2072,7507;MI:0004- affinity chromatography technologies;8197175;10.01.05.01,32.01,70.10;"";"ERCC4 is involved in Xeroderma pigmentosum group F.";""
532;M1 mAChR-TRPC6-multiprotein complex;;Rat;P62161,P08482,Q62658,P05696,Q99N77,(P63329,P20651);24244,25229,25639,24680,89823,(24674,24675);MI:0019- coimmunoprecipitation;15994335;14.07.03,18.01.07,18.02.01,20.01.01.01,20.03.01,30.05.02.24.02;"Complex constitutes only after stimulation of M1 mAChRs with carbachol. The results of the examinations of the time course of these associations suggest that M1 mAChRs and PKC associate with TRPC6 channels at the same time or slightly earlier than FKBP12, calcineurin, and calmodulin and that the later proteins remain in the TRPC6 complex after M1 mAChRs and PKC have disappeared.";"";"The authors didn't describe the specific isoform of protein kinase C. "
533;IMP3-IMP4-MPP10 complex;;Human;Q9NV31,Q96G21,O00566;55272,92856,10199;MI:0096- pull down | MI:0029- cosedimentation through density gradients | MI:0019- coimmunoprecipitation;12655004;14.10,16.01,16.03.03,70.10;"The formation of the hImp3-hMpp10-hImp4 complex correlates with the nucleolar localization of these proteins.";"";""
534;M1 mAChR-TRPC6-PKC complex;;Rat;P08482,P05696,Q99N77;25229,24680,89823;MI:0019- coimmunoprecipitation;15994335;14.07.03,18.01.07,18.02.01,20.01.01.01,20.03.01,30.05.02.24.02;"Complex constitutes only after stimulation of M1 mAChRs with carbachol. The results of the examinations of the time course of these associations suggest that M1 mAChRs and PKC associate with TRPC6 channels at the same time or slightly earlier than FKBP12, calcineurin, and calmodulin and that the later proteins remain in the TRPC6 complex after M1 mAChRs and PKC have disappeared. Maximal association of M1 mAChRs and PKC with TRPC6 channels occurs ~2 min after the addition of carbachol.";"";"The authors didn't describe the specific isoform of protein kinase C. "
535;TRAP complex; thyroid hormone receptor-associated protein complex;Human;P24863,Q15648,Q9BTT4,Q93074,Q9UHV7,O60244,Q9Y2X0,Q9NVC6,Q13503,O75448,Q6P2C8,Q9Y3C7,Q9NPJ6,O75586,P10827,Q9Y2W1;892,5469,84246,9968,9969,9282,10025,9440,9412,9862,9442,51003,29079,10001,7067,9967;MI:0004- affinity chromatography technologies;10198638;11.02.03.04,18.02.09,30.01.09.08,30.01.11,70.10;"The human thyroid hormone receptor-associated protein (TRAP) complex is a coactivator for nuclear receptors.  Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"Two, up to now uncharacterized members of the complex have been additionally isolated: TRAP97 and TRAP93. "
536;TRPC1-TRPC3-TRPC7 complex;;Human;P48995,Q13507,Q9HCX4;7220,7222,57113;MI:0019- coimmunoprecipitation;15972814;20.01.01.01,20.03.01,34.01.01.01,70.02;"The results indicate that endogenous TRPC1, TRPC3, and TRPC7 participate in forming heteromeric store-operated channels, whereas TRPC3 and TRPC7 can also participate in forming heteromeric receptor-operated channels.";"";""
537;Mediator complex; Mediator of transcriptional regulation;Mouse;O35692,A2ABV5,Q6PGF3,Q8VCD5,Q9R0X0,Q9CQ39,Q9CQA5,Q921D4,Q9CZB6;57261,26896,216154,234959,56771,108098,67381,69792,66213;MI:0091- chromatography technologies | MI:0006- anti bait coimmunoprecipitation;9671713;11.02.03,11.02.03.04,16.01,18.01.07,18.02.09,30.01.05.01,70.10;"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. The mouse mediator complex binds to the RNA polymerase II C-terminal domain (CTD) and stimulates phosphorylation of the CTD by TFIIH. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
538;Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV | COX;Mouse;P19783,P12787,P19536,P43024,P56391,Q9CPQ1,P48771,P56393,P17665,Q64445,Q9MD68,P00405,P00416;12857,12858,12859,12861,110323,12864,12866,66142,12867,12868,19224,17709,0;MI:0047- far western blotting;12865426;02.11.05,02.13.03,16.01,20.01.15,70.16.05;"Cytochrome oxidase (COX) is the fourth complex of the mitochondrial respiratory chain. It transfers electrons from ferrocytochrome c to molecular oxygen.";"";""
540;HMG1-TBP-TATA complex;;Mammalia;P10103,P20226;282691,6908;MI:0413- electrophoretic mobility shift assay;11390376;11.02.03.04.03,16.03.01;"HMG-1 binding increases the affinity of TBP for the TATA box. The HMG1-TBP-TATA complex is proposed to inhibit the assembly of the preinitiation complex.";"";""
541;IGF1-IGFBP3-ALS complex;;Human;P05019,P35858,P17936;3479,3483,3486;MI:0004- affinity chromatography technologies;9795367;36.25.07;"Circulating levels of IGF-I, IGFBP-3 and ALS, and their degree of association in the ternary complex in the fetus increased with gestational age.";"IGF1 is implicated in the pathophysiology of pre-eclampsia.";""
542;Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV, heart | COX;Bovine;P00423,P00426,P00428,P07471,P00429,P04038,P07470,P13183,P00430,P10175,P00396,P68530,P00415;281090,444878,287012,282200,100270792,782486,338086,327674,327718,615757,0,3283880,0;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;6303162;02.11.05,02.13.03,16.01,20.01.15,70.16.05;"Cytochrome oxidase (COX) is the fourth complex of the mitochondrial respiratory chain. It transfers electrons from ferrocytochrome c to molecular oxygen.";"";""
543;Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV, liver | COX;Bovine;P00423,P00426,P00428,P13182,P00429,P04038,P13184,P13183,P00430,P14622,P00396,P68530,P00415;281090,444878,287012,282199,100270792,782486,327688,327674,327718,281091,0,3283880,0;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;6303162;02.11.05,02.13.03,16.01,20.01.15,70.16.05;"Cytochrome oxidase (COX) is the fourth complex of the mitochondrial respiratory chain. It transfers electrons from ferrocytochrome c to molecular oxygen.";"";""
544;TRPC3-TRPC6-Ca2+-signaling complex;;Dog;Q9JID2,P29994,Q63269,P10687,O89040,Q99JE6,Q08849,Q9JMI9,(Q99N76,Q99N77,Q99N78);81662,25262,25679,24654,85240,29322,81802,60395,(89823,89823,89823);MI:0019- coimmunoprecipitation;15623527;20.01.01.01,20.03.01,70.02,75.03.09;"The results demonstrate that most of the same Ca2+-signaling proteins display polarized apical localization in MDCK cells. The data suggest that apically localized TRPC channels can be regulated by Ca2+-signaling mechanisms.";"";"Since several proteins  from dog  were not available in the UniProt database at the time of annotation, the orthologous proteins from rat were used. "
546;Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV | COX;Rat;P10888,P11240,P12075,P10818,P80430,P11950,P35171,P80431,P80432,P80433,P05503,P00406,P05505;29445,252934,94194,25282,0,286962,29507,303393,100188937,171335,26195,26198,26204;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;6303162;02.11.05,02.13.03,16.01,20.01.15,70.16.05;"Cytochrome oxidase (COX) is the fourth complex of the mitochondrial respiratory chain. It transfers electrons from ferrocytochrome c to molecular oxygen.";"";""
547;SMCC complex; SRB/MED-containing cofactor complex;Human;P24863,P49336,Q15648,Q93074,Q9UHV7,O60244,Q9Y2X0,Q9NVC6,Q13503,O75448,Q6P2C8,Q9NPJ6,O75586,Q9Y2W1;892,1024,5469,9968,9969,9282,10025,9440,9412,9862,9442,29079,10001,9967;MI:0004- affinity chromatography technologies;10198638;11.02.03.04,16.01,18.01.07,18.02.09,30.01.11,70.10;"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors. ";"";"In SMCC two, up to now uncharacterized members of the complex have been additionally isolated: TRAP97 and TRAP93."
548;DRIP complex; vitamine-D-receptor interacting protein complex;Human;Q15648,Q93074,Q9UHV7,O60244,Q9Y2X0,Q9NVC6,Q9ULK4,O75448,O95402,Q9NPJ6,O75586,O43513,P28702,P11473;5469,9968,9969,9282,10025,9440,9439,9862,9441,29079,10001,9443,6257,7421;MI:0004- affinity chromatography technologies | MI:0047- far western blotting;9637681;11.02.03.04.01,14.07.04,18.02.09,30.01.09.08,30.01.11,70.10;"Nuclear receptors such as the steroid and thyroid hormone and vitamins A and D receptors, are known to regulate transcription by binding their cognate lipophilic ligands and subsequently undergoing a conformational change that alters their ability to interact with coregulatory proteins. These coregulatory proteins typically consist of complexes like DRIP that either repress (corepressors) or activate (coactivators) transcription. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
549;DRIP complex; vitamine-D-receptor interacting protein complex;Human;Q15648,Q93074,Q9UHV7,O60244,Q9Y2X0,Q9NVC6,Q9ULK4,O75448,O95402,Q9NPJ6,O75586,O43513,P28702,P11473;5469,9968,9969,9282,10025,9440,9439,9862,9441,29079,10001,9443,6257,7421;MI:0004- affinity chromatography technologies;10235266;11.02.03.04.01,14.07.04,16.01,18.02.09,30.01.09.08,30.01.11,70.10;"Nuclear receptors such as the steroid and thyroid hormone and vitamins A and D receptors, are known to regulate transcription by binding their cognate lipophilic ligands and subsequently undergoing a conformational change that alters their ability to interact with coregulatory proteins. These coregulatory proteins typically consist of complexes like DRIP that either repress (corepressors) or activate (coactivators) transcription. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
550;NOS3-CAV1-NOSTRIN complex;;Human;Q03135,P29474,Q8IVI9;857,4846,115677;MI:0019- coimmunoprecipitation | MI:0663- confocal microscopy;16807357;14.04,70.02,75.03.08,77.03.03.02;"Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN.";"";""
551;TDT-TDIF2-core-histone complex;;Human;P04053,Q5QJE6,(O75367,Q9P0M6);1791,30836,(9555,55506);MI:0019- coimmunoprecipitation;12786946;10.01.09.05,18.02.01,70.10;"The authors propose a dual function for TdIF2 in the N region synthesis. One is the function as an inhibitor of TdT. The other is that of a chromatin remodeling protein.";"";""
552;IFNB1-IFNAR1-IFNAR2- complex;;Human;P17181,P48551,P01574;3454,3455,3456;MI:0030- cross-linking studies;10493588;14.01,16.01;"";"";""
553;RHOA-IP3R-TRPC1 complex;;Human;Q14643,P61586,P48995;3708,387,7220;MI:0096- pull down | MI:0019- coimmunoprecipitation;12766172;20.01.01.01,20.03.01.01,34.01.01.01,70.02,77.03.03.02;"Cells were stimulated with thrombin. The authors showed that thrombin stimulation of endothelial cells induced translocation of Rho, and subsequent co-localization of Rho with TRPC1 and IP3R at the plasmalemma.";"";""
554;PBAF complex (Polybromo- and BAF containing complex); SWI/SNF complex B;Human;O96019,Q68CP9,Q86U86,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q969G3;86,196528,55193,6597,6598,6599,6601,6602,6603,6605;MI:0226- ion exchange chromatography;11780067;10.01.09.05,11.02.03.04.01,16.03.01,30.01.09.08,30.01.11,42.10.03,70.10.03;"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome. As additional members of the complex the authors mentioned actin and beta-tubulin.";"";""
555;BAF complex; SWI/SNF-A complex;Human;O96019,O14497,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q969G3;86,8289,6597,6598,6599,6601,6602,6603,6605;MI:0226- ion exchange chromatography;11780067;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10.03;"";"";""
556;PBAF complex (Polybromo- and BAF containing complex); SWI/SNF complex B;Human;O96019,Q68CP9,Q86U86,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3;86,196528,55193,6597,6598,6599,6601,6602,6605;MI:0007- anti tag coimmunoprecipitation;15985610;10.01.09.05,11.02.03.04.01,16.03.01,30.01.09.08,30.01.11,42.10.03,70.10.03;"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome.";"";""
557;TRP1-G alpha-11-IP3R3-CAV1 signaling complex;;Human;Q03135,P29992,Q14573,P48995;857,2767,3710,7220;MI:0019- coimmunoprecipitation;10766822;20.01.01.01,20.03.01.01,34.01.01.01,70.02;"The results demonstrate that caveolar microdomains provide a scaffold for  assembly of key Ca(2+) signaling proteins into a complex and  coordination of the molecular interactions leading to the activation of SOC (store-operated Ca(2+) influx).";"";""
558;Channel complex TRPM6-TRPM7;;Human;Q9BX84,Q96QT4;140803,54822;MI:0055- fluorescent resonance energy transfer;14976260;20.01.01.01,20.03.01.01,70.02,75.03.09;"";"";""
559;Decapping complex;;Human;Q9NPI6,Q8IU60,P26196,Q96F86,Q6P2E9;55802,167227,1656,80153,23644;MI:0019- coimmunoprecipitation;16364915;11.04.03.11,70.03;"Decapping is a key step in mRNA turnover. The decapping complex was found to be localized in cytoplasmic processing bodies (PBs), which are thought to be the sites of mRNA decay.";"";""
560;Kir6.2-Sur1 complex; K(ATP) channel complex;Mouse;Q09429,Q61743;25559,16514;MI:0040- electron microscopy | MI:0096- pull down;16308567;16.19,20.01.01.01,20.03.01.01,20.03.22,70.02;"The close juxtaposition of Kir6.2 and SUR1 subunits in both transmembrane and cytosolic domains provides for extensive intersubunit interactions and is consistent with earlier studies demonstrating physical interactions between SUR1 and Kir6.2 within both transmembrane and cytosolic domains.";"";"A fusion protein of rat SUR1 and mouse Kir6.2 was used for analysis. "
561;LSm1-7 complex;;Human;O15116,Q9Y333,P62310,Q9Y4Z0,Q9Y4Y9,P62312,Q9UK45;27257,57819,27258,25804,23658,11157,51690;MI:0226- ion exchange chromatography;15711010;11.04.03.11,16.03.03,70.03;"The cytoplasmic LSm1-7 complex is involved in mRNA decay. The complex has been shown to accumulate in processing bodies (PBs). The LSm2-8 complex which differs in only one subunit from the LSm1-7 complex is involved in RNA splicing. In contrast to the LSM1-7 complex, recombinant LSm2-8 binds to U6 snRNA in vitro.";"";""
562;LSm2-8 complex;;Human;Q9Y333,P62310,Q9Y4Z0,Q9Y4Y9,P62312,Q9UK45,O95777;57819,27258,25804,23658,11157,51690,51691;MI:0029- cosedimentation through density gradients | MI:0226- ion exchange chromatography;10523320;11.04.03.01,16.03.03,70.03,70.10;"The LSm2-8 complex which differs in only one subunit from the LSm1-7 complex is involved in RNA splicing. In contrast to the LSM1-7 complex, recombinant LSm2-8 binds to U6 snRNA in vitro.";"";""
563;F1F0-ATP synthase (EC 3.6.3.14), mitochondrial; Complex V | F1F0 ATPase;Human;P25705,P06576,P36542,P30049,P56381,P24539,P05496,O75947,P56385,P18859,P56134,O75964,P48047,Q6IAQ7,P00846,P03928;498,506,509,513,514,515,516,10476,521,522,9551,10632,539,93974,4508,4509;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;12110673;01.04,02.13.03,02.45.15,16.19.03,20.01.15,70.16.05,75.03.12.03;"F1F0 ATPase is the fifth complex in the respiratory chain. The mammalian complex V consists of 16 different subunits with alpha(3), beta(3), gamma, delta and epsilon comprising the F1 part and a, b, c, d, e, f, g, A6L, OSCP, and coupling factor 6 providing the F0 and stator. Also associated in the complex under some conditions is an intrinsic inhibitor protein IF1.";"";""
564;BAF complex; SWI/SNF complex A;Human;O96019,O14497,Q12824,Q92922,Q8TAQ2,Q969G3,(P51531,P51532),(Q96GM5,Q92925,Q6STE5);86,8289,6598,6599,6601,6605,(6595,6597),(6602,6603,6604);MI:0226- ion exchange chromatography | MI:0004- affinity chromatography technologies;8895581;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10;"";"";"At the time of annotation, the additional member BAF110 of the protein complex was not found in the UniProt database."
565;PBAF complex (Polybromo- and BAF containing complex); SWI/SNF complex B;Human;O96019,Q68CP9,Q86U86,P51532,Q12824,Q92922,Q8TAQ2,Q969G3,(Q96GM5,Q92925,Q6STE5);86,196528,55193,6597,6598,6599,6601,6605,(6602,6603,6604);MI:0226- ion exchange chromatography | MI:0004- affinity chromatography technologies;8895581;10.01.09.05,11.02.03.04.01,16.03.01,30.01.09.08,30.01.11,42.10.03,70.10.03;"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome.";"";"At the time of annotation, the additional member BAF110 of the protein complex was not found in the UniProt database."
566;BAF complex; SWI/SNF complex A;Human;P60709,O96019,O14497,P51532,Q12824,Q92922,Q8TAQ2,Q969G3,(Q96GM5,Q92925,Q6STE5);60,86,8289,6597,6598,6599,6601,6605,(6602,6603,6604);MI:0006- anti bait coimmunoprecipitation;9845365;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10;"Beta-actin and BAF53 directly interact with BRG1 in the BAF complex. The actin subunit is required for optimal ATPase activity of BRG1.";"";""
567;Clathrin-CAP-1A-Na(v)1.8 channel complex;;Rat;Q8CJ99,Q62968,(P08081,P08082,P11442);266809,29571,(83800,116561,54241);MI:0096- pull down;15797711;14.04,18.02.10,20.09.18.09.01,73.03.13;"The interaction of CAP-1A with Nav1.8 C-terminus recruits clathrin to the protein complex.";"";""
568;Nuclear pore complex;;Rat;Q9NRG9,P57740,Q8WUM0,P49791,P37199,Q12769,Q5RJY5,Q92621,P35658,Q68FY1,Q8NFH4,Q8NFH3,O08587,P70582,P17955,Q9BW27,O08658,Q66HC5,P52948,P70581,O15504,P52591,P11654,Q3SWS8,P49792,P55735,Q96EE3,P12270;8086,57122,55746,25281,117021,23279,366016,23165,8021,295692,79023,348995,25497,53372,65274,79902,113929,291874,4928,245922,11097,113975,58958,362281,5903,6396,81929,7175;MI:0069- mass spectrometry studies of complexes | MI:0028- cosedimentation in solution;12196509;20.01.10,20.01.21,20.03.01.05,20.09.01,70.10.05;"All trafficking of macromolecules between the cytoplasm and the nucleus occurs through nuclear pore complexes (NPCs), which are supramolecular assemblies at points of fusion between the inner and outer nuclear membranes. NPCs are composed of an eightfold symmetric spoke-ring complex, cytoplasmic fibers, and a nuclear basket. ";"";"Since several proteins from rat were not available in the UniProt database at the time of annotation, the orthologous human proteins were used. In rat, the nuclear pore complex contains two different isoforms of NUPL1. Human isoform p45 has not yet been isolated. Isoforms of NUP98 are autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively."
569;PSD95-Nos1-Grin2b complex;;Rat;P31016,Q00960,P29476;29495,24410,24598;MI:0096- pull down | MI:0018- two hybrid;10488080;14.01,73.03.13,77.03.01.01.01;"The mechanism for the assembly of this ternary complex depends on a PDZ-PDZ interaction between PSD-95 and nNOS that is mechanistically distinct from PDZ-peptide interactions in that the tertiary structure of both domains is important.";"";""
570;p300-CBP-p270-SWI/SNF complex;;Human;O14497,Q92793,Q09472,P51532,Q12824,Q92922,Q8TAQ2;8289,1387,2033,6597,6598,6599,6601;MI:0006- anti bait coimmunoprecipitation;9584200;10.01.09.05,11.02.03.04.01,14.07.04,16.03.01,42.10.03,70.10.03;"";"";"Several other, not further characterized members of the complex have been isolated: p75,p71,p64,p59 and p50."
571;p300-CBP-p270 complex;;Human;O14497,Q92793,Q09472;8289,1387,2033;MI:0006- anti bait coimmunoprecipitation;8995708;11.02.03.04.01,16.03.01,70.10;"";"";""
572;PYR complex; Ikaros containing chromatin remodeling complex;Mouse;Q6PDQ2,P70288,P63158,Q03267,Q60973,Q9Z0H3,P97496,Q6PDG5,Q61466,O54941,(P60710,P63260),(Q9Z2N8,Q99MR0);107932,15182,15289,22778,245688,20587,20588,68094,83797,57376,(11461,11465),(56456,83766);MI:0091- chromatography technologies | MI:0004- affinity chromatography technologies;11003653;10.01.09.05,11.02.03.04,14.07.04,16.03.01,41.05.04,42.10.03,43.03.07,70.10,73.03.07.01;"Ikaros targets two types of chromatin-remodeling factors-activators (SWI/SNF) and repressors (NuRD)-in a single complex (PYR complex) to the beta-globin locus in adult erythroid cells.";"";""
574;F1-ATP synthase (EC 3.6.3.14) -  IF1 (inhibitor protein)  complex, mitochondrial; Complex V (F1-ATPase-IF1 subunit) |;Bovine;P19483,P00829,P05631,P05630,P05632,P01096;282578,327675,327668,338081,617230,327699;MI:0114- x-ray crystallography;12923572;01.04,02.13.03,02.45.15,16.01,16.19.03,70.16.05,75.03.12.03;"F1F0 ATPase is the fifth complex in the respiratory chain. The mammalian complex V consists of 16 different subunits with alpha(3), beta(3), gamma, delta and epsilon comprising the F1 part and a, b, c, d, e, f, g, A6L, OSCP, and coupling factor 6 providing the F0 and stator. Also associated in the complex under some conditions is an intrinsic inhibitor protein IF1.";"";""
575;ABIN2-NFKB1-MAP3K8 complex;;Human;P41279,P19838,Q8NFZ5;1326,4790,79155;MI:0096- pull down;15169888;14.01,16.01,30.01.05.01;"The optimal TPL-2 stability in vivo requires interaction with ABIN-2 as well as p105. Together, these data raise the possibility that ABIN-2 functions in the TLR4 signaling pathway which regulates TPL-2 activation.";"";""
576;F1F0-ATP synthase (EC 3.6.3.14), mitochondrial; Complex V | F1F0 ATPase;Bovine;P19483,P00829,P05631,P05630,P05632,P13619,P32876,P13620,Q00361,P02721,P13621,P01096,P00847,P03929;282578,327675,327668,338081,617230,282701,338053,282710,338040,282690,281640,327699,3283882,3283881;MI:0114- x-ray crystallography | MI:0226- ion exchange chromatography;8240295;01.04,02.13.03,02.45.15,16.19.03,70.16.05,75.03.12.03;"F1F0 ATPase is the fifth complex in the respiratory chain. The mammalian complex V consists of 16 different subunits with alpha(3), beta(3), gamma, delta and epsilon comprising the F1 part and a, b, c, d, e, f, g, A6L, OSCP, and coupling factor 6 providing the F0 and stator. Also associated in the complex under some conditions is an intrinsic inhibitor protein IF1.";"";""
577;FHL2-p53-HIPK2 complex;;Human;Q14192,Q9H2X6,P04637;2274,28996,7157;MI:0019- coimmunoprecipitation;16343438;11.02.03.04,16.01,18.02,70.10;"";"";""
578;PYR complex;;Mouse;Q9Z0H3,Q6PDG5,Q61466,O54941;20587,68094,83797,57376;MI:0091- chromatography technologies | MI:0004- affinity chromatography technologies | MI:0412- electrophoretic mobility supershift assay;9892636;10.01.09.05,11.02.03.04,14.07.04,16.03.01,41.05.04,42.10.03,43.03.07,70.10,73.03.07.01;"This complex is restricted to definitive (adult-type) hematopoietic cells and specifically binds DNA sequences containing long stretches of pyrimidines.";"";""
579;Epo-R-PLC-gamma-TRPC2 complex;;Mouse;P14753,Q62077,Q9R244;13857,18803,22064;MI:0019- coimmunoprecipitation;15329338;20.01.01.01,20.03.01,70.02,73.03.07;"PLC is involved in Epo-modulated Ca 2+ influx through TRPC2.";"";""
580;Epo-R-IP(3)R type II-TRPC2 complex;;Mouse;P14753,Q9Z329,Q9R244;13857,16439,22064;MI:0019- coimmunoprecipitation;15329338;20.01.01.01,20.03.01,70.02;"Mutant analysis data demonstrates a requirement for IP(3)R binding domains in Epo-modulated Ca 2+ influx through TRPC2.";"";""
581;Epo-R-PLC-gamma 1-IP(3)R type II-TRPC2 signaling complex;;Mouse;P14753,Q9Z329,Q62077,Q9R244;13857,16439,18803,22064;MI:0019- coimmunoprecipitation;15329338;20.01.01.01,20.03.01,70.02;"The experiments support the conclusion that after Epo stimulation, PLC-gamma activation produces IP3, which activates IP3R, and IP3R interaction with TRPC2 contributes to and is required for channel opening.";"";""
582;Ikaros complex; 2 MD complex;Mouse;Q6PDQ2,O09106,P70288,Q03267,P81183,O08900,Q60972,Q3TKT4,P97496,Q61466,Q99JR8,Q6P9Z1;107932,433759,15182,22778,22779,22780,19646,20586,20588,83797,83796,66993;MI:0007- anti tag coimmunoprecipitation;10204490;01.03,10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,43.03.07.02.01.02,70.10,73.03.07.02.01.02;"";"";"At the time of annotation, the additional member of the protein complex, Ikaros isoform 7, was not found in the UniProt database."
583;Ikaros-NuRD complex;;Mouse;Q6PDQ2,O09106,P70288,Q03267,P81183,O08900;107932,433759,15182,22778,22779,22780;MI:0071- molecular sieving | MI:0007- anti tag coimmunoprecipitation;10204490;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,43.03.07.02.01.02,70.10,73.03.07.02.01.02;"";"";"At the time of annotation, the additional member of the protein complex, Ikaros isoform 7, was not found in the UniProt database."
584;Ppp3cb-RyR2-mAkap complex;;Rat;Q9WVC7,P20651,O08661;64553,24675,689560;MI:0019- coimmunoprecipitation;16306226;11.02.03.04,20.01.01.01,20.03.01.01,30.01.09.03,30.01.09.07,41.05.15,75.03.12.03;"RyR and CaN activities are important for the induction of cellular hypertrophy by beta-adrenergic receptor signaling. The results show a novel function of the mAKAP complex involving the integration of cAMP and Ca2+ signals that promote myocyte hypertrophy.";"mAKAP complex is involved in adrenergic-induced cardiac hypertrophy.";""
585;Mi2/NuRD-BCL6-MTA3 complex;;Human;P41182,Q14839,Q13547,O95983,Q9BTC8;604,1108,3065,53615,57504;MI:0006- anti bait coimmunoprecipitation;15454082;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,43.03.07.02.01.01,70.10,77.03.05.03;"";"";""
586;Ccnb1-Itpr1-Cdc2 signaling complex;;Rat;P30277,P39951,P29994;25203,54237,25262;MI:0019- coimmunoprecipitation;16237118;10.03.01,14.07.03,30.01.09.03,34.01.01.01;"The interaction between IP3R1 and CyB/cdc2 can be seen only in PHA-stimulated cells.";"";""
587;NuRD.1 complex; nucleosome remodeling and histone deacetylation complex;Human;Q14839,Q6IT96,Q92769,O95983,Q13330,Q9BTC8,Q09028,Q16576;1108,3065,3066,53615,9112,57504,5928,5931;MI:0091- chromatography technologies | MI:0004- affinity chromatography technologies;9885572;10.01.09.05,11.02.03.04.03,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"";"";"Several other subunits of the complex were found in the analysis, which have not been further characterized: N190, N170, N160, N140, N135, N130, N85, N75, N68, N66, N38."
588;Respiratory chain supercomplex (complex I, III, IV), mitochondrial, heart; Respirasome;Bovine;P00423,P00426,P00428,P13182,P00429,P04038,P13184,P13183,P00430,P10175,P00125,P00396,P68530,P00415,P00157,P03887,P03892,P03898,P03910,P03902,P03920,P03924,Q02377,P34942,Q8HXG6,O97725,Q95KV7,Q02370,Q02371,Q01321,P23935,Q02366,Q05752,P42029,P34943,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369,Q02376,Q02827,P15690,P17694,P23709,Q02375,Q02379,P23934,P42026,P42028,P25708,P04394,P25712,P07552,P00130,P00129,P31800,P23004,P13272,P00126,P13271;281090,444878,287012,282199,100270792,782486,327688,327674,327718,615757,512500,0,3283880,0,3283889,0,0,3283884,3283886,3283885,0,3283888,327673,338060,326346,281742,338084,327698,338064,327704,327714,327670,338063,327710,404188,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660,282289,338046,288380,327697,287327,327680,338057,327691,338079,287027,287014,282290,327717,281570,616109,616871,282393,282394,287020,613899,286885;MI:0276- blue native page;10775262;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. The complete respiratory chain supercomplex consists of: 1: complex I = NADH dehydrogenase, mitochondrial 2: complex III = bc1-complex, mitochondrial 3: complex IV = cytochrome c oxidase, mitochondrial The stoichiometric association of complexes within the supercomplex varies: complex I was found as monomer, complex III was found as dimer, complex IV was absent or present as monomer, dimer, or trimer- PMID:16782043 predicts the following supercomplex model: complex I: monomer complex II: dimer complex IV: tetramer Additionally the authors present a model for a higher supramolecular association of respirasomes into a "respiratory string".";"";""
589;Respiratory chain supercomplex (complex I, III, IV), mitochondrial, heart; Respirasome;Bovine;P00423,P00426,P00428,P13182,P00429,P04038,P13184,P13183,P00430,P10175,P00125,P00396,P68530,P00415,P00157,P03887,P03892,P03898,P03910,P03902,P03920,P03924,Q02377,P34942,Q8HXG6,O97725,Q95KV7,Q02370,Q02371,Q01321,P23935,Q02366,Q05752,P42029,P34943,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369,Q02376,Q02827,P15690,P17694,P23709,Q02375,Q02379,P23934,P42026,P42028,P25708,P04394,P25712,P07552,P00130,P00129,P31800,P23004,P13272,P00126,P13271;281090,444878,287012,282199,100270792,782486,327688,327674,327718,615757,512500,0,3283880,0,3283889,0,0,3283884,3283886,3283885,0,3283888,327673,338060,326346,281742,338084,327698,338064,327704,327714,327670,338063,327710,404188,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660,282289,338046,288380,327697,287327,327680,338057,327691,338079,287027,287014,282290,327717,281570,616109,616871,282393,282394,287020,613899,286885;MI:0040- electron microscopy;16551638;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"The complete respiratory chain supercomplex consists of: 1: complex I = NADH dehydrogenase, mitochondrial 2: complex III = bc1-complex, mitochondrial 3: complex IV = cytochrome c oxidase, mitochondrial Stoichiometric association of complexes within the supercomplex: complex I = monomer, complex III = dimer, complex IV = monomer- PMID:16782043 predicts the following supercomplex model: complex I: monomer complex II: dimer complex IV: tetramer Additionally the authors present a model for a higher supramolecular association of respirasomes into a "respiratory string".";"";""
590;Kv4.2-KChIP3-Dpp10 channel complex;;Rat;Q6Q629,Q63881,Q9JM47;363972,65180,65199;MI:0019- coimmunoprecipitation;16123112;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"Analysis done in heterologously expressing Xenopus oocytes show, that when Kv4.2 is not coexpressed, DPP10 and KChIP3 don't associate with each other.";"";""
591;SAP complex (Sin3-associated protein complex);;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,Q9H0E3,O75446,Q96ST3;51742,3065,3066,5928,5931,79595,8819,25942;MI:0004- affinity chromatography technologies;9885572;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03,70.10;"";"";"In PMID:12724404, SAP45 has been identified as an additional member of the complex."
592;SAP complex (Sin3-associated protein complex); mSin3A corepressor complex;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,Q9H0E3,O75446,Q96ST3,Q9H7L9;51742,3065,3066,5928,5931,79595,8819,25942,64426;MI:0006- anti bait coimmunoprecipitation | MI:0091- chromatography technologies | MI:0004- affinity chromatography technologies;12724404;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03,70.10;"";"";"SAP45 has been newly identified as a member of the SAP complex. Two other subunits of the complex were found in the analysis, which have not been further characterized: SAP38, SAP28."
593;Kv4.2-Dpp10 channel complex;;Rat;Q6Q629,Q63881;363972,65180;MI:0019- coimmunoprecipitation;15671030;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02,77.03.01.01.01;"The results distinguish DPPX and DPP10 as a functional DPP subfamily able to effectively traffic and modulate Kv4 channels, a unique property within the larger DPPIV-like class of proteins.";"";""
594;Kv4.2-DPPX channel complex;;Rat;P46101,Q63881;29272,65180;MI:0019- coimmunoprecipitation;15671030;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02,77.03.01.01.01;"The results distinguish DPPX and DPP10 as a functional DPP subfamily able to effectively traffic and modulate Kv4 channels, a unique property within the larger DPPIV-like class of proteins.";"";""
595;Kv4.2-DPP10 channel complex;;Human;Q8N608,Q9NZV8;57628,3751;MI:0019- coimmunoprecipitation;15454437;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"This study shows that, similar to DPP6, DPP10 may play a critical part in the assembly of the Kv4 macromolecular complex in the brain and modulate its function.";"";""
596;SIN3-HDAC-SAP30-ARID4 complex;;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,O75446,Q96ST3;51742,3065,3066,5928,5931,8819,25942;MI:0006- anti bait coimmunoprecipitation | MI:0004- affinity chromatography technologies;11283269;10.01.09.05,10.03.01.02,11.02.03.04.03,14.07.04,42.10.03,70.10;"RBP1 associates with mSIN3-HDAC complex.";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: SAP38, SAP28."
597;Cx43/Gja1-Tom20-Hsp90ab complex;;Rat;P08050,P34058,Q62760;24392,301252,266601;MI:0019- coimmunoprecipitation;16741159;20.09.04,70.16.05;"Cx43 is transported to the inner mitochondrial membrane through translocation via the TOM complex. A normal mitochondrial Cx43 content is important for the diazoxide-related pathway of preconditioning. Its genetic depletion abolishes the protection of ischemia- and diazoxide-induced preconditioning.";"";""
598;Kv4.3-Dpp10 channel complex;;Rat;Q6Q629,Q62897;363972,65195;MI:0007- anti tag coimmunoprecipitation;15911355;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPPY(DPP10) also form homomers by themselves and heteromers with DPPX(DPP6) in the absence of Kv4 channels.";"";""
599;Kv4.3-Dpp6 channel complex;;Rat;P46101,Q62897;29272,65195;MI:0007- anti tag coimmunoprecipitation;15911355;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"DPPX (Dpp6) and DPPY preferentially form complexes with channel proteins in Kv4 family.";"";""
600;Kv4.1-Dpp6 channel complex;;Rat;P46101,Q03719;29272,16506;MI:0007- anti tag coimmunoprecipitation;15911355;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"DPPX (Dpp6) and DPPY preferentially form complexes with channel proteins in Kv4 family.";"";"Since Kcnd1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
601;Kv4.1-Dpp10 channel complex;;Rat;Q6Q629,Q03719;363972,16506;MI:0007- anti tag coimmunoprecipitation;15911355;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"DPPY(DPP10) also form homomers by themselves and heteromers with DPPX(DPP6) in the absence of Kv4 channels.";"";"Since Kcnd1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
602;Kv4.2-Dpp10 channel complex;;Rat;Q6Q629,Q63881;363972,65180;MI:0007- anti tag coimmunoprecipitation;15911355;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"DPPY(DPP10) also form homomers by themselves and heteromers with DPPX(DPP6) in the absence of Kv4 channels.";"";""
603;Kv4.2-Dpp6 channel complex;;Rat;P46101,Q63881;29272,65180;MI:0007- anti tag coimmunoprecipitation;15911355;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02;"DPPX (Dpp6) and DPPY preferentially form complexes with channel proteins in Kv4 family.";"";""
604;Kv4.2-DPPX-KChIP channel complex;;Rat;P46101,Q63881,(Q8R426,Q9JM59,Q9JM47,Q99MG9);29272,65180,(65023,56817,65199,259243);MI:0006- anti bait coimmunoprecipitation;12575952;14.04,18.02.10,20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"DPPX facilitates the intracellular trafficking of Kv4 proteins and drastically increases the surface expression of Kv4 channels.";"";""
605;TIM (TIMM17ab, TIMM23, TIMM44) complex, mitochondrial;;Human;Q99595,O60830,O14925,O43615;10440,10245,10431,10469;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;10339406;14.04,70.16.05;"Translocation of nuclear-encoded  mitochondrial preproteins is  mediated by translocases in the  outer (TOM) and inner (TIM)  membranes.";"";""
606;Kv4.2-Kchip1 channel complex;;Rat;Q63881,Q8R426;65180,65023;MI:0019- coimmunoprecipitation;15356203;20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.";"";""
607;Kv4.2-Kchip2 channel complex;;Rat;Q63881,Q9JM59;65180,56817;MI:0019- coimmunoprecipitation;15356203;20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.";"";""
608;Kv4.2-Kchip3 channel complex;;Rat;Q63881,Q9JM47;65180,65199;MI:0019- coimmunoprecipitation;15356203;20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.";"";""
609;Kv4.2-Kv4.3 channel complex;;Rat;Q63881,Q62897;65180,65195;MI:0019- coimmunoprecipitation;15356203;20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"";"";""
610;MSL complex;;Human;Q7Z3B3,Q9HCI7,Q8N5Y2,Q9H7Z6;284058,55167,10943,84148;MI:0019- coimmunoprecipitation;16227571;10.01.09.05,14.07.04,70.10;"The authors found that reduction in the levels of hMSLs and acetylation of H4 at lysine 16 are correlated with reduced transcription of some genes and with a G2/M cell cycle arrest.";"";""
611;Exocyst complex;Sec6/8 complex;Rat;Q8R3S6,O54921,Q62825,Q62824,P97878,O54923,O54922,O54924;69940,171455,252881,116654,60627,50556,64632,245709;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;8982167;16.01,20.01.10,20.09.16.09.03,70.02;"The exocyst is a conserved eight-subunit complex involved in the docking of exocytic vesicles. It is thought to be involved in directing vesicles to their precise sites of fusion. The exocyst is regulated by many small GTPases, including members of the Rab, Rho and Ral families. ";"";"Since Exoc1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
612;CTF18-CTF8-DCC1 complex;;Human;Q8WVB6,Q8WV66,Q9BVC3;63922,54921,79075;MI:0019- coimmunoprecipitation;12766176;10.03,10.03.04.05,70.10;"This complex is required for sister chromatid cohesion and loads proliferating cell nuclear antigen onto DNA (PMID:12930902).";"";""
613;CTF18-CTF8-DCC1-RFC3 complex;;Human;Q8WVB6,Q8WV66,Q9BVC3,P40938;63922,54921,79075,5983;MI:0019- coimmunoprecipitation;12766176;16.01,70.10;"";"";""
614;NRD complex (Nucleosome remodeling and deacetylation complex);;Human;O60341,Q12873,Q14839,Q13547,Q92769,Q13330,Q09028;23028,1107,1108,3065,3066,9112,5928;MI:0006- anti bait coimmunoprecipitation;9804427;10.01.09.05,11.02.03.04,14.07.04,42.10.03,70.10;"";"";""
615;Ubiquitin E3 ligase (SKP1A, SKP2, CUL1);;Human;Q13616,P63208,Q13309;8454,6500,6502;MI:0019- coimmunoprecipitation;9736735;10.03.01.01.03,14.07.05,14.13.01.01,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin D proteins.";"";""
616;TIM (Timm17a, Timm23, Timm44, Hsp70) complex, mitochondrial;;Rat;P55063,O35092,O35093,O35094;24963,54311,54312,29635;MI:0019- coimmunoprecipitation;9538267;14.04,70.16.05;"Translocation of nuclear-encoded  mitochondrial preproteins is  mediated by translocases in the  outer (TOM) and inner (TIM)  membranes.";"";""
617;CASK-LIN7C-APBA1 complex;;Human;Q02410,O14936,Q9NUP9;320,8573,55327;MI:0019- coimmunoprecipitation;9822620;14.04,14.07.01,77.03.01.01.01;"This complex may play an important role in the trafficking and processing of APP in neurons.";"";""
618;MRN complex (MRE11-RAD50-NBN complex);;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0004- affinity chromatography technologies;16163361;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"The MRN complex functions as an essential guardian of genome integrity by directing the proper processing of DNA ends, including DNA breaks.";"";""
619;MRE11A-RAD50-NBN-TRF2 complex;;Human;P49959,O60934,Q92878,Q15554;4361,4683,10111,7014;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;10888888;10.03.01.03,16.03.01,42.10.03,70.10.03;"Several experiments indicate that TRF2 is not involved in DSB repair. RAD50-MRE11-NBS1 complex functions at telomeres, possibly by modulating t-loop formation.";"";""
620;CoREST-HDAC complex;;Human;O60341,Q13547,Q92769,Q9P0W2,Q96BD5,Q9UKL0,O75362;23028,3065,3066,10362,51317,23186,7764;MI:0006- anti bait coimmunoprecipitation;11171972;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"";"";"RbAp46 and RbAp48 were not identified in this complex, although these proteins have been observed in all previously identified complexes and are thought to be part of an HDAC1/2 core."
621;AKAP250-PKA-PDE4D complex;;Human;Q02952,Q08499,(P17612,P22694,P22612);9590,5144,(5566,5567,5568);MI:0019- coimmunoprecipitation;16642035;14.04,18.01.03,18.02.01,30.01.09.07,70.02;"This complex localized cAMP-degrading enzyme activity to plasma membrane sites to generate transient cAMP changes in response to adenylyl cyclase activity. The authors don't show PKA in coimmunoprecipitation experiment but describe that PKA is acting through an association with PDE4.";"";""
622;Ubiquitin E3 ligase (VHL, TCEB1, TCEB2, CUL2);;Human;Q13617,Q15369,Q15370,P40337;8453,6921,6923,7428;MI:0019- coimmunoprecipitation | MI:0051- fluorescence technologies;9122164;14.07.05,14.13,70.03,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.";"";""
623;TIM (TIMM9, TIMM10) complex, mitochondrial;;Human;P62072,Q9Y5J7;26519,26520;MI:0040- electron microscopy;16387659;14.04,70.16.05;"Translocation of nuclear-encoded  mitochondrial preproteins is  mediated by translocases in the  outer (TOM) and inner (TIM)  membranes.";"";""
624;LSD1-CoREST complex;;Human;O60341,Q9UKL0;23028,23186;MI:0114- x-ray crystallography;16885027;10.01.09.05,11.02.03.04.03,14.07.09,42.10.03,70.10;"CoREST endows LSD1 with the ability to demethylate nucleosomal substrates and protects LSD1 from proteasomal degradation in vivo.";"";""
626;LSD1 complex;;Human;O60341,Q13363,Q13547,Q9NP66,Q9P0W2,P08107,Q96BD5,Q96EK2,Q9UKL0,Q9P2K3,Q92766,Q9UBW7,O75362;23028,1487,3065,10363,10362,3303,51317,112885,23186,55758,6239,7750,7764;MI:0004- affinity chromatography technologies;16140033;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,42.10.03,70.10;"CoREST positively regulates LSD1 function, while BHC80 inhibits CoREST/LSD1-mediated demethylation in vitro. These findings suggest that LSD1-mediated histone demethylation is regulated dynamically in vivo.";"";"Another subunit of the complex was found in the analysis, which has not been further characterized: Y182."
627;MRN-TRRAP complex (MRE11A-RAD50-NBN-TRRAP complex);;Human;P49959,O60934,Q92878,Q9Y4A5;4361,4683,10111,8295;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;16382133;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"TRRAP-depleted extracts show a reduced nonhomologous DNA end-joining activity in vitro. TRRAP may function as a molecular link between DSB signaling, repair, and chromatin remodeling.";"";""
628;SNARE complex (Stx, Stx8, Vti1b, VAMP8);;Rat;O70257,Q9Z2Q7,Q9WUF4,P58200;60466,59074,83730,366673;MI:0019- coimmunoprecipitation;11101518;16.01,20.01.10,20.09.07.27,20.09.16.09.05,70.02,70.22;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. This SNARE complex functions in the homotypic fusion of late endosomes, which is one step in the delivery of endocytosed material to lysosomes.";"";""
629;BLM-TRF2 complex;;Human;P54132,P62380;641,9519;MI:0019- coimmunoprecipitation | MI:0055- fluorescent resonance energy transfer;12444098;10.01.02,40.20,42.10.03;"";"BLM is involved in Bloom syndrome (BS).";"The results identify BLM as the first protein found to affect telomeric DNA synthesis specifically in human ALT immortalized cell lines. "
630;RyR2 macromolecular complex;;Rat;P97534,O08661,(P62138,P62142,P63088),(P63331,P62716),(P27791,P68182),(P12368,P12369);58950,689560,(24668,25594,24669),(24672,24673),(25636,293508),(29699,24679);MI:0019- coimmunoprecipitation;12401811;14.07.03,20.01.01.01,20.03.01.01,30.01.09.07,36.25.09.04,75.03.12.03;"This complex contains kinase and two phosphatases that are bound to the channel via targeting proteins. ";"The hyperphosphorylation of RyR2 by protein kinase A is general feature of heart failure.";""
631;Tacc1-chTOG-AuroraA  complex;;Human;O14965,Q14008,O75410;6790,9793,6867;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;14603251;10.03.05.01,12.07,70.10.04;"This complex could be involved in the regulation of mRNA translation, cell division in conjunction and microtubule organization. ";"This complex may be affected during mammary gland oncogenesis.";""
632;Anti-HDAC2 complex;;Human;O60341,Q12873,Q14839,Q14687,P78347,Q13547,Q92769,Q9P0W2,Q13330,O94776,Q96BD5,Q09028,Q16576,Q9UKL0,Q9UBW7,Q14202,(Q96ST3,O75182);23028,1107,1108,23199,2969,3065,3066,10362,9112,9219,51317,5928,5931,23186,7750,9203,(25942,23309);MI:0006- anti bait coimmunoprecipitation | MI:0091- chromatography technologies;12493763;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"";"XFIM (ZMYM3) is involved in X-linked mental retardation.";""
633;anti-BHC110 complex;;Human;O60341,Q14687,P78347,Q13547,Q92769,Q9P0W2,Q96BD5,Q9UKL0,Q9UBW7,Q14202,O75362;23028,23199,2969,3065,3066,10362,51317,23186,7750,9203,7764;MI:0006- anti bait coimmunoprecipitation | MI:0091- chromatography technologies;12493763;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"";"XFIM (ZMYM3) is involved in X-linked mental retardation.";""
634;XFIM complex;;Human;O60341,P78347,Q13547,Q92769,Q14202;23028,2969,3065,3066,9203;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving;12493763;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,70.10;"";"XFIM (ZMYM3) is involved in X-linked mental retardation.";""
635;AGPS-GNPAT complex;;Human;O00116,O15228;8540,8443;MI:0030- cross-linking studies;10215861;01.06,70.19;"";"";""
636;BHC complex;BRAF-histone deacetylase complex, BRAF-HDAC complex;Human;O60341,Q13547,Q92769,Q9P0W2,Q96BD5,Q9UKL0;23028,3065,3066,10362,51317,23186;MI:0004- affinity chromatography technologies | MI:0091- chromatography technologies | MI:0007- anti tag coimmunoprecipitation | MI:0006- anti bait coimmunoprecipitation;12032298;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,43.03.13,70.10;"The BHC complex mediates repression of neuron-specific genes.";"";""
638;cGMP kinase signaling complex (IP3RI, IRAG, cGKI-beta);;Bovine;Q9TU34,Q9N1F0,P21136;317697,281918,282004;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;10724174;14.07.03,20.01.01.01,30.01.09.07,34.01.01.01,70.02,70.07,75.03.12.02;"The results identify IRAG as an essential NO/cGKI-dependent regulator of IP3-induced calcium release.";"";""
639;RANBPM-Muskelin-TWA1-HSMpp8 complex;;Human;Q9NWU2,Q9UL63,Q99549,Q96S59;54994,4289,54737,10048;MI:0071- molecular sieving | MI:0019- coimmunoprecipitation;12559565;16.01,42.04.05,70.03;"This complex might play a role  in RanGTPase cycle.";"";""
640;SNARE complex (Snap47, Stx1a, Vamp2);;Rat;Q6P6S0,P32851,P63045;303183,116470,24803;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients;16621800;16.01,20.09.07.27,20.09.16.09.05,70.02;"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane.  In vitro, the SNARE complex consisting of Snap47, syntaxin 1a and VAMP-2 was shown to catalyze the fusion of proteoliposomes.";"";""
641;RANBPM-SMP1 complex;;Human;Q96S59,O95807;10048,23585;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0096- pull down;15014887;41.05.25,70.03;"This complex may be involved in the process of male germ cell differentiation.";"";""
642;CtBP complex;;Human;O60341,O00257,Q9Y232,Q13363,P56545,Q9H9B1,Q96KQ7,Q13547,Q92769,Q96JN0,Q9UKL0,Q9P2K3,Q92766,P37275,O60315,O75362,Q92618;23028,8535,9425,1487,1488,79813,10919,3065,3066,84458,23186,55758,6239,6935,9839,7764,9658;MI:0007- anti tag coimmunoprecipitation;12700765;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"";"CtBP is implicated in tumorigenesis.";""
643;CtBP core complex;;Human;O60341,Q13363,P56545,Q9H9B1,Q96KQ7,Q13547,Q92769,Q9UKL0,P37275;23028,1487,1488,79813,10919,3065,3066,23186,6935;MI:0029- cosedimentation through density gradients | MI:0071- molecular sieving;12700765;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"";"CtBP is implicated in tumorigenesis.";""
644;ASPP1-SAM68 complex;;Human;Q07666,Q96KQ4;10657,23368;MI:0018- two hybrid;16474851;11.04.03.01,70.10;"The authors suggest that the interaction of ASPP1 with nuclear SAM68 is spatially restricted to human spermatogenesis.";"";""
646;HDAC1-associated protein complex;;Human;O60341,Q12873,Q13547,Q9UBB5,O95983,O94776,Q09028,Q16576,Q9UKL0;23028,1107,3065,8932,53615,9219,5928,5931,23186;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;11102443;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"";"";""
647;HPFH(-198) complex;;Mouse;P13864,Q3THK3,O70422,Q96FH6;13433,98053,14885,3047;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes;17114178;11.02.03.04,70.10;"Described complex contains Britisch HPFH mutant carrying a T->C point mutation. ";"";"Since Hbg1 from mouse was not available in the UniProt database at the time of annotation, the orthologous protein from human was used."
648;HDAC1-associated core complex cI;;Human;O60341,Q13547,Q9UKL0;23028,3065,23186;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11102443;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"";"";"Another subunit of the complex was found in the analysis, which has not been further characterized: p37."
649;HDAC1-associated core complex cII;;Human;Q12873,Q13547,Q9UBB5,O95983,O94776,Q09028,Q16576,Q9UKL0,(Q86YP4,Q8WXI9);1107,3065,8932,53615,9219,5928,5931,23186,(54815,57459);MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11102443;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"";"";""
650;HDAC2-asscociated core complex;;Human;Q12873,Q92769,O95983,O94776,Q09028,Q16576,(Q86YP4,Q8WXI9);1107,3066,53615,9219,5928,5931,(54815,57459);MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;11102443;10.01.09.05,11.02.03.04.03,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"";"";""
651;SNARE complex (Snap25, Stx1a, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0091- chromatography technologies;9177194;16.01,20.09.07.27,20.09.16.09.05,70.02;"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane.";"";""
652;AP3-BLOC1 complex;;Human;O00203,Q13367,O14617,Q9Y2T2,P53677,Q92572,P59780,P78537,Q6QNY1,Q6QNY0,Q9NUP1,Q96EV8,Q8TDH9,Q9UL45,O95295;8546,8120,8943,26985,10947,1176,10239,2647,282991,388552,55330,84062,63915,26258,23557;MI:0019- coimmunoprecipitation;16837549;14.04,42.02;"BLOC-1 interacts physically and functionally with AP-3 to facilitate the trafficking of a known AP-3 cargo.";"";""
653;SNARE complex (Ykt6, Stx5, Gosr2, Bet1);;Rat;Q62896,O35165,Q08851,Q5EGY4;29631,64154,65134,64351;MI:0019- coimmunoprecipitation;12589064;16.01,20.09.07.27,20.09.16.09.05,70.02;"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane. Ykt6 was found to be selectively expressed in brain neurons.";"";""
654;BLOC1-BLOC2 complex;;Human;P78537,Q6QNY1,Q6QNY0,Q9NUP1,Q96EV8,Q969F9,Q9UPZ3,Q86YV9,Q8TDH9,Q9UL45,O95295;2647,282991,388552,55330,84062,84343,11234,79803,63915,26258,23557;MI:0019- coimmunoprecipitation;16837549;14.04,70.22;"BLOC-1 interacts with BLOC-2 to facilitate Tyrp1 trafficking by a mechanism apparently independent of AP-3 function.";"";""
655;HSF1-HSF2 complex;;Human;Q00613,Q03933;3297,3298;MI:0019- coimmunoprecipitation;16336210;16.01;"";"";""
656;VPS35-VPS29-VPS26A complex;;Human;O75436,Q9UBQ0,Q96QK1;9559,51699,55737;MI:0019- coimmunoprecipitation;11102511;14.04;"";"";""
657;Retromer complex (SNX1, SNX2, VPS35, VPS29, VPS26A);;Human;Q13596,O60749,O75436,Q9UBQ0,Q96QK1;6642,6643,9559,51699,55737;MI:0019- coimmunoprecipitation | MI:0018- two hybrid | MI:0051- fluorescence technologies;16732284;14.04,20.09.07,20.09.07.29;"";"";""
658;SNARE complex (Sec22b, Stx5, Gosr2, Bet1);;Rat;Q62896,O35165,Q4KM74,Q08851;29631,64154,310710,65134;MI:0019- coimmunoprecipitation;11035026;16.01,20.09.07.27,20.09.16.09.05,70.02;"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane.";"";""
659;MeCP1 complex; Mi2/NuRD-MBD2 complex;Human;Q14839,Q8WXI9,Q13547,Q92769,Q9UBB5,O95983,O94776,Q09028,Q16576;1108,57459,3065,3066,8932,53615,9219,5928,5931;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;11297506;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,16.03.01,42.10.03,70.10;"MeCP1 protein complex represses transcription through preferential binding, remodeling, and deacetylation of methylated nucleosomes. ";"CHD4 is involved in dermatomyositis (PMID:9790534).";""
660;TIM (TIMM23, TIMM50) complex, mitochondrial;;Human;O14925,Q3ZCQ8;10431,92609;MI:0019- coimmunoprecipitation;15044455;14.04,70.16.05;"Translocation of nuclear-encoded  mitochondrial preproteins is  mediated by translocases in the  outer (TOM) and inner (TIM)  membranes.";"";""
661;Karyopherin complex;;Rat;P83953,P52296,P25961;288064,24917,56813;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;16574786;20.09.01;"";"";""
662;Hoxa9-PBX2-Meis1 complex;;Mammalia;P09631,Q60954,P40425;15405,17268,5089;MI:0019- coimmunoprecipitation;10082572;16.03.01,43.03.07,70.10;"";"Hoxa9, PBX2 and Meis1 are associated with leukemias.";""
663;SNARE complex (Stx5, Ykt6, Gosr1, Bet1);;Rat;O35152,Q62931,Q08851,Q5EGY4;54400,94189,65134,64351;MI:0019- coimmunoprecipitation;14742712;16.01,20.01.10,20.09.07.05,20.09.07.27,20.09.16.09.05,70.08,70.22;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
664;SNARE complex (Stx5, Gosr2, Sec22b, Bet1);;Rat;Q62896,O35165,Q4KM74,Q08851;29631,64154,310710,65134;MI:0019- coimmunoprecipitation;14742712;16.01,20.01.10,20.09.07.05,20.09.07.27,20.09.16.09.05,70.08,70.22;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
665;BKCA alpha-Cav1.2 channel complex;;Rat;P22002,Q62976;24239,83731;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;17068255;20.01.01.01,20.03.01.01,34.03,70.02,77.03.01.01;"BKCa-Cav complexes reconstitute a functional "Ca(2+) nanodomain" where Ca(2+) influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics.";"";""
666;BKCA alpha-Cav2.1 channel complex;;Rat;P54282,Q62976;25398,83731;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;17068255;20.01.01.01,20.03.01.01,34.03,70.02,77.03.01.01;"BKCa-Cav complexes reconstitute a functional "Ca(2+) nanodomain" where Ca(2+) influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics.";"";""
667;BKCA alpha-Cav2.2 channel complex;;Rat;Q02294,Q62976;257648,83731;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;17068255;20.01.01.01,20.03.01.01,34.03,70.02,77.03.01.01;"BKCa-Cav complexes reconstitute a functional "Ca(2+) nanodomain" where Ca(2+) influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics.";"";""
668;BKCA-beta2AR-AKAP79 signaling complex;;Human;P07550,P24588,Q12791;154,9495,3778;MI:0019- coimmunoprecipitation;15141163;20.01.01.01,20.03.01.01,30.05.02.24,34.03,36.25.09.01;"BKCa is preferentially regulated by beta2AR within the channel macromolecular complex. Only expression of all three components of the complex reconstituted full-beta2 agonist modulation of the channel.  The ability of beta2AR to form a complex with BKCa, and concomitantly bind phosphorylation-modulatory components (AKAP79/150) enables specific and local regulation of BKCa channels and defines a signal transduction pathway governing cellular excitability in diverse tissues.";"";""
669;beta2AR-AKAP79/150  complex;;Rat;P10608,P24587;24176,171026;MI:0019- coimmunoprecipitation;15141163;20.01.01.01,20.03.01.01,30.05.02.24,34.03,77.03.01.01.01;"Beta2AR constitutively recruits AKAP79, which enables the targeting of AKAP79 to the channel (PMID:10753752). AKAP79 associates with beta2AR via the third intracellular loop and the C-terminus independently (PMID:10753752).";"";""
670;BKCa-AKAP79/150 complex;;Rat;P24587,Q62976;171026,83731;MI:0019- coimmunoprecipitation;15141163;20.01.01.01,20.03.01.01,30.05.02.24,34.03,77.03.01.01.01;"";"";""
671;BKCa-beta2AR complex;;Rat;P10608,Q62976;24176,83731;MI:0019- coimmunoprecipitation;15141163;20.01.01.01,20.03.01.01,30.05.02.24,34.03,75.03.12.02,77.03.01.01.01;"";"";""
672;BKCA-beta2AR complex;;Human;P07550,Q12791;154,3778;MI:0019- coimmunoprecipitation;15141163;20.01.01.01,20.03.01.01,30.05.02.24,34.03,75.03.12.02,77.03.09.01;"";"";""
673;SNARE complex (Stx5, p97, Nsfl1c);;Rat;O35987,Q08851,P46462;83809,65134,116643;MI:0040- electron microscopy;10930451;16.01,20.01.10,20.09.07.03,20.09.07.27,20.09.16.09.05,70.07,70.08;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The SNARE complex containing syntaxin5, p97 and p47 is involved in the regulation of the smooth domain of transitional ER and hence one of the earliest membrane differentiated components of the secretory pathway.";"";""
674;Gamma-secretase complex (Aph1a, Ncstn, Psen1, Psenen, Tmp21);;Mouse;Q8BVF7,P57716,P49769,Q9CQR7,Q9D1D4;226548,59287,19164,66340,68581;MI:0019- coimmunoprecipitation;16641999;18.02;"";"";""
675;TMP21-P24 complex;;Mouse;P97799,Q9D1D4;22360,68581;MI:0019- coimmunoprecipitation;16641999;20.09.07,70.07,70.08;"";"";""
676;Metallothionein-3 complex;;Mouse;P60710,Q04447,O08553,P11499,Q61696,P28184;11461,12709,12934,15516,193740,17751;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes;17018872;77.03.01.01.01;"";"";"Metallothionein-3 consists of 16 proteins but only five were identified."
677;Mt3-Hsp84-Ck complex;;Mouse;Q04447,P11499,P28184;12709,15516,17751;MI:0019- coimmunoprecipitation;17018872;77.03.01.01.01;"";"";""
678;GINS complex;;Human;Q14691,Q9Y248,Q9BRX5,Q9BRT9;9837,51659,64785,84296;MI:0019- coimmunoprecipitation;17170760;10.01.03.03,70.10;"This complex stimulates DNA polymerase alpha-primase.";"";""
679;Tis7-Sin3-Hdac1-Ncor1-Sap30 complex;;Mouse;O09106,P19182,Q60974,O88574,Q62141;433759,15982,20185,60406,20467;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;12198164;10.01.09.05,11.02.03.04.03,42.10.03,70.10;"";"";""
680;RANBMP-CD39 complex;;Human;P49961,P43487;953,5902;MI:0019- coimmunoprecipitation;16478441;18.02.01,70.02,73.03.07.02.01;"NTPDase activity of recombinant CD39, but not of N-terminus-deleted-CD39 mutant, is substantially diminished by RanBPM co-expression in COS-7 cells. CD39 associations with RanBPM have the potential to regulate NTPDase catalytic activity.";"";""
681;(C-CFTR)2-NHERF-ezrin complex;;Human;P13569,P15311,O14745;1080,7430,9368;MI:0019- coimmunoprecipitation | MI:0067- light scattering | MI:0071- molecular sieving | MI:0107- surface plasmon resonance;16129695;20.01.01.07.09,20.03.01.01,70.02,70.04,75.03.09;"Ezrin is a regulator that can positively control the cooperative binding of NHERF with the cytoplasmic domains of CFTR, thus modulating the stoichiometry of C-CFTR to NHERF interaction. The regulation of NHERF by ezrin may be employed as a general mechanism to assemble channels and receptors in the membrane cytoskeleton.";"CFTR is involved in cystic fibrosis (PMID:10811849).";""
682;C-CFTR-NHERF(PDZ1 domain)-ezrin complex;;Human;P13569,P15311,O14745;1080,7430,9368;MI:0019- coimmunoprecipitation | MI:0067- light scattering | MI:0071- molecular sieving | MI:0107- surface plasmon resonance;16129695;20.01.01.07.09,20.03.01.01,70.02,70.04,75.03.09;"There are two types of 1:1:1 ternary complexes formed between C-CFTR and NHERF·ezFERM. Gel filtration experiments show that the fraction eluted at 11.3 ml is a ternary complex with C-CFTR bound to the first PDZ domain of the binary NHERF·ezFERM complex. Ezrin is a regulator that can positively control the cooperative binding of NHERF with the cytoplasmic domains of CFTR, thus modulating the stoichiometry of C-CFTR to NHERF interaction. The regulation of NHERF by ezrin may be employed as a general mechanism to assemble channels and receptors in the membrane cytoskeleton.";"CFTR is involved in cystic fibrosis (PMID:10811849).";""
683;C-CFTR-NHERF(PDZ2 domain)-ezrin complex;;Human;P13569,P15311,O14745;1080,7430,9368;MI:0019- coimmunoprecipitation | MI:0067- light scattering | MI:0071- molecular sieving | MI:0107- surface plasmon resonance;16129695;20.01.01.07.09,20.03.01.01,70.02,70.04,75.03.09;"There are two types of 1:1:1 ternary complexes formed between C-CFTR and NHERF·ezFERM. Gel filtration experiments show that the fraction eluted at 11.9 ml is a ternary complex with C-CFTR bound to the second PDZ domain of the binary NHERF·ezFERM complex. Ezrin is a regulator that can positively control the cooperative binding of NHERF with the cytoplasmic domains of CFTR, thus modulating the stoichiometry of C-CFTR to NHERF interaction. The regulation of NHERF by ezrin may be employed as a general mechanism to assemble channels and receptors in the membrane cytoskeleton.";"CFTR is involved in cystic fibrosis (PMID:10811849).";""
684;PAX9-MSX1 complex;;Human;P28360,P55771;4487,5083;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;15721141;11.02.03.04,47.03.11.01;"";"PAX9 is involved  in tooth agenesis. The results indicate a functional relationship between Pax9 and Msx1 during tooth development.";""
685;MeCP1 complex; Mi2/NuRD-MBD2 complex;Human;Q14839,Q8WXI9,Q13547,Q92769,Q9UBB5,O95983,O94776,Q09028,Q16576;1108,57459,3065,3066,8932,53615,9219,5928,5931;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;11756549;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,16.03.01,42.10.03,70.10;"MeCP1 protein complex represses transcription through preferential binding, remodeling, and deacetylation of methylated nucleosomes. ";"CHD4 is involved in dermatomyositis (PMID:9790534).";""
686;Apg16L-Apg12-Apg5 complex;;Mouse;Q9CQY1,Q8C0J2,Q99J83;67526,77040,11793;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes | MI:0018- two hybrid | MI:0004- affinity chromatography technologies;12665549;14.13.04;"In conjunction with Apg12-Apg5, Apg16L associates with the autophagic isolation membrane for the duration of autophagosome formation.";"";""
687;CFTR-NHERF-beta(2)AR signaling complex;;Human;P07550,P13569,O14745;154,1080,9368;MI:0096- pull down | MI:0006- anti bait coimmunoprecipitation;12502786;20.01.01.07.09,20.03.01.01,30.05.02,70.02,75.03.09;"The results indicate that PDZ-based interactions with ezrin/radixin/moesin-binding phosphoprotein 50 (EBP50) govern both physical and functional regulation of CFTR by beta (2) AR. Assembly of the complex is regulated by PKA-dependent phosphorylation.";"CFTR is involved in cystic fibrosis (PMID:10811849).";""
688;Cd2ap-Fyn complex;;Mouse;Q9JLQ0,P39688;12488,14360;MI:0019- coimmunoprecipitation;16628251;16.01,77.03.07.01;"CD2AP associates with Fyn and Synpo but not with Neph1. The association of Fyn with CD2AP is probably mediated by the SH3 domain of Fyn binding to proline sequences in CD2AP. ";"Combinations of Cd2ap heterozygosity and heterozygosity Fyn proto-oncogene (Fyn) but not kin of IRRE like 1 (Neph1) resulted in spontaneous proteinuria and in FSGS-like glomerular damage.";""
690;Cd2ap-Synpo complex;;Mouse;Q9JLQ0,Q8CC35;12488,104027;MI:0006- anti bait coimmunoprecipitation;16628251;16.01,42.04;"The interaction between CD2AP and Synpo reinforces the idea that CD2AP plays a central role in regulating the actin cytoskeleton. CD2AP associates with Fyn and Synpo but not with Neph1.";"Combinations of Cd2ap heterozygosity and heterozygosity of synaptopodin (Synpo) but not kind of IRRE like 1 (Neph1) resulted in spontaneous proteinuria and in FSGS-like glomerular damage .";""
691;SIN3-SAP25 complex;;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,Q9H0E3,O00422,Q1EHW4,O75446,Q96ST3,Q9H7L9;51742,3065,3066,5928,5931,79595,10284,751865,8819,25942,64426;MI:0007- anti tag coimmunoprecipitation;16449650;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03,70.10;"";"";"Since human SAP25 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
692;LysRS-Hint-Mitf complex;;Rat;P62959,Q5XIM7,O88368;690660,292028,25094;MI:0091- chromatography technologies;14975237;11.02.03.04,16.01;"LysRS can play a key role via Ap4A as an important signaling molecule in MITF transcriptional activity.";"";""
693;TOM (Tomm70, Tomm20, Tomm22) complex, mitochondrial;;Rat;Q62760,Q75Q41,Q75Q39;266601,300075,304017;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;11956321;14.04,70.16.01;"Translocation of nuclear-encoded  mitochondrial preproteins is  mediated by translocases in the  outer (TOM) and inner (TIM)  membranes.";"";""
694;Bad-Gk-Wave1-Pkaca-Ppp1cc complex;;Mouse;Q3U9H3,P52792,Q3U7K1,P05132,Q8R5H6;12015,103988,19047,18747,83767;MI:0019- coimmunoprecipitation;12931191;02.01.03,40.10.02,70.16;"";"";""
695;SIN3-HDAC-SAP30-ARID4 complex; mSin3A corepressor complex;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,O75446,Q96ST3;51742,3065,3066,5928,5931,8819,25942;MI:0006- anti bait coimmunoprecipitation;12724404;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03,70.10;"";"";"Another subunit of the complex was found in the analysis, which has not been further characterized: SAP250."
696;BRMS1-SIN3-HDAC complex;;Human;Q9HCU9,Q13547,Q92769,Q09028,Q16576,O75446,Q96ST3,O75182;25855,3065,3066,5928,5931,8819,25942,23309;MI:0007- anti tag coimmunoprecipitation;14581478;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"BRMS1 may participate in transcriptional regulation via interaction with the Sin3-HDAC complex and suggest a novel mechanism by which BRMS1 might suppress cancer metastasis.";"";""
697;BRMS1-RBP1 complex;;Human;Q4LE39,Q9HCU9;51742,25855;MI:0007- anti tag coimmunoprecipitation;14581478;11.02.03.04.03,70.10;"BRMS1 may participate in transcriptional regulation via interaction with the mSin3.HDAC complex and suggest a novel mechanism by which BRMS1 might suppress cancer metastasis.";"";""
698;SIN3-HDAC-SAP30-ARID4 complex;;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,O75446,Q96ST3;51742,3065,3066,5928,5931,8819,25942;MI:0006- anti bait coimmunoprecipitation;9702189;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"SAP30 is involved in the functional recruitment of the mSin3-histone deacetylase complex to a specific subset of N-CoR corepressor complexes.";"";""
700;Snap25-caveolin complex;;Rat;P41350,P60881;25404,25012;MI:0019- coimmunoprecipitation | MI:0416- fluorescence microscopy;10934248;34.03.01,73.03.13,77.03.01.01.01;"A short-lasting SNAP25-caveolin interaction may be involved in the early phase of synaptic potentiation.";"";""
701;HuR-Tia1-Tiar-Hrnpu complex;;Rat;B5DF91,Q6IMY8,Q5PQR7,Q5BJN3;363854,117280,312510,361655;MI:0412- electrophoretic mobility supershift assay | MI:0019- coimmunoprecipitation;12855701;11.02.03.04.07,16.03.03;"HuR, TIA-1, TIAR, and hnRNP U bind the first 60 nucleotides of the 3'-UTR of murine COX-2. ";"";"Since Elavl1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
702;ARD1-NATH complex;;Human;Q9BXJ9,P36406;80155,373;MI:0019- coimmunoprecipitation | MI:0051- fluorescence technologies;15496142;12.07,16.01,70.10;"";"";""
703;SNARE complex (Vamp7, Stx5, Bet1, Vti1a); PCTV-cis-Golgi SNARE-complex;Rat;Q62896,Q08851,Q9JHW5,Q9JI51;29631,65134,85491,65277;MI:0019- coimmunoprecipitation;16735505;20.09.07.03,20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
704;SNARE complex (RINT1, ZW10, p31, Stx18);;Mammalia;P48556,Q6NUQ1,Q68FW4,O43264;5714,60561,360953,9183;MI:0047- far western blotting;15029241;10.03.01,20.09.07.03,20.09.07.27,20.09.16.09.05,70.07;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ZW10 is known to participate directly in turning off the spindle checkpoint.  The present results display an unexpected role  in membrane trafficking between ER and Golgi during interphase.";"";""
705;SNARE complex (RINT1, ZW10, p31);;Human;P48556,Q6NUQ1,O43264;5714,60561,9183;MI:0047- far western blotting;15029241;10.03.01,20.09.07.03,20.09.07.27,20.09.16.09.05,70.07;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ZW10 is known to participate directly in turning off the spindle checkpoint.  The present results display an unexpected role  in membrane trafficking between ER and Golgi during interphase.";"";""
706;SNARE complex (HGS, SNAP25, STX13); HGS-containing complex;Human;O14964,P60880,Q86Y82;9146,6616,23673;MI:0047- far western blotting;14769786;20.09.07.27,20.09.16.09.05,70.22;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";"STX12 and STX13 are identical (see GeneID:23673): "STX12 syntaxin 12 (Homo sapiens) Also known as STX13- STX14- MGC51957"."
707;SNARE complex (VAMP2, SNAP25, STX13);;Human;P60880,Q86Y82,P63027;6616,23673,6844;MI:0047- far western blotting;14769786;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ";"";"STX12 and STX13 are identical (see GeneID:23673): "STX12 syntaxin 12 (Homo sapiens) Also known as STX13- STX14- MGC51957"."
709;cGMP kinase signaling complex (IP3RI, IRAG, cGKI-beta);;Bovine;Q9TU34,Q9N1F0,P21136;317697,281918,282004;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;10724174;14.07.03,20.01.01.01,30.01.09.07,34.01.01.01,36.25.09.01,75.03.12.02;"The results identify IRAG as an essential NO/cGKI-dependent regulator of IP3-induced calcium release.";"";""
710;Brg1-associated complex I;;Human;O96019,O14497,O14744,P51532,Q12824,Q92922,Q8TAQ2,Q969G3,(Q96GM5,Q92925,Q6STE5);86,8289,10419,6597,6598,6599,6601,6605,(6602,6603,6604);MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11238380;10.01.09.05,11.02.03.04,16.03.01,42.10.03,70.10;"";"";"In a following paper (PMID:14559996) p66 has been identified as PRMT5."
711;Brm-associated complex; BRM containing SWI/SNF remodeling complex;Human;O96019,O14497,O14744,P51531,Q12824,Q92922,Q8TAQ2,Q969G3,(Q96GM5,Q92925,Q6STE5);86,8289,10419,6595,6598,6599,6601,6605,(6602,6603,6604);MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11238380;10.01.09.05,11.02.03.04,14.07.09,16.03.01,42.10.03,70.10;"";"";"In a following paper (PMID:14559996) p66 has been identified as PRMT5."
712;cGMP kinase signaling complex (IP3RI, IRAG, cGKI-beta, alpha-actin, calponin H1, PLN, RhoA);;Bovine;P62739,Q2HJ38,Q9TU34,Q9N1F0,P61014,P21136,P61585;515610,534583,317697,281918,18821,282004,338049;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;12480535;14.07.03,20.01.01.01,30.01.09.07,34.01.01.01,36.25.09.01,70.07,75.03.12.02;"The results suggest that PLB may have additional functions to regulate the activity of the Calcium-transporting ATPase  SERCA II.";"";"Since bovine PLN was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
713;BRG1-SIN3A complex;;Human;O96019,O14497,Q92769,O14744,Q09028,Q96ST3,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q6STE5,Q969G3;86,8289,3066,10419,5928,25942,6597,6598,6599,6601,6602,6603,6604,6605;MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11238380;10.01.09.05,11.02.03.04.03,16.03.01,42.10.03,70.10;"Components of the Sin3 complex cofractionate with BRG1-associated complex I, but not with BRG1-associated complex II.";"";""
714;BRM-SIN3A complex;;Human;O96019,O14497,Q13547,Q92769,O14744,Q09028,Q96ST3,P51531,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q6STE5,Q969G3;86,8289,3065,3066,10419,5928,25942,6595,6598,6599,6601,6602,6603,6604,6605;MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11238380;10.01.09.05,11.02.03.04.03,16.03.01,42.10.03,70.10;"Components of the Sin3 complex cofractionate with BRM-associated complex.";"";""
716;PU.1-associated protein complex;;Mouse;P31809,P70696,Q9Z2D6,P09405,P17433;26365,319177,17257,17975,20375;MI:0004- affinity chromatography technologies;14647463;11.02.03.04,16.03.01,70.10;"";"";""
717;PU.1-Sin3A-Hdac-MeCP2 complex;;Mouse;O09106,Q9Z2D6,Q60520,P17433;433759,17257,20466,20375;MI:0004- affinity chromatography technologies;14647463;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,43.03.07,70.10;"The authors suggest that MeCP2 acts as a corepressor of PU.1 probably due to facilitating complex formation with mSin3A and HDACs.";"";""
718;TRPV5-S100A10-annexin 2 complex;;Mouse;P07356,P08207,P69744;12306,20194,194352;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;12660155;14.04,18.02.10,20.01.01.01,20.03.01.01,70.02,75.03.09;"Downregulation of annexin 2  inhibited TRPV5 and TRPV6-mediated currents in transfected HEK293 cells.";"";""
719;S100A10-annexin 2 complex;;Mouse;P07356,P08207;12306,20194;MI:0019- coimmunoprecipitation;12660155;14.04,16.17.01,18.02.10;"";"";""
720;PU.1-SIN3A-HDAC complex;;Human;Q13547,Q96ST3,P17947;3065,25942,6688;MI:0007- anti tag coimmunoprecipitation;11593411;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"";"";""
721;PU.1-TBP complex;;Human;P17947,P20226;6688,6908;MI:0007- anti tag coimmunoprecipitation;14647463;11.02.03.04.03,16.03.01,70.10;"";"";""
722;MRG15-PAM14-RB complex;;Human;Q9UBU8,Q9Y605,P06400;10933,93621,5925;MI:0006- anti bait coimmunoprecipitation;11500496;11.02.03.04.01,40.20,70.10;"MRG15 blocks the RB-induced repression of this promotor, leading to transcription activation.";"";""
723;MAF1 complex; MRG15-associated factors 1;Human;Q9UBU8,Q9Y605,P06400;10933,93621,5925;MI:0006- anti bait coimmunoprecipitation | MI:0029- cosedimentation through density gradients;12397079;11.02.03.04.01,40.20,70.10;"";"";""
724;MAF2 complex; MRG15-associated factors 2;Human;Q9UBU8,Q9H7Z6;10933,84148;MI:0006- anti bait coimmunoprecipitation | MI:0029- cosedimentation through density gradients;12397079;11.02.03.04.01,14.07.04,40.20,70.10;"";"";""
725;P2X7 receptor signalling complex;;Human;P60709,O43707,P08238,P08107,P11142,P05107,Q16787,Q13368,Q64663,P42356,P23467,O95425;60,81,3326,3303,3312,3689,3909,4356,29665,5297,5787,6840;MI:0019- coimmunoprecipitation;11707406;20.01.01,20.03.01.01,30.05,42.04,70.02;"";"";"Since human P2rx7 was not available in the Uniprot database at the time of annotation, the orthologous protein from rat was used."
726;DDB2 complex;Ubiquitin E3 ligase;Human;P61201,Q9UNS2,Q9BT78,Q92905,Q7L5N1,Q99627,Q13619,Q16531,Q92466,Q13098,P62877,(Q9UBW8,Q9H9Q2);9318,8533,51138,10987,10980,10920,8451,1642,1643,2873,9978,(50813,64708);MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;12732143;10.01.05.01,14.07.05,16.03.01,32.01.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Results suggest that the distinct UV response of the DDB2 and CSA complexes is involved in diverse mechanisms of nucleotide excision repair (NER). The DDB2 complex binds to DNA after UV irradiation.";"";""
727;CSA complex;Ubiquitin E3 ligase;Human;P61201,Q9UNS2,Q9BT78,Q92905,Q7L5N1,Q99627,Q13619,Q16531,Q13216,Q13098,P62877,(Q9UBW8,Q9H9Q2);9318,8533,51138,10987,10980,10920,8451,1642,1161,2873,9978,(50813,64708);MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;12732143;10.01.05.01,14.07.05,16.01,32.01.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Results suggest that the distinct UV response of the DDB2 and CSA complexes is involved in diverse mechanisms of nucleotide excision repair (NER). The CSA complex does not bind to DNA, regardless of UV damage.";"";""
728;CSA-POLIIa complex;Ubiquitin E3 ligase;Human;P61201,Q9UNS2,Q9BT78,Q92905,Q7L5N1,Q99627,Q13619,Q16531,Q13216,Q13098,P24928,P62877,(Q9UBW8,Q9H9Q2);9318,8533,51138,10987,10980,10920,8451,1642,1161,2873,5430,9978,(50813,64708);MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;12732143;10.01.05.01,11.02.03,14.07.05,32.01.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. This complex has been purified from UV-irradiated cells. Results suggest that the distinct UV response of the DDB2 and CSA complexes is involved in diverse mechanisms of nucleotide excision repair (NER).";"";""
729;Ubiquitin E3 ligase (FBXO31, SKP1A, CUL1, RBX1);;Human;Q13616,Q5XUX0,P62877,P63208;8454,79791,9978,6500;MI:0007- anti tag coimmunoprecipitation;16357137;10.03.01.01,14.07.05,14.13,40.20;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. FBXO31 is the chromosome 16q24.3 senescence gene, a candidate breast tumor suppressor, and a component of an SCF complex.";"";""
730;SNARE complex (STX4, SNAP23, VAMP1);;Human;O00161,Q12846,P23763;8773,6810,6843;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16920918;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
731;SNARE complex (STX4, SNAP23, VAMP2);;Human;O00161,Q12846,P63027;8773,6810,6844;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16920918;20.09.07.27,20.09.16.09.03;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
732;SIN3 complex;;Human;Q13547,Q92769,Q09028,Q16576,O00422,O75446,Q96ST3;3065,3066,5928,5931,10284,8819,25942;MI:0006- anti bait coimmunoprecipitation | MI:0091- chromatography technologies;11784859;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"";"";""
733;SNARE complex (STX4, VAMP1, VAMP7);;Human;Q12846,P23763,P51809;6810,6843,6845;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16920918;20.09.07.27,20.09.16.09.03;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
734;SNARE complex (STX4, SNAP23, VAMP2);;Mammalia;O00161,Q12846,P63045;8773,6810,24803;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16920918;20.09.07.27,20.09.16.09.03;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
735;SNARE complex (Vti1b, Stx6, Stx7); Q-SNARE complex;Mouse;Q9JKK1,O70439,O88384;58244,53331,53612;MI:0019- coimmunoprecipitation;15640147;20.09.07.27,20.09.16.09.03,70.08;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
736;SNARE complex (Vti1b, Stx7, Stx8, Vamp8);;Mouse;O70439,O88983,O70404,O88384;53331,55943,22320,53612;MI:0019- coimmunoprecipitation;15640147;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
737;Ppp2c-PKA-Ryr2-mAkap-Pde4d3 complex;;Rat;Q9WVC7,O08661,(P63331,P62716),(P27791,P68182);64553,689560,(24672,24673),(25636,293508);MI:0019- coimmunoprecipitation;11590243;30.01.09.03,30.01.09.07,36.25.09.04,70.10.05,75.03.12.03;"The authors describe the association of PP2A and RyR with the mAKAP complex, an assembly that is likely to be important to the integration of cAMP and Ca2+ signaling to the myocyte nucleus.";"";"An additional component was mentioned as PDE4D3. "
738;SIN3-ING1b complex I;;Human;Q4LE39,Q13547,Q92769,Q9UK53,Q09028,Q16576,O00422,O75446,Q96ST3;51742,3065,3066,3621,5928,5931,10284,8819,25942;MI:0006- anti bait coimmunoprecipitation | MI:0091- chromatography technologies;11784859;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"SAP30 is a specific component of Sin3 complexes since it is absent in other HDAC1/2-containing complexes such as NuRD.";"";""
739;SIN3-ING1b complex II;;Human;O96019,O14497,Q4LE39,Q13547,Q92769,Q9UK53,Q09028,Q16576,O00422,O75446,Q96ST3,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5;86,8289,51742,3065,3066,3621,5928,5931,10284,8819,25942,6597,6598,6599,6601,6602;MI:0006- anti bait coimmunoprecipitation | MI:0091- chromatography technologies;11784859;10.01.09.05,11.02.03.04.03,14.07.04,16.01,18.02.09,42.10.03,70.10;"SAP30 is a specific component of Sin3 complexes since it is absent in other HDAC1/2-containing complexes such as NuRD.";"";""
740;Exon junction complex, EIF4A3-MLN51-MAGOH-Y14 (RNA-protein complex);;Human;O15234,P38919,P61326,Q9Y5S9;22794,9775,4116,9939;MI:0004- affinity chromatography technologies | MI:0040- electron microscopy | MI:0071- molecular sieving | MI:0114- x-ray crystallography;16797590;11.04.03.11,12.07,16.03.03,20.01.21,20.09.01,70.03,70.10;"This protein complex remains stably bound to the mRNA through different cellular environments. Magoh and Y14 form a tight heterodimer. The authors propose a that eIF4AIII interacts with Y14:Magoh to enforce a compact arrangement of eIF4AIII's two domains and allow MLN51 to interact with both eIF4AIII and the RNA.";"";""
741;NCOR-HDAC3 complex;;Human;Q13227,O15379,O75376,O60907,Q9BZK7;2874,8841,9611,6907,79718;MI:0007- anti tag coimmunoprecipitation;11931768;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,30.01.05.01.02,42.10.03,70.10;"N-CoR-HDAC3 complex inhibits JNK activation through the associated GPS2 subunit and thus could potentially provide an alternative mechanism for hormone-mediated antagonism of AP-1 function.";"";""
742;eIF3 complex (EIF3S6, EIF3S5, EIF3S4, EIF3S3, EIF3S6IP, EIF3S2, EIF3S9, EIF3S12,  EIF3S10, EIF3S8,  EIF3S1, EIF3S7);;Human;Q14152,P55884,Q99613,O15371,P60228,Q9Y262,O00303,O75821,O15372,Q13347,O75822,Q9UBQ5;8661,8662,8663,8664,3646,51386,8665,8666,8667,8668,8669,27335;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;14519125;12.04.01;"";"";""
743;SIN3-SAP25 complex;;Human;Q4LE39,Q13547,Q92769,Q09028,Q16576,Q9H0E3,O00422,Q1EHW4,O75446,Q96ST3,Q9H7L9;51742,3065,3066,5928,5931,79595,10284,751865,8819,25942,64426;MI:0007- anti tag coimmunoprecipitation;16449650;10.01.09.05,11.02.03.04.03,14.07.04,16.01,42.10.03,70.10;"SAP25 binds to the PAH1 domain of SIN3A. ";"";"Since human SAP25 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
744;Exon junction complex (EIF4A3-MLN51-MAGOH-Y14); RNA-protein complex;Human;O15234,P38919,P61326,Q9Y5S9;22794,9775,4116,9939;MI:0004- affinity chromatography technologies;16314458;11.04.03.11,12.07,16.03.03,20.01.21,20.09.01,70.03,70.10;"The experiments demonstrate that eIF4AIII, MLN51, and Magoh:Y14 are able to form a stable tetrameric complex when co-expressed in vivo. Both eIF4AIII and MLN51 are required for the stable association of either with the Magoh:Y14 heterodimer.";"";""
745;NCOR-SIN3-RPD3 complex;;Human;Q92769,Q9Y618,Q96ST3,O75182;3066,9612,25942,23309;MI:0006- anti bait coimmunoprecipitation;9139820;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"The authors predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity. ";"";""
746;C/EBPalpha-HNF6 complex;;Human;P49715,Q9UBC0;1050,3175;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;16440369;11.02.03.04.01,70.10;"Formation of the C/EBPalpha-HNF6 protein complex required the HNF6 cut domain and the C/EBPalpha activation domain (AD) 1/AD2 sequences. The C/EBPalpha-HNF6 protein complex stimulates recruitment of the CBP coactivator protein for expression of Foxa2.";"";""
747;NCOR-SIN3-HDAC1 complex;;Human;Q13547,Q9Y618,Q96ST3;3065,9612,25942;MI:0096- pull down;9150137;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"N-CoR directly interact with mSin3A. ";"";""
748;TRAF6-TAK1 complex;;Human;O43318,Q9Y4K3;6885,7189;MI:0019- coimmunoprecipitation;16543409;30.05.01.18;"During IL-1 signaling cascade a complex consisting of TRAF6, TAK1, TAB1, TAB2, and the two ubiquitin ligases Uev1A and Ubc13 is formed, phosphorylating TRAF6 and subsequently TAK1. TAK1 activation leads to activation of both NF{kappa}B and the MAPKs, followed by gene transcription. SOCS-3 (suppressor of cytokine signaling-3) inhibits IL-1 signal transduction by inhibiting ubiquitination of TRAF6, thus preventing association and activation of TAK1.";"";""
749;MeCP2-SIN3A-HDAC complex;;Human;Q13547,Q92769,P51608,Q96ST3;3065,3066,4204,25942;MI:0096- pull down;9620804;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,16.03.01,41.05.04.01,42.10.03,70.10;"MeCp binds specifically to methylated DNA, thus linking two global mechanisms of gene regulation, DNA methylation and histone deacetylation. ";"";""
750;MeCP2-Sin3a-Hdac complex;;Rat;Q99PA2,Q99PA1,Q00566,Q60520;84576,84577,29386,20466;MI:0006- anti bait coimmunoprecipitation;9620804;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,16.03.01,41.05.04.01,42.10.03,70.10,77.03.01.01.01;"MeCp binds specifically to methylated DNA, thus linking two global mechanisms of gene regulation, DNA methylation and histone deacetylation. ";"";"Since Sin3a from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
751;Trpc1-dystrophin-alpha1-syntrophin complex;;Mouse;P11531,Q61234,Q61056;13405,20648,22063;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;17202249;18.02.10,20.01.01.01,20.03.01.01,70.02,75.03.12;"The control of cationic channels by PDZ-containing scaffolding proteins might be a widespread function of dystrophin-associated protein complexes for controlling transmembrane ions fluxes. The authors propose that the dystrophin-based cytoskeleton, by the intermediate of PDZ-containing alpha-1-syntrophin, maintains normal TRPC1-dependent store-operated influx during activation of calcium release in muscle cells.";"";""
752;SMRT core complex;;Human;O15379,Q9Y618,O60907;8841,9612,6907;MI:0071- molecular sieving | MI:0226- ion exchange chromatography | MI:0006- anti bait coimmunoprecipitation;10944117;10.01.09.05,11.02.03.04.03,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"";"TBL1 is involved in deafness.";"Another subunit of the complex was found in the analysis, which has not been further characterized: SMRT-p37."
753;UTM-SGCE-DAG1-CAV1-NOS3 complex;;Human;Q03135,Q14118,P29474,O43556,P46939;857,1605,4846,8910,7402;MI:0019- coimmunoprecipitation;17127434;18.02.01,45.03.11,77.03.03.02;"The authors propose that this utrophin associated protein complex (UAPC) in human umbilical vein endothelial cells (HUVECs) may play an important role in the regulation of vascular tone.";"";""
754;Exon junction complex (EIF4A3-MLN51-UPF3B-MAGOH-Y14); RNA-protein complex;Human;O15234,P38919,P61326,Q9Y5S9,Q0VAK7;22794,9775,4116,9939,65109;MI:0007- anti tag coimmunoprecipitation;16209946;11.04.03.11,12.07,16.03.03,20.01.21,20.09.01,70.03,70.10;"";"";""
755;Exon junction complex (F4A3-MLN51-UPF3B-MAGOH-Y14-PYM); RNA-protein complex;Human;O15234,P38919,P61326,Q9Y5S9,Q0VAK7,Q9BRP8;22794,9775,4116,9939,65109,84305;MI:0007- anti tag coimmunoprecipitation;16209946;11.04.03.11,12.07,16.03.03,20.01.21,20.09.01,70.03,70.10;"";"";""
756;Prune-Gelsolin complex;;Human;P06396,Q86TP1;2934,58497;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;17103319;34.05.01;"";"";""
757;Prune-GSK3beta complex;;Human;P49841,Q86TP1;2932,58497;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;17103319;34.05.01;"";"";""
758;Prune/Nm23-H1 complex;;Human;P15531,Q86TP1;4830,58497;MI:0087- predictive text mining;14998490;34.05;"";"";""
759;Fgfr1-Kal1 complex;;Rat;Q04589,P23352;79114,3730;MI:0019- coimmunoprecipitation;17186267;30.05.01.12.03,36.25.01.13,47.03.01.01.01,77.03.01.01.01;"The authors propose that during the initial steps of olfactory bulb formation, anosmin-1 cooperates with FGFR1 to promote functional FGF-signalling that in turn promotes olfactory bulb development.";"KAL1 and FGFR1 are involved in Kallmann syndrome.";"Since KAL1 from rat was not available in the UniProt database at the time of annotation, the orthologous human protein was used."
760;Apoptosis- and splicing-associated protein complex (ASAP-L), SAP18-RNPS1-Acinus-L;;Human;Q9UKV3,Q15287,O00422;22985,10921,10284;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;12665594;11.04.03,40.10.02,70.10;"In vitro splicing assays suggest that the ASAP complexes function to repress splicing in vitro and that the ability of RNPS1 (and possibly Acinus-L) to activate splicing is overcome both when it is a component of ASAP and in the presence of the intact complex. In vitro assays using an apoptotic extract strongly indicate that ASAP complexes disassemble during apoptosis.";"";""
761;Apoptosis- and splicing-associated protein complex (ASAP-S), SAP18-RNPS1-Acinus-S;;Human;Q9UKV3,Q15287,O00422;22985,10921,10284;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;12665594;11.04.03,40.10.02,70.10;"In vitro splicing assays suggest that the ASAP complexes function to repress splicing in vitro and that the ability of RNPS1 (and possibly Acinus-L) to activate splicing is overcome both when it is a component of ASAP and in the presence of the intact complex. In vitro assays using an apoptotic extract strongly indicate that ASAP complexes disassemble during apoptosis.";"";""
762;Ahnak1-dysferlin complex;;Rat;Q38PG1,Q9ESD7;191572,26903;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;17185750;42.02,45.03.12,70.02,75.03.12;"The authors provide evidence for a functional cooperation between dysferlin and AHNAK during muscle regeneration.";"Dysf is involved in autosomal recessive limb girdle muscular dystrophy 2B (LGMD2B), Miyoshi myopathy (MM) and distal anterior compartment myopathy (DMAT).";"Since Dysf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from human was used."
763;Y14-Magoh complex;;Human;P61326,Q9Y5S9;4116,9939;MI:0055- fluorescent resonance energy transfer | MI:0114- x-ray crystallography | MI:0029- cosedimentation through density gradients;12781131;11.04.03,20.01.21,20.09.01,70.03,70.10;"Y14 and Magoh form an extremely stable heterodimer. Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface.";"";""
764;Dysferlin-affixin complex;;Human;O75923,Q9HBI1;8291,29780;MI:0019- coimmunoprecipitation | MI:0051- fluorescence technologies;15835269;42.02,45.03.12.01,75.03.12.01;"The results suggest that affixin may participate in membrane repair with dysferlin.";"DYSF is involved in Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B).";""
765;SNARE complex (Stx6, Snap29);;Rat;Q9Z2P6,Q63635;116500,60562;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;9880331;20.09.07.27,20.09.16.09.05,70.08;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
766;Cask-Grip1-Prkce-Rgs4-Gria2 complex;;Rat;Q62915,P19491,P97879,P09216,P49799;29647,29627,84016,29340,29480;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;17084383;01.08.01,73.03.13,77.03.01.01.01;"The associations between CASK, PKCepsilon, and RGS4 were up-regulated in the adult brain compared with postnatal day 11 rat brain. In contrast, the associations of CASK with Mint1, GRIP1, and GluR2/3 were down-regulated in the adult brain. These results suggest that CASK protein complex is developmentally regulated by unknown signals.";"";""
767;Cask-Grip1-Gria2-Mint1 complex;;Rat;O35430,Q62915,P19491,P97879;83589,29647,29627,84016;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;17084383;01.08.01,73.03.13,77.03.01.01.01;"The associations between CASK, PKCepsilon, and RGS4 were up-regulated in the adult brain compared with postnatal day 11 rat brain. In contrast, the associations of CASK with Mint1, GRIP1, and GluR2/3 were down-regulated in the adult brain. These results suggest that CASK protein complex is developmentally regulated by unknown signals.";"";""
768;NdpkA-Ampkalpha1 complex;;Rat;Q05982,P54645;191575,65248;MI:0019- coimmunoprecipitation;16026327;16.01,70.03,77.03.11.07;"";"";""
769;Exon junction complex (EIF4A3-MLN51-MAGOH-Y14),  RNA-protein complex;;Human;O15234,P38919,P61326,Q9Y5S9;22794,9775,4116,9939;MI:0071- molecular sieving | MI:0114- x-ray crystallography;16923391;11.04.03.11,12.07,16.03.03,16.19.03,20.01.21,20.09.01,70.03,70.10;"The DEAD-box protein eIF4AIII encloses an ATP molecule and provides the binding sites for six ribonucleotides. Btz wraps around eIF4AIII and stacks against the 5' nucleotide. An intertwined network of interactions anchors Mago-Y14 and Btz at the interface between the two domains of eIF4AIII, effectively stabilizing the ATP bound state.";"";""
770;TREX complex;;Human;Q13838,Q96FV9,Q8NI27,Q96J01,Q86V81,Q13769,Q86W42,Q6I9Y2;7919,9984,57187,84321,10189,8563,79228,80145;MI:0007- anti tag coimmunoprecipitation;15998806;16.03.03,20.01.21,20.09.01,70.10.06,70.10.09;"The TREX complex is recruited by the CBC complex to the 5-prime end of spliced RNAs and is involved in RNA export from the nucleus into the cytoplasm. The TREX complex contains the THO transcription elongation complex.";"";""
771;NDPKA-AMPKalpha1 complex;;Human;P15531,Q13131;4830,5562;MI:0019- coimmunoprecipitation;16026327;16.01,70.03,77.03.11.07;"";"";""
772;eIF4AIII-Btz complex;;Human;O15234,P38919;22794,9775;MI:0071- molecular sieving | MI:0114- x-ray crystallography;16923391;11.04.03.11;"The 3.0 Angstroem resolution structure of the eIF4AIII-Btz subcomplex reveals a dramatic conformational change of the helicase domains as compared to EJC bound eIF4AIII. More generally, the authors propose that similarly to what observed for protein kinases, members of the DEAD-box family of proteins are likely to adopt a similar structure in their 'on' state (when bound to ATP and RNA) despite having different conformations in their 'off' states.";"";""
773;Y14-Magoh complex;;Human;P61326,Q9Y5S9;4116,9939;MI:0114- x-ray crystallography | MI:0071- molecular sieving;16923391;11.04.03,20.01.21,20.09.01,70.03,70.10;"Y14 and Magoh form an extremely stable heterodimer. Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface.";"";""
774;THO complex;;Human;Q96FV9,Q8NI27,Q13769,Q86W42,Q6I9Y2;9984,57187,8563,79228,80145;MI:0007- anti tag coimmunoprecipitation;15998806;16.03.03,70.10.09;"The human THO complex associates with spliced mRNA, but not with unspliced pre-mRNA in vitro. Transcription is not required for this recruitment. It was also shown that the human THO complex colocalizes with splicing factors in nuclear speckle domains in vivo. The TREX complex contains the THO transcription elongation complex.";"";""
775;CBC complex (cap binding complex);;Human;Q09161,P52298;4686,22916;MI:0114- x-ray crystallography;11545740;16.03.03,20.01.21,20.09.01,70.10;"The heterodimeric nuclear cap binding complex (CBC) binds to 5'-capped polymerase II transcripts. It enhances the efficiency of several mRNA maturation steps and is essential for U snRNA nuclear export in multicellular eukaryotes.";"";""
776;Plp1-Calr-Itgav complex;;Rat;P18418,P43406,P60203;64202,16410,24943;MI:0019- coimmunoprecipitation;12196561;30.05.02.26,43.03.11,73.03.11;"The PLP protein may be involved in signaling through integrins in oligodendrocytes.";"";"Since Itgav from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
777;Exon junction complex; EJC complex;Mammalia;Q9UBU9,Q9Y5S9,Q15287,Q8IYB3,Q86V81,Q9HAU5,Q9BZI7;10482,9939,10921,10250,10189,26019,65109;MI:0019- coimmunoprecipitation;12093754;01.03.16.01,16.03.03,20.01.21,20.09.01,70.10;"The exon junction complex (EJC) is a protein complex that assembles near exon-exon junctions of mRNAs as a result of splicing. EJC proteins play important roles in postsplicing events including mRNA export, cytoplasmic localization, and nonsense-mediated decay. ";"";""
778;LARC complex (LCR-associated remodeling complex);;Human;P60709,O96019,O14497,Q14839,Q92785,Q8WXI9,Q13547,Q92769,P07910,Q9UBB5,O95983,O94776,Q09028,P51532,Q12824,Q92922,Q8TAQ2,Q92925,Q969G3;60,86,8289,1108,5977,57459,3065,3066,3183,8932,53615,9219,5928,6597,6598,6599,6601,6603,6605;MI:0091- chromatography technologies | MI:0004- affinity chromatography technologies;16217013;10.01.09.05,11.02.03.04,14.07.04,16.03.01,42.10.03,70.10;"LARC binds to the hypersensitive 2 (HS2)-Maf recognition element (MARE) DNA in a sequence-specific manner and remodels nucleosomes.";"";""
779;K(ATP) macromolecular complex (Kir6.2, Pkm2, Gapdh, Tpi1);;Rat;P04797,P70673,P11980,P48500;24383,83535,25630,24849;MI:0019- coimmunoprecipitation | MI:0397- two hybrid array | MI:0416- fluorescence microscopy;16170200;18.02.10,20.01.01.01,20.03.01.01,70.02,75.03.12.03;"The authors provide evidence that the activity of the identified three glycolytic enzymes regulate channel activity, presumably by altering the ATP levels in the microenvironment of the K(ATP) channel protein complex.";"";""
781;URI complex (Unconventional prefoldin RPB5 Interactor);Prefoldin-like complex;Human;Q13616,Q9UHV9,P19388,O94763,Q9Y265,Q9Y230,P63208,Q13309,Q9ULZ2;8454,5202,5434,8725,8607,10856,6500,6502,26228;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;14615539;11.02.03.04,30.01.09.11,32.01.11;"The URI complex participates in the regulation of nutrient-sensitive, TOR-dependent transcription programs.";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized: p42, p40, p10. At the time of annotation, the additional member PFD4-related protein of the protein complex was not found in the UniProt database."
782;Itch-Fam/Usp9x complex;;Rat;Q5YB86,P70398;311567,22284;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;17038327;14.07.05,16.01,18.02;"Interaction between Itch and FAM reverses Itch auto-ubiquitylation and protects the ligase from proteasomal degradation.";"";"Since Usp9x of the rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
783;ITCH-FAM/USP9x complex;;Human;Q96J02,Q93008;83737,8239;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;17038327;14.07.05,16.01,18.02;"Interaction between Itch and FAM reverses Itch auto-ubiquitylation and protects the ligase from proteasomal degradation.";"";""
784;SMG-1-Upf1-eRF1-eRF3 complex (SURF);;Human;P62495,Q96Q15,Q92900,(P15170,Q8IYD1);2107,23049,5976,(2935,23708);MI:0006- anti bait coimmunoprecipitation;16452507;11.04.03.11,14.07.03,20.01.21,20.09.01,70.03,70.10;"An association between SURF and the EJC is required for SMG-1-mediated Upf1 phosphorylation and NMD (nonsense-mediated mRNA decay).";"";""
785;Exon junction complex; EJC complex;Human;Q13838,P38919,P61326,Q9Y5S9,Q15287,Q8IYB3,Q86V81,Q9BZI7;7919,9775,4116,9939,10921,10250,10189,65109;MI:0019- coimmunoprecipitation;1473001;01.03.16.01,16.03.03,20.01.21,20.09.01,70.10;"The exon junction complex (EJC) is a protein complex that assembles near exon-exon junctions of mRNAs as a result of splicing. EJC proteins play important roles in postsplicing events including mRNA export, cytoplasmic localization, and nonsense-mediated decay.";"";""
786;MR-UBC9-SRC1 complex;;Human;Q15788,P08235,Q08209;8648,4306,5530;MI:0019- coimmunoprecipitation | MI:0051- fluorescence technologies;17105732;11.02.03.04,70.10;"";"";""
787;NuA4/Tip60-HAT complex B;;Human;O96019,Q9NPF5,Q9H2F5,Q92993,Q9UBU8,Q9Y265,Q9Y230,Q9Y4A5;86,55929,80314,10524,10933,8607,10856,8295;MI:0007- anti tag coimmunoprecipitation;14966270;10.01.02,10.01.05.01,10.01.09.05,14.07.04,16.03.01,32.01.09,42.10.03,70.10;"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.";"";""
788;Exosome;;Human;Q9Y2L1,Q9Y3B2,Q13868,Q9NQT5,Q9NPD3,Q9NQT4,Q5RKV6,Q15024,Q96B26,Q06265;22894,51013,23404,51010,54512,56915,118460,23016,11340,5393;MI:0019- coimmunoprecipitation;11719186;01.03.16.01,16.03.03,70.03,70.10;"Inherently unstable mammalian mRNAs contain AU-rich elements (AREs) within their 3' untranslated regions. The mammalian exosome is required for rapid 3'-to-5' degradation of ARE-containing RNAs but not for poly(A) shortening. ARE recognition requires certain ARE binding proteins that can interact with the exosome and recruit it to unstable RNAs, thereby promoting their rapid degradation.";"";""
789;Exosome;;Human;Q9Y2L1,Q9Y3B2,Q01780,Q13868,Q9NQT5,Q9NPD3,Q9NQT4,Q5RKV6,Q15024,Q96B26,Q06265;22894,51013,5394,23404,51010,54512,56915,118460,23016,11340,5393;MI:0019- coimmunoprecipitation;11719186;01.03.16.01,16.03.03,70.10;"Inherently unstable mammalian mRNAs contain AU-rich elements (AREs) within their 3' untranslated regions. The mammalian exosome is required for rapid 3'-to-5' degradation of ARE-containing RNAs but not for poly(A) shortening. ARE recognition requires certain ARE binding proteins that can interact with the exosome and recruit it to unstable RNAs, thereby promoting their rapid degradation. The exosome complex containing PMSCL was only found in the nuclear complex.";"";""
790;DDB complex;;Human;Q16531,Q92466;1642,1643;MI:0004- affinity chromatography technologies | MI:0028- cosedimentation in solution;16223728;10.01.05.01,16.03.01,32.01.09;"";"";""
791;SNARE complex (Vamp2, Snap25, Stx1a, Cplx1); Complexin I complex;Rat;P63041,P60881,P32851,P63045;64832,25012,116470,24803;MI:0019- coimmunoprecipitation;7553862;16.01.01,18.02.07,20.09.07.27,20.09.16.09.05,73.03.13,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
792;SNARE complex (Vamp2, Snap25, Cplx2, Stx1a); Complexin II complex;Rat;P84087,P60881,P32851,P63045;116657,25012,116470,24803;MI:0019- coimmunoprecipitation;7553862;16.01.01,18.02.07,20.09.07.27,20.09.16.09.05,73.03.13,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
793;SNARE complex (VAMP2, SNAP25, STX1a, CPLX1); Complexin I complex;Human;O14810,P60880,Q16623,P63027;10815,6616,6804,6844;MI:0019- coimmunoprecipitation;7553862;16.01.01,18.02.07,20.09.07.27,20.09.16.09.05,73.03.13,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
794;SNARE complex (VAMP2, SNAP25, STX1a, CPLX2); Complexin II complex;Human;Q6PUV4,P60880,Q16623,P63027;10814,6616,6804,6844;MI:0019- coimmunoprecipitation;7553862;16.01.01,18.02.07,20.09.07.27,20.09.16.09.05,73.03.13,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
795;SNARE complex (Vamp2, Snap25, Stx1a, Cplx1); Complexin I complex;Mouse;P63040,P60879,O35526,P63044;12889,20614,20907,22318;MI:0019- coimmunoprecipitation;7553862;16.01.01,18.02.07,20.09.07.27,20.09.16.09.05,73.03.13,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
796;SNARE complex (Vamp2, Snap25, Stx1a, Cplx2); Complexin II complex;Mouse;P84086,P60879,O35526,P63044;12890,20614,20907,22318;MI:0019- coimmunoprecipitation;7553862;16.01.01,18.02.07,20.09.07.27,20.09.16.09.05,73.03.13,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
797;SNARE complex (STX11, VAMP2, SNAP23);;Human;O00161,O75558,P63027;8773,8676,6844;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;10036234;20.01.10,20.09.07.27,20.09.16.09.05,70.22;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
798;NuA4/Tip60-HAT complex A;;Human;O96019,Q9H0E9,Q9HAF1,Q9NPF5,Q96L91,Q9H2F5,Q52LR7,Q92993,Q9NXR8,Q9UBU8,Q9NV56,Q9Y265,Q9Y230,Q9Y4A5,O95619;86,10902,64769,55929,57634,80314,26122,10524,54556,10933,55257,8607,10856,8295,8089;MI:0004- affinity chromatography technologies;14966270;01.04,10.01.02,10.01.05.01,10.01.09.05,14.07.04,16.03.01,32.01.09,42.10.03,70.10;"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.";"";""
799;DMAP1-associated complex;;Human;O96019,Q9H0E9,Q9NPF5,Q96L91,Q9H2F5,Q9Y265,Q9Y230,Q6ZRS2,Q9Y4A5,Q15906;86,10902,55929,57634,80314,8607,10856,10847,8295,6944;MI:0004- affinity chromatography technologies;14966270;01.04,10.01.02,10.01.05.01,10.01.09.05,42.10.03,70.10;"";"";""
800;DNMT1-HDAC1-DMAP1 complex;;Mammalia;Q9JI44,P13864,P70288;66233,13433,15182;MI:0007- anti tag coimmunoprecipitation;10888872;10.01.09.01,11.02.03.04.03,11.02.03.04.07,70.10;"";"";""
801;SNARE complex (STX2, SNAP23);;Human;O00161,P32856;8773,2054;MI:0019- coimmunoprecipitation;10648404;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
802;Cdc42-Par6b-Par3-Prkci complex;;Mammalia;P60766,Q99NH2,Q9JK83,Q62074;12540,93742,58220,18759;MI:0007- anti tag coimmunoprecipitation;10934474;30.01.05.05.01,40.01.03,41.05.19,42.06,70.06;"The results indicate that Cdc42, in the GTP-bound state, links to the Par3-PKC-lambda/iota complex through Par6.";"";""
803;BRG1-SIN3A-HDAC containing SWI/SNF remodeling complex I;;Human;O96019,O14497,Q92769,O14744,Q96ST3,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3;86,8289,3066,10419,25942,6597,6598,6599,6601,6602,6605;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;14559996;10.01.09.05,11.02.03.04,14.07.04,14.07.09,16.03.01,42.10.03,70.10;"The authors provide evidence, that PRMT5, mSin3A/HDAC2, and the Brg1-based hSWI/SNF complex are involved in cad transcriptional repression.";"";""
804;CDC42-Par6c-Par3-Prkcz complex;;Dog;P60952,Q99NH2,Q9Z101,Q02956;403934,93742,56513,18762;MI:0096- pull down;10934474;30.01.05.05.01,40.01.03,41.05.19,42.06,70.06,75.03.09;"Only activated Cdc42 was able to bind to all three endogenous proteins.";"";"Since Prkcz, Pard6a and Pard3 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
805;SNARE complex (STX4, SNAP23);;Human;O00161,Q12846;8773,6810;MI:0019- coimmunoprecipitation;10961877;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
806;BRM-SIN3A-HDAC complex; BRM-Sin3A-HDAC containing SWI/SNF remodeling complex;Human;O96019,O14497,Q92769,O14744,Q96ST3,P51531,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q969G3;86,8289,3066,10419,25942,6595,6598,6599,6601,6602,6603,6605;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;14559996;10.01.09.05,11.02.03.04,14.07.04,14.07.09,42.10.03,70.10;"";"";""
807;BRG1-associated complex; BRG1 containing SWI/SNF remodeling complex;Human;O96019,O14497,O14744,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3;86,8289,10419,6597,6598,6599,6601,6602,6605;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;14559996;10.01.09.05,11.02.03.04,14.07.09,16.03.01,42.10.03,70.10;"";"";""
808;BRM-associated complex; BRM containing SWI/SNF remodeling complex;Human;O96019,O14497,O14744,P51531,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q969G3;86,8289,10419,6595,6598,6599,6601,6602,6603,6605;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;14559996;10.01.09.05,11.02.03.04,14.07.09,16.03.01,42.10.03,70.10;"";"";""
809;eRF1-eRF3-GTP-Mg(2+) complex;;Human;P62495,(P15170,Q8IYD1);2107,(2935,23708);MI:0065- isothermal titration calorimetry;16914449;12.04.03,16.17.07,16.19.05,30.01.05.05.01,70.03;"eRF3 binds GDP independently of the presence or absence of eRF1 whereas GTP binds only to the eRF1-eRF3 complex. The authors suggest that the quaternary eRF1-eRF3-GTP-Mg2+ complex binds to the ribosomal pretermination complex.";"";""
810;FCP1-associated protein complex;;Human;Q9Y5B0,P84090,P35269,P30876,O14744,Q15208,Q9BQA1;9150,2079,2962,5431,10419,11329,79084;MI:0004- affinity chromatography technologies;15670829;11.02.03.01.04,14.07.09,70.10;"FCP1-associated PRMT5 can methylate histones H4 in vitro.";"";""
811;FCP1-associated protein complex;;Human;Q9Y5B0,P84090,P35269,P30876,O14744,Q15208,Q9BQA1;9150,2079,2962,5431,10419,11329,79084;MI:0004- affinity chromatography technologies;12560496;11.02.03.01.04,14.07.09,70.10;"The authors suggest a putative role of FCP1 CTD-phosphatase in linking the transcription elongation with the splicing process.";"";""
812;Upf complex (UPF1, UPF2, UPF3a);;Human;Q92900,Q9HAU5,Q9H1J1;5976,26019,65110;MI:0019- coimmunoprecipitation;11163187;01.03.16.01,16.03.03,70.03,70.10.06;"Human Upf proteins target mRNA for nonsense-mediated decay when bound downstream of a termination codon. Nonsense-mediated decay (NMD) rids eukaryotic cells of aberrant mRNAs containing premature termination codons. These are discriminated from true termination codons by downstream cis-elements, such as exon-exon junctions.";"";""
813;Upf complex (UPF1, UPF2, UPF3b);;Human;Q92900,Q9HAU5,Q9BZI7;5976,26019,65109;MI:0019- coimmunoprecipitation;11163187;01.03.16.01,16.03.03,70.03,70.10.06;"Human Upf proteins target mRNA for nonsense-mediated decay when bound downstream of a termination codon. Nonsense-mediated decay (NMD) rids eukaryotic cells of aberrant mRNAs containing premature termination codons. These are discriminated from true termination codons by downstream cis-elements, such as exon-exon junctions.";"";""
814;Postsplicing complex;;Human;Q9UBU9,Q9Y5S9,Q15287,Q92900,Q9HAU5,Q9H1J1,Q9BZI7;10482,9939,10921,5976,26019,65110,65109;MI:0019- coimmunoprecipitation;11546874;01.03.16.01,16.03.03,70.10.06;"A final quality-control step in mRNA maturation is mRNA surveillance. This process detects mRNAs with truncated open reading frames and subjects them to nonsense-mediated mRNA decay (NMD). The protein RNPS1, a component of the postsplicing complex that is deposited 5' to exon-exon junctions, interacts with the evolutionarily conserved human Upf complex, a central component of NMD.";"";""
815;MRIP-MBS-RHOA complex;;Human;Q6WCQ1,O14974,P61586;23164,4659,387;MI:0019- coimmunoprecipitation;14506264;14.10,16.01,18.02.01,75.03.12.02;"";"";""
816;MRIP-RHOA complex;;Human;Q6WCQ1,P61586;23164,387;MI:0096- pull down;14506264;16.01,75.03.12.02;"";"";""
817;MRIP-MBS complex;;Human;Q6WCQ1,O14974;23164,4659;MI:0096- pull down;14506264;16.01,75.03.12.02;"";"";""
819;20S methylosome-SmD complex;;Human;P54105,O14744,P62314,P62318;1207,10419,6632,6634;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;11713266;14.07.09,14.10,70.03;"PRMT5 and pICln bind only to unmethylated SMD1 and SMD3.";"";""
820;SNARE complex (STX6, SNAP23);;Human;O00161,O43752;8773,10228;MI:0019- coimmunoprecipitation;11001914;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
821;Par-3-VE-cadherin-alpha-beta-catenin complex;;Hamster;P55284,P26231,Q02248,Q99NH2;12562,12385,12387,93742;MI:0019- coimmunoprecipitation;17057644;40.01.03,41.05.19,42.06,70.06;"The authors show that both PAR-3 and PAR-6 can directly and independently associate with VE-cadherin, and that both are recruited to cell-cell contacts independently of each other.";"";"Since  Ctnna1, Ctnnb1, Cdh5 and Pard3 from hamster were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
822;mRNA decay complex (UPF1, UPF2, UPF3B, DCP2, XRN1, XRN2, EXOSC2, EXOSC4, EXOSC10, PARN);;Human;Q8IU60,Q01780,Q13868,Q9NPD3,O95453,Q92900,Q9HAU5,Q9BZI7,Q8IZH2,Q9H0D6;167227,5394,23404,54512,5073,5976,26019,65109,54464,22803;MI:0019- coimmunoprecipitation;14527413;01.03.16.01,16.03.03,70.03,70.10;"From experiments, it is concluded that nonsense-mediated mRNA decay (NMD) in mammalian cells degrades mRNAs from both 5' and 3' ends by recruiting decapping and 5'-->3' exonuclease activities as well as deadenylating and 3'-->5' exonuclease activities. All these activities are present within the mRNA decay complex.";"";""
823;PAR-3-VE-cadherin complex, endothelial;;Mouse;P55284,Q99NH2;12562,93742;MI:0019- coimmunoprecipitation | MI:0096- pull down;17057644;40.01.03,42.06,77.03.03.02;"Complex isolated from microvascular endothelial monolayers from mouse myocardium (myEnd). Transient transfection experiments confirmed that the recruitment of PAR-3 by VE-cadherin in living cells is mediated through the PDZ-domain-binding motif of VE-cadherin and PDZ domain 3 of PAR-3.";"";""
824;Anti-SMN protein complex;;Human;Q9UHI6,P57678,O14893,Q16637,P14678;11218,50628,8487,6606,6628;MI:0006- anti bait coimmunoprecipitation;11713266;11.04.03.01,14.10,70.03;"";"";""
825;JBP1-pICln complex;;Human;P54105,O14744,P14678;1207,10419,6628;MI:0006- anti bait coimmunoprecipitation;11713266;14.07.09,14.10,70.03;"";"";""
826;PAR-3-VE-cadherin-beta-catenin complex;;Human;P33151,P35222,Q8TEW0;1003,1499,56288;MI:0019- coimmunoprecipitation;17057644;40.01.03,42.06,70.06;"";"";""
827;NgR-TROY-LINGO1 complex;;Human;Q96FE5,Q9BZR6,Q9NS68;84894,65078,55504;MI:0051- fluorescence technologies;17239012;16.01,73.03.13;"";"";""
828;TRPC1-STIM1-ORAI1 complex;;Human;Q9UQB3,Q96D31,P48995;1501,84876,7220;MI:0019- coimmunoprecipitation | MI:0096- pull down;17224452;18.02.10,20.01.01.01,20.03.01.01,34.01.01.01,70.02;"The results show that all three proteins are essential for generation of TRPC1-SOC channels (store-operated calcium channels). The dynamic assembly of a TRPC1-STIM1-Orai1 complex is involved in activation of Ca2+ entry.";"";""
829;PAR-6-VE-cadherin complex, endothelial;;Human;P33151,(Q9NPB6,Q9BYG4);1003,(50855,84552);MI:0019- coimmunoprecipitation;17057644;40.01.03,42.06,77.03.03.02;"";"";""
830;Trpc1-Stim1-Orai1 complex;;Rat;Q5M848,P84903,Q9QX01;304496,361618,89821;MI:0019- coimmunoprecipitation | MI:0096- pull down;17224452;18.02.10,20.01.01.01,20.03.01.01,34.01.01.01,70.02;"The results show that all three proteins are essential for generation of TRPC1-SOC channels (store-operated calcium channels). The dynamic assembly of a TRPC1-STIM1-Orai1 complex is involved in activation of Ca2+ entry.";"";""
831;PAR-6-PAR-3-VE-cadherin complex, endothelial;;Human;P33151,Q8TEW0,(Q9NPB6,Q9BYG4);1003,56288,(50855,84552);MI:0019- coimmunoprecipitation;17057644;40.01.03,42.06,77.03.03.02;"PAR-3 and PAR-6 are recruited independently to cell-cell contacts and the localization of PAR-6 at cell junctions requires fully matured cell-cell contacts.";"";""
832;Anti-Sm protein complex;;Human;P54105,Q9UHI6,P57678,O14744,O14893,Q16637,P14678;1207,11218,50628,10419,8487,6606,6628;MI:0006- anti bait coimmunoprecipitation;11713266;14.07.09,70.03;"";"";""
833;6S methyltransferase complex;;Human;P54105,P62314,P62318;1207,6632,6634;MI:0029- cosedimentation through density gradients;11713266;14.10,16.01,70.03;"";"";""
834;20S methylosome and RG-containing Sm protein complex;;Human;P54105,O14744,P14678,P62314,P62316,P62318;1207,10419,6628,6632,6633,6634;MI:0029- cosedimentation through density gradients;11713266;11.04.03.01,14.07.09,70.03;"";"";""
835;6S methyltransferase and RG-containing Sm proteins complex;;Human;P54105,P14678,P62314,P62316,P62318,P62304,P62306,P62308;1207,6628,6632,6633,6634,6635,6636,6637;MI:0029- cosedimentation through density gradients;11713266;11.04.03.01,70.03;"snRNPs, integral components of the pre-mRNA splicing machinery, consist of seven Sm proteins which assemble in the cytoplasm as a ring structure on the snRNAs U1, U2, U4, and U5. The survival motor neuron (SMN) protein, the spinal muscular atrophy disease gene product, is crucial for snRNP core particle assembly in vivo. Results indicate that methylation of Sm proteins by the methylosome directs Sm proteins to the SMN complex for assembly into snRNP core particles and suggest that the methylosome can regulate snRNP assembly.";"";""
836;20S methyltransferase core complex; methylosome;Human;P54105,O14744;1207,10419;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;11713266;14.07.09,14.10,16.01,70.03;"The  methylation of Sm proteins by the methylosome directs Sm proteins to the SMN complex for assembly into snRNP core particles and thus the methylosome can regulate snRNP assembly.";"";""
837;20S methyltransferase complex; methylosome;Human;P54105,O14744,Q9BQA1;1207,10419,79084;MI:0006- anti bait coimmunoprecipitation;11756452;14.07.09,14.10,16.01,70.03;"";"";""
838;p27-Cdk2-Fgf2 complex;;Rabbit;A8UKE6,Q0GMK8,P48799;0,0,100009068;MI:0019- coimmunoprecipitation;17209046;14.07.03,77.03.02.02;"";"";""
839;LIN9-BMYB complex;;Human;Q5TKA1,P10244;286826,4605;MI:0019- coimmunoprecipitation;17098733;10.03.01;"";"";""
840;Disc1-Grb2-Kif5a complex;;Rat;Q810H6,P62994,Q6QLM7;307940,81504,314906;MI:0019- coimmunoprecipitation;72012467;14.04,30.01.05,34.05.02,40.01.03.03,73.03.13;"The authors suggest that DISC1 is required for NT-3-induced axon elongation and ERK activation at the distal part of axons by recruiting Grb2 to axonal tips. ";"DISC1 is involved in Schizophrenia.";""
841;SNARE complex (Stx1a, Snap25, Vamp);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0019- coimmunoprecipitation;8824312;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
842;SNARE complex (Stx3, Snap25, Vamp2, Cplx1);;Rat;P63041,P60881,Q08849,P63045;64832,25012,81802,24803;MI:0019- coimmunoprecipitation;8824312;20.09.07.27,20.09.16.09.05,77.03.02.02;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
843;SNARE complex (STX1A, SNAP25, VAMP2);;Bovine;Q9TRF1,P32850,P63026;540853,788566,282116;MI:0019- coimmunoprecipitation;8824312;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
844;SNARE complex (Stx1a, Snap25, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
845;PCI-PSA-SCG2 complex;;Human;P07288,P13521,P05154;354,7857,5104;MI:0401- biochemical;17253189;18.02,73.03.02;"The complex formation among PCI, PSA, and Sg is modulated by several factors in seminal plasma.";"";""
846;RICH1/AMOT polarity complex, Flag-Rich1 precipitated;;Human;Q4VCS5,Q68EM7,P47756,Q9Y5K6,Q8NI35,Q8N3R9,Q96B97,(P52907,P47755);154796,55114,832,23607,10207,64398,30011,(829,830);MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;16678097;18.01.03,18.02.01.01.01,30.01.05.05,40.01.03,41.05.19,42.06,70.06,75.03.09;"In an additional immunoblot the authors show that Par-3 and aPKC likely associate with Rich1 at lower levels than Pals1 and Patj since they were not identified by MS. The authors propose that Rich1 and Amot maintain TJ integrity by the coordinate regulation of Cdc42 and by linking specific components of the TJ to intracellular protein trafficking.";"";""
847;RICH1-PAR3-aPKC polarity complex;;Human;Q68EM7,Q8TEW0,P41743;55114,56288,5584;MI:0007- anti tag coimmunoprecipitation;16678097;18.01.03,18.02.01.01.01,30.01.05.05,40.01.03,42.06,70.06,75.03.09;"Immunoblotting revealed aPKC and the 100 kDa isoform of Par-3, but not Par-6, in Rich1 immunoprecipitates. Par-3 and aPKC likely associate with Rich1 at lower levels than Pals1 and Patj since they were not identified by MS (see complex 846).";"";""
848;RICH1/AMOT polarity complex, Flag-Amot precipitated;;Human;Q4VCS5,Q8IY63,Q9Y2J4,Q68EM7,Q8NI35,O75970,Q8N3R9,Q5T2T1;154796,154810,51421,55114,10207,8777,64398,143098;MI:0007- anti tag coimmunoprecipitation;16678097;18.01.03,18.02.01.01.01,30.01.05.05,40.01.03,41.05.19,42.06,70.06,75.03.09;"The authors suggest that Amot is a component of at least two complexes, only one of which contains Rich1.";"";""
851;SNARE complex (Stx2, Snap25, Vamp2);;Rat;P60881,P50279,P63045;25012,25130,24803;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
852;SNARE complex (Stx3, Snap25, Vamp2);;Rat;P60881,Q08849,P63045;25012,81802,24803;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
853;SNARE complex (Stx4, Snap25, Vamp2);;Rat;P60881,Q08850,P63045;25012,81803,24803;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
854;SNARE complex (Stx1a, Snap25, Vamp8);;Rat;P60881,P32851,Q9WUF4;25012,116470,83730;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
855;SNARE complex (Stx2, Snap25, Vamp8);;Rat;P60881,P50279,Q9WUF4;25012,25130,83730;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
856;SNARE complex (Stx3, Snap25, Vamp8);;Rat;P60881,Q08849,Q9WUF4;25012,81802,83730;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
857;SNARE complex (Stx4, Snap25, Vamp8);;Rat;P60881,Q08850,Q9WUF4;25012,81803,83730;MI:0047- far western blotting;10336434;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
858;CRB3-PALS1-PATJ cell polarity complex;;Dog;Q8QZT4,Q63ZW7,Q9JLB2;224912,12695,56217;MI:0096- pull down;15738264;40.01.03,41.05.19,42.06,70.06,75.03.09;"The authors demonstrate that PATJ is required for the correct formation of tight junctions in MDCKII cells.";"";"Since CRB3, INADL and MPP5 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
859;SNARE complex (Stx4, Stx6, Stx7, Vamp3, Vamp7, Vamp8, Vti1b);;Mouse;P70452,Q9JKK1,O70439,P63024,P70280,O70404,O88384;20909,58244,53331,22319,20955,22320,53612;MI:0019- coimmunoprecipitation;11278762;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
860;DNMT1-G9a-PCNA complex;;Human;P26358,Q96KQ7,P12004;1786,10919,5111;MI:0019- coimmunoprecipitation;17085482;10.01.03,10.01.09.01,14.07.09,42.10.03,70.10;"DNMT1 and G9a are loaded onto the chromatin simultaneously in a ternary complex with loading factor PCNA during chromatin replication. Direct cooperation between DNMT1 and G9a provides a mechanism of coordinated DNA and H3K9 methylation during cell division.";"";""
861;Par-3-p75NTR complex;;Mouse;Q9Z0W1,Q99NH2;18053,93742;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;17082460;41.05.13,42.06.04,43.03.13,45.03.17,47.03.01,70.06.04,73.03.13,75.03.17,77.03.01;"The authors found that Par-3 and p75NTR did not interact in SC/DRG cocultures before the induction of myelination, whereas after induction, Par-3 and p75NTR transiently associated, peaking at 2 days after induction.";"";""
862;DNMT1-G9a complex;;Human;P26358,Q96KQ7;1786,10919;MI:0019- coimmunoprecipitation | MI:0096- pull down;17085482;10.01.03,10.01.09.01,10.03.01.01.05,14.07.09,42.10.03,70.10;"Direct cooperation between DNMT1 and G9a provides a mechanism of coordinated DNA and H3K9 methylation during cell division. The complex of DNMT1 and G9a led to enhanced DNA and histone methylation of in vitro assembled chromatin substrates.";"";""
863;Srf-Myocd-Msx1 complex;;Rat;Q9QUG0,Q8R5I7,Q9JM73;81710,246297,20807;MI:0019- coimmunoprecipitation;17030628;11.02.03.04;"Msx1 or Msx2 formed a ternary complex with SRF and myocardin and inhibited the binding of SRF or SRF/myocardin to the CArG-box motif, resulting in inhibition of their transcription.";"";"Since Srf from rat was not available in the Uniprot database at the time of annotation, the orthologous protein from mouse was used."
864;Srf-Myocd-Msx2 complex;;Rat;P52953,Q8R5I7,Q9JM73;25483,246297,20807;MI:0019- coimmunoprecipitation;17030628;11.02.03.04;"Msx1 or Msx2 formed a ternary complex with SRF and myocardin and inhibited the binding of SRF or SRF/myocardin to the CArG-box motif, resulting in inhibition of their transcription.";"";"Since Srf from rat was not available in the Uniprot database at the time of annotation, the orthologous mouse protein was used."
867;TRAP-SMCC mediator complex;;Human;Q15648,Q9P086,Q9NVC6,Q9BUE0,Q15528,Q71SY5,Q9NX70,Q9NPJ6,Q96G25,A0JLT2;5469,400569,9440,54797,6837,81857,55588,29079,112950,219541;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;14638676;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10;"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
868;aPKC-PAR-6-PAR-3 cell polarity complex;;Dog;Q99NH2,Q9JK83,Q62074;93742,58220,18759;MI:0006- anti bait coimmunoprecipitation;16638806;40.01.03,41.05.19,42.06,70.06,75.03.09;"This study suggests that the suppression of apical PAR-3-aPKC-PAR-6 complex activity by mLgl is mediated through the suppression of the interaction of the aPKC-PAR-6 complex with PAR-3 or Cdc42.";"";"Since  PRKCI, PARD3 and PARD6b from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
871;BRAF53-BRCA2 complex;;Human;O60341,P51587,Q13547,Q92769,Q9P0W2,Q96BD5,Q9UKL0;23028,675,3065,3066,10362,51317,23186;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;11207365;10.01.05.01,10.01.09.05,10.03.01.01,11.02.03.04.03,14.07.04,16.03.01,42.10.03,43.03.13,70.10;"Antibody microinjection experiments suggest a role for BRCA2/BRAF35 complex in modulation of cell cycle progression. ";"BRCA2 confers susceptibility to in breast cancer.";""
872;SNARE complex (Stx1a, Snap29);;Rat;Q9Z2P6,P32851;116500,116470;MI:0019- coimmunoprecipitation;11707603;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
873;SNARE complex (STX1A, SNAP29);;Human;O95721,Q16623;9342,6804;MI:0019- coimmunoprecipitation;11707603;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
874;SNARE complex (VAMP3, VAMP4, VAMP8, STX6);;Human;O43752,Q15836,O75379,Q9BV40;10228,9341,8674,8673;MI:0019- coimmunoprecipitation;11839770;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
875;SNARE complex (VAMP3, VAMP4, STX16);;Human;O14662,Q15836,O75379;8675,9341,8674;MI:0019- coimmunoprecipitation;11839770;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
876;SNARE complex (VAMP3, STX6, VTI1A);;Human;O43752,Q15836,Q96AJ9;10228,9341,143187;MI:0019- coimmunoprecipitation;11839770;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
877;SNARE complex (VAMP4, STX6, STX16, VTI1a, VTI1b);;Human;O14662,O43752,O75379,Q96AJ9,Q9UEU0;8675,10228,8674,143187,10490;MI:0019- coimmunoprecipitation;11839770;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
878;Prkac-Akap5-Adrb1 complex;;Rat;P18090,P24587,(P27791,P68182);24925,171026,(25636,293508);MI:0019- coimmunoprecipitation | MI:0055- fluorescent resonance energy transfer;16940053;14.07.03,30.05.02.24;"AKAP79 provides PKA to phosphorylate the beta(1)-AR and thereby dictate the recycling and resensitization itineraries of the beta(1)-AR.";"ADRB1 is involved in hypertension and heart failure.";""
879;PRKAC-AKAP5-ADRB1 complex;;Human;P08588,P24588,(P17612,P22694,P22612);153,9495,(5566,5567,5568);MI:0019- coimmunoprecipitation | MI:0055- fluorescent resonance energy transfer;16940053;14.07.03,30.05.02.24;"AKAP79 provides PKA to phosphorylate the beta(1)-AR and thereby dictate the recycling and resensitization itineraries of the beta(1)-AR.";"ADRB1 is involved in hypertension and heart failure.";""
880;SNARE complex (Vamp4, Stx6, Stx16, Vti1b);;Rat;B5DF99,Q63635,O70480,P58200;362283,60562,53330,366673;MI:0019- coimmunoprecipitation;12067063;20.09.07.25,20.09.07.29,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. This complex may have a role in synaptic vesicle biogenesis or recycling. ";"";"Since VAMP-4 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
881;SNARE complex (Vamp4, Stx6, Stx16, Vti1a);;Rat;B5DF99,Q63635,O70480,Q9JI51;362283,60562,53330,65277;MI:0019- coimmunoprecipitation;12067063;20.09.07.25,20.09.07.29,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. This complex may have a role in synaptic vesicle biogenesis or recycling. ";"";"Since VAMP-4 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
882;PAR-6-aPKC-PAR-3 complex;;Dog;Q99NH2,Q62074,(Q9Z101,Q9JK83);93742,18759,(56513,58220);MI:0019- coimmunoprecipitation;11532031;40.01.03,41.05.19,42.06,70.06,75.03.09;"The ternary complex formation and junctional co-localization of PAR-6 with aPKC and ASIP/PAR-3 are observed during the early stage of epithelial cell polarization. PAR-6 forms a stable protein complex through the disappearance and reformation of cell-cell contact induced by calcium switch.";"";"Since PARD6, PARD3 and PRKCI from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
883;PAR-6-aPKC-PAR-3-Cdc42-Rac1 complex;;Dog;P60766,Q99NH2,Q62074,P63001,(Q9Z101,Q9JK83);12540,93742,18759,19353,(56513,58220);MI:0019- coimmunoprecipitation;11532031;30.01.05.05.01,40.01.03,41.05.19,42.06,70.06,75.03.09;"This is the first in vivo evidence for a molecular interaction between the PAR-6-aPKC-PAR-3 ternary complex and Cdc42-Rac1.";"";"Since the proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
884;GluR1-cadherin-catenin complex;;Rat;Q9Z1Y3,Q9WU82,P19490;83501,84353,50592;MI:0019- coimmunoprecipitation;16515543;45.03.17,73.03.13;"";"";""
885;Glur4-cadherin-catenin complex;;Rat;Q9Z1Y3,Q9WU82,P19493;83501,84353,29629;MI:0019- coimmunoprecipitation;16515543;45.03.17,73.03.13;"";"";""
886;MTA1 complex;;Human;Q6IT96,Q92769,O95983,Q13330,Q09028,Q16576;3065,3066,53615,9112,5928,5931;MI:0004- affinity chromatography technologies | MI:0091- chromatography technologies;12920132;10.01.09.05,11.02.03.04.03,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"";"MTA1 is involved in metastasis or cancer formation. ";"Several other subunits of the complex were found in the analysis, which have not been further characterized: p68, p66 and three so-called MTA1-associated proteins."
887;Glur2-Glur4-Plp-Itgav complex;;Rat;Q63845,P19491,P19493,P43406,P60203;0,29627,29629,16410,24943;MI:0019- coimmunoprecipitation;16510724;30.05.02.24.06,77.03.01;"The coimmunoprecipitation studies showed an increased association of GluR2 and GluR4 subunits of AMPA receptor with the {alpha}v integrin/PLP complex after agonist stimulation of AMPA receptor (PMID:16510724).";"";"Since ItgaV from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
888;MTA2 complex;;Human;Q14839,Q13547,Q92769,O95983,O94776,Q09028,Q16576,(Q96ST3,O75182);1108,3065,3066,53615,9219,5928,5931,(25942,23309);MI:0004- affinity chromatography technologies | MI:0091- chromatography technologies;12920132;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,70.10;"Since MTA2 is not involved in metastasis or cancer formation, the authors suggest a housekeeping role of the MTA2 complex.";"";""
889;MTA1-HDAC core complex;;Human;Q6IT96,Q92769,Q13330,Q09028,Q16576;3065,3066,9112,5928,5931;MI:0004- affinity chromatography technologies | MI:0091- chromatography technologies;12920132;10.01.09.05,11.02.03.04.03,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"";"MTA1 is involved in metastasis or cancer formation.";""
890;PAR-3-PKCz-Tiam2 complex;;Rat;Q9Z340,P09217,Q6ZPF3;81918,25522,24001;MI:0019- coimmunoprecipitation;15723051;40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"";"";"Since Tiam2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
891;PAR-3-PKC-zeta-Tiam1 complex;;Rat;Q9Z340,P09217,Q60610;81918,25522,21844;MI:0019- coimmunoprecipitation;15723051;40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"";"";"Since Tiam1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
892;PAR-3-aPKC-Tiam2 complex;;Rat;Q9Z340,Q62074,Q6ZPF3;81918,18759,24001;MI:0019- coimmunoprecipitation;15723051;40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"";"";"Since aPKC and Tiam2 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
893;PAR-3-aPKC-Tiam1 complex;;Rat;Q9Z340,Q62074,Q60610;81918,18759,21844;MI:0019- coimmunoprecipitation;15723051;40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"";"";"Since aPKC and Tiam1 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
894;Tiam2-PAR-3-aPKC-PAR-6-Cdc42-GTP complex;;Rat;Q8CFN2,Q9Z340,Q6B4M5,P97701,Q6ZPF3;64465,81918,307799,84006,24001;MI:0096- pull down;15723051;30.01.05.05.01,40.01.03,41.05.13,41.05.19,43.03.13,73.03.13;"STEF-DeltaN (Tiam2) interacted with GST-Cdc42-GTPgammaS only in the presence of exogenous PAR-6-aPKC-PAR-3. However, the association of STEF-DeltaN with Cdc42 was not detected in the absence of PAR-3, indicating that STEF forms a complex with activated Cdc42 through the interaction with PAR-3. For pull down analyses immobilized beads were incubated with COS7 cell lysate expressing the indicated proteins.";"";"Since Tiam2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
895;hMediator complex (MED23, CDK8, CCNC, MED7);;Human;P24863,P49336,Q9ULK4,O43513;892,1024,9439,9443;MI:0071- molecular sieving | MI:0226- ion exchange chromatography | MI:0006- anti bait coimmunoprecipitation;10353252;11.02.03.04.01,18.01.07,18.02.09,70.10;"The high-molecular-mass mammalian Mediator complexes have many subunits in common. However, their reported subunit compositions are not identical (PMID:10838567).";"";""
896;hMediator complex (MED23, CDK8, CCNC);;Human;P24863,P49336,Q9ULK4;892,1024,9439;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;11416138;11.02.03.04.01,18.01.07,18.02.09,70.10;"The high-molecular-mass mammalian Mediator complexes have many subunits in common. However, their reported subunit compositions are not identical (PMID:10838567).";"";""
897;CDK8-CyclinC-Mediator complex;;Human;P24863,P49336;892,1024;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;11416138;11.02.03.04.03,14.07.03,18.01.01,18.02,70.10;"It has been shown hat CDK8 phosphorylates the cyclin H subunit of TFIIH and inhibits its function in transcription (PMID:10993082). This explains, why the CDK8-CyclinC-Mediator complex inhibits basal and activated transcription.";"";""
898;Mediator complex 1;High-molecular-mass Mediator complex 1 | 2MDa Mediator complex 1;Human;P24863,P49336,O60244,Q9ULK4,O75586;892,1024,9282,9439,10001;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;11416138;11.02.03.04.01,18.01.07,18.02.09,70.10;"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
899;Par-3-KIF3A-PKC-zeta complex;;Rat;Q9WV62,Q9Z340,P09217;84392,81918,25522;MI:0006- anti bait coimmunoprecipitation;15048131;20.09.14,40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"Coimmunoprecipitation done with anti-PAR-3 or with anti-KIF3A yielded the same results.";"";""
900;Mediator complex 2;High-molecular-mass Mediator complex 2 | 2MDa Mediator complex 2;Human;O60244,Q9ULK4,O75586;9282,9439,10001;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;11416138;11.02.03.04.01,18.01.07,18.02.09,70.10;"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
901;Par-3-KIF3A-aPKC complex;;Rat;Q9WV62,Q9Z340,Q62074;84392,81918,18759;MI:0006- anti bait coimmunoprecipitation;15048131;20.09.14,40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"";"";"Since aPKC from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
902;SNARE complex (Stx5, Gosr1, GS15);;Rat;O35152,Q62931,Q08851;54400,94189,65134;MI:0019- coimmunoprecipitation;12070132;20.09.07.27,20.09.16.09.05,70.08,77.03.11.07;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
903;RET-Rai complex;;Human;P07949,Q92529;5979,53358;MI:0019- coimmunoprecipitation;15940252;30.05;"RAI protein forms complexes with two variants of RET oncoprotein: MEN2A and PTC.";"";""
904;SHC3-GAB1 complex;;Human;Q13480,Q92529;2549,53358;MI:0019- coimmunoprecipitation;15940252;30.05;"RAI protein forms complexes with two variants of RET oncoprotein: MEN2A and PTC.";"";""
905;KIF3A/B-PAR-3-aPKC-PAR-6 complex;;Mammalia;Q9Y496,O15066,Q8TEW0,P41743,(Q9NPB6,Q9BYG5);11127,9371,56288,5584,(50855,84612);MI:0007- anti tag coimmunoprecipitation;15048131;20.09.14,40.01.03,41.05.13,41.05.19,43.03.13,73.03.13;"The results indicate that PAR-3 interacts with KIF3 in vivo and that aPKC associates with KIF3 through its interaction with PAR-3.";"";""
906;ADAR1-CDK2 complex;;Human;P55265,P24941;103,1017;MI:0019- coimmunoprecipitation;17224799;10.03.01,14.07.03;"";"";""
907;SNARE complex (Stx5, Gosr1, Bet1, Gef2);;Rat;Q62896,P60522,Q62931,Q08851;29631,64670,94189,65134;MI:0019- coimmunoprecipitation;12070132;20.09.07.27,20.09.16.09.05,70.08,77.03.11.07;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. Following the MGI nomenclature GEF-2 and GATE-16 are identical.";"";""
908;PAR-6-aPKC-PAR-3 complex;;Dog;Q99NH2,Q62074,(Q9Z101,Q9JK83);93742,18759,(56513,58220);MI:0019- coimmunoprecipitation;11257119;40.01.03,41.05.19,42.06,70.06,75.03.09;"PAR-6 immunoprecipitates specifically contain endogenous aPKC-lambda, full-length PAR-3, and its splicing variant.";"";"Since  PARD6, PARD3 and PRKCI from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
909;ARC92-Mediator complex; A-Med complex;Human;P49336,Q15648,Q93074,Q9UHV7,O60244,Q96RN5,Q9Y2X0,Q9NVC6,Q9ULK4,Q71SY5,O95402,O75586,O43513;1024,5469,9968,9969,9282,51586,10025,9440,9439,81857,9441,10001,9443;MI:0006- anti bait coimmunoprecipitation;14657022;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10;"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
910;CRSP-Mediator 2 complex; CRSP-Med 2 complex;Human;O60244,Q96RN5,Q9Y2X0,Q9NVC6,Q9BUE0,Q9ULK4,O75448,Q9NPJ6,O75586,O43513;9282,51586,10025,9440,54797,9439,9862,29079,10001,9443;MI:0029- cosedimentation through density gradients | MI:0040- electron microscopy | MI:0004- affinity chromatography technologies;15175162;11.02.03.04.01,18.01.07,18.02.09,70.10;"The CRSP-Med 2 complex is a promotor-selective coactivator. It cannot activate transcription from a VDR-responsive promoter, which needs coactivator recruitment by Med220. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: p97 and p26."
911;Par3-Apc-Kif3a complex;;Rat;P70478,Q9WV62,Q9Z340;24205,84392,81918;MI:0006- anti bait coimmunoprecipitation;15556865;20.09.14,40.01.03,41.05.13,41.05.19,43.03.13,73.03.13,77.03.01.01.01;"The results suggest that mPar3 is polarized in developing neurons through APC- and kinesin-mediated transport to the plus ends of rapidly growing microtubules at the nascent axon tip, a process that involves a spatially regulated GSK-3beta activity.";"";""
912;Kal1-Fgfr1 complex;;Rat;Q04589,P23352;79114,3730;MI:0019- coimmunoprecipitation;17186267;30.05.01.12.03,47.03.02.02,77.03.02.02;"";"";"Since Kal1 protein from rat was not available in the UniProt database at the time of annotation, the orthologous human protein was used."
913;SNARE complex (Stx1a, Snap25, Cplx2, Vamp2);;Rat;P84087,P60881,P32851,P63045;116657,25012,116470,24803;MI:0047- far western blotting;11751907;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
914;PALS1-PATJ-CRB3-PAR3-PAR6-aPKC-14-3-3 zeta complex;;Dog;Q8QZT4,Q63ZW7,Q9JLB2,Q99NH2,Q9Z101,Q62074,P63101;224912,12695,56217,93742,56513,18759,22631;MI:0096- pull down;14653998;40.01.03,41.05.19,42.06,70.06;"The authors previously demonstrated that the PALS1/PATJ/CRB3 and Par3/Par6/aPKC complexes interact via PALS1-Par6 binding. Component Par6 was not shown in the pull down experiment. Immobilized CRB3 carboxy-terminal peptides were used for precipitation. The authors suggest that Par3 phosphorylation and subsequent 14-3-3 binding is a crucial mechanism that regulates the function of the Par3/Par6/aPKC complex.";"";"Since  several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
915;SNARE complex (SNAP23, STX1A);;Human;O00161,Q16623;8773,6804;MI:0019- coimmunoprecipitation | MI:0096- pull down;12209004;18.02.10,20.01.01.07.09,20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. SNAP-23 physically associates with CFTR by binding to its amino-terminal tail, a region that modulates channel gating.";"";""
916;PALS1-Par3-aPKC-14-3-3 zeta complex;;Dog;Q9JLB2,Q99NH2,Q62074,P63101;56217,93742,18759,22631;MI:0096- pull down;14653998;40.01.03,41.05.19,42.06,70.06;"Immobilized GST-14-3-3 zeta was used for precipitation. The authors found that of the polarity proteins examined, Par3 was highly enriched after GST-14-3-3 zeta pulldown, suggesting that 14-3-3 zeta may directly associate with Par3.";"";"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.  "
917;CERF complex (CECR2-containing remodeling factor complex);;Human;Q9BXF3,P28370;27443,6594;MI:0071- molecular sieving | MI:0007- anti tag coimmunoprecipitation;15640247;10.01.09.05,41.05.13,42.10.03,70.10;"CERF displays an ATP hydrolyzing activity that is stimulated by nucleosomes. CERF plays a critical role in neurolation.";"";""
918;PAR3-PAR6-PALS1 complex;;Human;Q8N3R9,Q8TEW0,Q9NPB6;64398,56288,50855;MI:0007- anti tag coimmunoprecipitation;12545177;40.01.03,41.05.19,42.06,70.06;"HEK 293 cells transiently expressed with Mys-PALS1 and HA-Par6 or HA-Par3 showed that Par6, but not Par3, coimmunoprecipitated with PALS1. However, when all three proteins were expressed together, the authors detected a complex of PALS1 with both Par6 and Par3.";"";""
919;hNURF complex;;Human;Q12830,Q09028,Q16576,P28370;2186,5928,5931,6594;MI:0071- molecular sieving | MI:0007- anti tag coimmunoprecipitation;15640247;10.01.09.05,11.02.03.04,41.05.13,42.10.03,43.03.13,70.10;"hNURF possesses ATP-dependent chromatin remodeling activity and regulates engrailed-1 (en-1) and engrailed-2 (en-2) expression.";"";""
920;PAR3-PATJ-PALS1 complex;;Dog;Q63ZW7,Q9JLB2,Q99NH2;12695,56217,93742;MI:0007- anti tag coimmunoprecipitation;12545177;40.01.03,41.05.19,42.06,70.02,70.06;"The authors found that endogenous Par3 and PATJ were both coimmunoprecipitated with Myc-PALS1. Collectively, these data indicate that the Crb-PALS1-PATJ and Par3-Par6-aPKC complexes can associate with one another through a PALS1-Par6 interaction.";"";"Since  several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
921;Remodeling and spacing factor (RSF) complex;;Human;Q96T23,O60264;51773,8467;MI:0091- chromatography technologies;9836642;01.03,10.01.09.05,11.02.03.01.01,42.10.03,70.10;"RSF facilitates transcription initiation by remodeling nucleosomes in the promoter region to allow the formation of preinitiation complexes.";"";""
922;SNARE complex (Stx1a, Snap25, Cplx2, Vamp2);;Rat;P84087,P60881,P32851,P63045;116657,25012,116470,24803;MI:0047- far western blotting;10777504;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
923;SNF2L-RSF1 complex;;Human;Q96T23,P28370;51773,6594;MI:0071- molecular sieving | MI:0007- anti tag coimmunoprecipitation;15640247;10.01.09.05,42.10.03,70.10;"";"";""
924;Toposome;;Human;Q9NR30,Q08211,P07910,Q6P2Q9,Q96SB4,Q08945,P11388;9188,1660,3183,10594,6732,6749,7153;MI:0226- ion exchange chromatography | MI:0019- coimmunoprecipitation;15034300;10.01.02,10.03.01,16.03.01,70.10;"During chromosome segregation, the toposome complex separates entangled circular chromatin DNA about fourfold more efficiently than topoisomerase IIalpha alone.";"";""
925;WCRF complex; WCRF/hACF complex;Human;Q9NRL2,O60264;11177,8467;MI:0091- chromatography technologies;10655480;10.01.09.05,11.02.03.04,42.10.03,70.10;"ATPase activity of WCRF complex is stimulated by nucleososmal DNA.";"";""
926;SCRIB-LGL2 complex;;Human;Q6P1M3,Q14160;3993,23513;MI:0276- blue native page | MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;16791850;40.01.03,41.05.19,70.02,70.03;"Analyses done to localize the association of the proteins showed that exogenously expressed Scrib and Lgl2 can interact in either location (at the membrane and in the cytosol).";"";""
927;CENP-A nucleosome associated complex; CENP-A NAC complex;Human;Q03188,Q9H3R5,Q9NSP4,Q96H22,Q96BT3,Q71F23;1060,64946,79019,55839,80152,79682;MI:0676- tandem affinity purification;16622419;10.01.09.07,10.03.04.01,10.03.04.05,10.03.05.01,70.10.03;"Assembly of CENP-A NAC complex at centromeres is dependent on CENP-M, CENP-N and CENP-T.";"";""
928;SCRIB-VANGL2 complex;;Human;Q14160,Q9ULK5;23513,57216;MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down;16791850;41.05.19,70.02,75.03.09;"When human EGFP-hVangl2  fusion proteins expressed in transfected MDCK cells were quantitatively immunoprecipitated with anti-GFP, a small (2%) but reproducible amount of total endo Scrib was found in the full-length hVangl2 immunoprecipitate. Further analyses done in HEK293A cell extracts.";"";""
929;CEN complex; centromer chromatin complex;Human;P35226,Q9BZH6,Q13185,Q9HC52,P49450,P07199,Q03188,Q9H3R5,Q92674,Q9BS16,Q8N0S6,Q9NSP4,Q9BU64,Q53SF7,Q13619,Q16531,Q92620,P22087,P11021,P11142,Q69YN4,Q02241,Q6T4P5,Q71F23,Q8N1F7,Q9H0H5,Q06587,Q99496,Q96T23,Q8NEM2,O60264,Q9BXP5,Q08945,Q9Y5B9,Q15007,Q5T200,Q96JP5;648,55717,11335,57332,1058,1059,1060,64946,2491,64105,91687,79019,79172,22837,8451,1642,9785,2091,3309,3312,25962,9493,79948,79682,9688,29127,6015,6045,51773,79801,8467,51593,6749,11198,9589,23091,80829;MI:0402- chromatin immunoprecipitation assays | MI:0006- anti bait coimmunoprecipitation;15009096;10.03.01.01,10.03.04.01,10.03.05.01,70.10.03;"";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: unknown protein (40kD) and a protein similar to Riken cDNA 2610510J17."
930;Scrib-beta-PIX-GIT1 complex;;Human;Q14155,Q9Y2X7,Q14160;8874,28964,23513;MI:0006- anti bait coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes | MI:0096- pull down;15182672;20.09.16.09.03,41.05.13,70.02,70.06,73.03.13,75.03.09,75.03.17;"Yeast two-hybrid analysis showed that beta-PIX directly interacts with hScrib and hScrib PDZ domains. GIT1 had no affinity for Scrib but, as expected, directly bound to beta-PIX. The data highlight the important role of hScrib in the retention of beta-PIX at the plasma membrane upon membrane depolarization.";"";""
931;Scrib-beta-PIX-GIT1 complex;;Mouse;Q9ES28,Q68FF6,Q80U72;54126,216963,105782;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;15182672;20.09.16.09.03,41.05.13,70.02,70.06,73.03.13,75.03.09,75.03.17;"";"";""
932;Ppar(alpha)-Pric320 complex;;Rat;Q8BYH8,P37230;109151,25747;MI:0019- coimmunoprecipitation;16554032;11.02.03.04.01,70.10;"";"";"Since Pric320 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
933;SCRIB-APC complex;;Human;P25054,Q14160;324,23513;MI:0096- pull down | MI:0006- anti bait coimmunoprecipitation;16611247;40.01.03,41.05.13.01,41.05.19,42.06,43.03.13,45.03.09;"The in vitro translated APC bound to the PDZ domains 1 and 4 of hScrib. Mutational analysis provided the evidence that APC interacts with hScrib through its C terminal class 1 PDZ domain-binding sequence Threonine-X-Valine, which is shared by the C terminal sequences of the high-risk HPV E6 proteins.";"";""
934;FACT-NEK9 complex;;Human;Q8TD19,Q08945,Q9Y5B9;91754,6749,11198;MI:0006- anti bait coimmunoprecipitation;14660563;10.01.09.05,10.03.01.01.03,11.02.03.01.04,14.07.03,42.10.03,70.10;"Nek9 forms a stable, approximately 600-kDa complex with FACT in the interphase nuclei.";"";""
935;Scrib-APC-beta-catenin complex;;Mouse;Q61315,Q02248,Q80U72;11789,12387,105782;MI:0006- anti bait coimmunoprecipitation;16611247;40.01.03,41.05.13.01,41.05.19,42.06,43.03.13,45.03.09,73.03.13,75.03.17,77.03.01.01.01;"";"";""
936;FACT complex;;Human;Q08945,Q9Y5B9;6749,11198;MI:0006- anti bait coimmunoprecipitation;10421373;10.01.09.05,11.02.03.01.04,42.10.03,70.10;"FACT (for facilitates chromatin transcription) is a chromatin-specific elongation factor required for transcription of chromatin templates in vitro.";"";""
938;FACT complex, UV-activated; p53 Ser-392 kinase complex;Human;P68400,P19784,P67870,Q08945,Q9Y5B9;1457,1459,1460,6749,11198;MI:0071- molecular sieving;11239457;01.04,14.07.03,16.01,18.01.07,18.02,32.01.09,32.01.13,70.10;"In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53. Phosphorylation by the kinase complex enhances p53 activity.";"";""
939;Dysferlin-Dhpr complex;;Rat;Q02485,Q9ESD7;682930,26903;MI:0019- coimmunoprecipitation;16550931;16.01,75.03.12.01;"";"Dysf is involved in Miyoshi myopathy and limb-girdle muscular dystrophy 2B.";"Since Dysf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
940;AnnexinVI-Fyn-Pyk2-RasGAP complex;;Rat;P48037,Q62844,P70600,P50904;79125,25150,50646,25676;MI:0019- coimmunoprecipitation;10708762;16.01,30.01;"";"";""
941;Arf1-Ap1g1-Ap1b1 complex;;Rat;P52303,B2RYN6,P84079;29663,171494,64310;MI:0019- coimmunoprecipitation;10807927;16.01,20.09.07;"";"";""
942;Cd44-Ots8 complex;;Rat;P26051,Q64294;25406,54320;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;10903424;34.05.01,40.01.03.01,45.03.11,77.03.03.02;"TS-8 may alter the mode of endothelial cell growth and/or migration induced by CD44 in tumor angiogenesis.";"CD44 is involved in adhesion interactions and tumor metastasis. ";""
943;Class C Vps complex (VPS11, VPS18, STX7);;Human;O15400,Q9H270,Q9P253;8417,55823,57617;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;11382755;20.09.07,70.22,70.25;"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes and mediate vesicle trafficking steps in the endosome/lysosome pathway.";"";""
944;Class C Vps complex (VPS11, VPS18, VPS16);;Human;Q9H270,Q9H269,Q9P253;55823,64601,57617;MI:0019- coimmunoprecipitation;11382755;20.09.07,70.22,70.25;"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes, mediate vesicle trafficking steps in the endosome/lysosome pathway and are suggested to play a role in SNARE complex assembly.";"";""
945;Class C Vps complex (hVPS11, hVPS18, rVPS33a );;Mammalia;Q9H270,Q9P253,Q63615;55823,57617,65081;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;11382755;20.09.07,70.22,70.25;"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes, mediate vesicle trafficking steps in the endosome/lysosome pathway and are suggested to play a role in SNARE complex assembly.";"";""
946;Class C Vps complex (hVPS11, hVPS18, hVPS16, rVPS33a );;Mammalia;Q9H270,Q9H269,Q9P253,Q63615;55823,64601,57617,65081;MI:0019- coimmunoprecipitation;11382755;20.09.07,70.22,70.25;"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes, mediate vesicle trafficking steps in the endosome/lysosome pathway and are suggested to play a role in SNARE complex assembly.";"";""
947;CDC7-DBF7 complex;;Human;O00311,Q9UBU7;8317,10926;MI:0019- coimmunoprecipitation;10523313;10.01.03,10.01.11;"";"";""
948;Kif17-Lin10 complex;;Mouse;Q6PER2,Q99PW8;234678,16559;MI:0018- two hybrid | MI:0107- surface plasmon resonance;10846156;20.09.14,34.05.02,41.05.13,43.03.13,73.03.13;"The authors suggest that KIF17, a neuron-specific molecular motor with microtubule plus-end-directed motility interacts directly with a mLin-10 PDZ domain, resulting in the transport of NR2B in dendrites. They propose this motor-cargo complex as the sorting machinery for NR2B.";"";""
949;SNARE complex (Stx1a, Snap25, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0114- x-ray crystallography;15316007;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
950;SNARE complex (Stx1a, Snap25, Stxbp5);;Rat;P60881,P32851,Q9WU70;25012,116470,81022;MI:0114- x-ray crystallography;15316007;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
951;Fmrp-Lgl complex;;Mouse;P35922,Q80Y17;14265,16897;MI:0019- coimmunoprecipitation;15621528;41.05.13.01,77.03.01.01.01;"The Fmrp/Lgl/mRNA complex is developmentally regulated in mice.";"FMR1 gene is involved in Fragile X syndrome.";""
952;Kif13a-AP1 complex;;Mouse;O35643,P35585,Q8CA55,(P22892,O88512);11764,11767,16553,(11765,11766);MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid | MI:0027- cosedimentation;11106728;20.01.10,20.09.07,77.03.01.01.01;"KIF13A transports the mannose-6-phosphate receptor to the plasma membrane through direct interaction with AP-1 complex.";"";""
953;p97-Ufd1-Npl4-IP3 receptor complex;;Mouse;P11881,P60670,P70362,Q01853;16438,217365,22230,269523;MI:0006- anti bait coimmunoprecipitation;16103111;14.13.01.01,16.01,30.01.09.11,70.07;"The p97-Ufd1-Npl4 complex couples ubiquitinated IP3 receptors to proteasomal degradation and plays a key role in IP3 receptor processing. These data also establish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalian cells.";"";""
954;p97-Ufd1-Npl4-IP3 receptor complex;;Rat;P29994,Q9ES54,Q9ES53,P46462;25262,140639,84478,116643;MI:0006- anti bait coimmunoprecipitation;16103111;14.13.01.01,16.01,30.01.09.11,70.07;"The p97-Ufd1-Npl4 complex couples ubiquitinated IP3 receptors to proteasomal degradation and plays a key role in IP3 receptor processing. These data also establish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalian cells.";"";""
955;LLGL2-PAR-6B-PRKCI complex;;Human;Q6P1M3,Q9BYG5,P41743;3993,84612,5584;MI:0007- anti tag coimmunoprecipitation;12725730;40.01.03,41.05.19,42.06,70.06,75.03.09;"Mammalian Lgl-2 competes with PAR-3 for its incorporation to the PAR-6B/aPKC lambda complex in cDNA-transfected 293T cells  and support the presence of two independent protein complexes containing PAR-6B/aPKC lambda. Further results indicate that mLgl-2 interacts with the PDZ domain of PAR-6B and with the kinase domain of aPKC lambda and forms a protein complex independently of the one containing PAR-3. It was suggested that phosphorylation of mLgl-1/2 by aPKC lambda occurs during the cell-cell contact-induced cell polarization and that this is accompanied by dissociation of the interaction between mLgl-2 and the PAR-6B/aPKC lambda complex.";"";""
956;PAR-3-PAR-6B-PRKCI complex;;Human;Q8TEW0,Q9BYG5,P41743;56288,84612,5584;MI:0007- anti tag coimmunoprecipitation;12725730;40.01.03,41.05.19,42.06,70.06,75.03.09;"Mammalian Lgl-2 competes with PAR-3 for its incorporation to the PAR-6B/aPKC lambda complex in cDNA-transfected 293T cells  and support the presence of two independent protein complexes containing PAR-6B/aPKC lambda.";"";""
957;p97-Ufd1-Npl4 complex;;Rat;Q9ES54,Q9ES53,P46462;140639,84478,116643;MI:0004- affinity chromatography technologies;10811609;01.04,14.13.01.01,32.01.07,70.03,77.03.11.07;"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes in cytosol.";"";""
958;Ufd1-Npl4 complex;;Rat;Q9ES54,Q9ES53;140639,84478;MI:0004- affinity chromatography technologies;10811609;14.13.01.01,70.03,77.03.11.07;"This protein complex acts as adapters, directing a basic TER ATPase activity into different cellular pathways.";"";""
959;LLGL1-PAR-6B-PRKCI complex;;Human;Q15334,Q9BYG5,P41743;3996,84612,5584;MI:0019- coimmunoprecipitation;12725730;40.01.03,41.05.19,42.06,70.06,75.03.09;"Experiments done in lysates of MDCK, MTD-1A, or Caco 2 cells. The results indicate that PAR-6/aPKC selectively interacts with either mLgl or PAR-3 under the control of aPKC activity to regulate epithelial cell polarity.";"";""
960;p97-p47 oligomer complex;;Rat;O35987,P46462;83809,116643;MI:0071- molecular sieving;9214505;01.04,20.09.07.27,42.08,70.03,70.08,77.03.11.07;"p47 is a cofactor for p97-mediated membrane fusion (one trimer of p47 per hexamer of p97).";"";""
961;Tamalin-mGluR1a-cytohesin complex;;Rat;Q8R4T5,P23385,P63035;192254,24414,116692;MI:0019- coimmunoprecipitation;11850456;14.04,30.05.02.24.05,77.03.01.01.01;"The authors  suggest that the PDZ domain-containing proteins like tamalin may play a key role in connecting glutamate receptors to small GTP-binding proteins that regulate intracellular protein transport and synaptic organization.";"";""
962;Tamalin-mGluR1a complex;;Rat;Q8R4T5,P23385;192254,24414;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;11850456;14.04,30.05.02.24.05,77.03.01.01.01;"The authors show that tamalin causes an increase in not only cell-surface expression of mGluR1a in transfected cells but also in neuritic distribution of endogenous mGluR5 in cultured hippocampal neurons.";"";""
963;Tamalin-mGluR5 complex;;Rat;Q8R4T5,P22756;192254,29559;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;11850456;14.04,30.05.02.24.05,77.03.01.01.01;"The authors show that tamalin causes an increase in not only cell-surface expression of mGluR1a in transfected cells but also in neuritic distribution of endogenous mGluR5 in cultured hippocampal neurons.";"";""
964;BRCA1-RAD50-MRE11-NBS1 complex; BRCA1-RAD50-MRE11-p95 complex;Human;P38398,P49959,O60934,Q92878;672,4361,4683,10111;MI:0006- anti bait coimmunoprecipitation;10426999;10.01.05.01,32.01.09,70.10;" ";"BRCA1 is involved in breast cancer.";""
965;mPar6c-Mlgl-aPKC complex;;Mouse;Q80Y17,Q9Z101,Q62074;16897,56513,18759;MI:0006- anti bait coimmunoprecipitation;12629547;40.01.03,41.05.19,45.03.09;"The data suggest that the phosphorylation of Mlgl by aPKC is important for appropriate cell polarization in the wounding assay. The authors propose that an interaction between Mlgl, mPar-6C and aPKC, and the consequent phosphorylation of Mlgl, may regulate Mlgl in a polarized fashion such that it can exert localized effects on protein trafficking and secretion.";"";""
966;Rab27A-Melanophilin-MyosinVa complex;;Mouse;Q91V27,Q99104,Q9ERI2;171531,17918,11891;MI:0019- coimmunoprecipitation;11856727;20.01.10;"";"Mutation in the Myo5a gene causes pigment granule transport defects in human Griscelli syndrome.";""
967;Pallidin-Mu complex; BLOC-1 complex;Mouse;Q8R015,Q9R0C0;17828,18457;MI:0019- coimmunoprecipitation;12019270;42.25,77.03.02.05;"The authors propose that BLOC-1 mediates the biogenesis of lysosome-related organelles by a mechanism that may involve self-assembly and interaction with the actin cytoskeleton.";"";""
968;Crb1-Mupp1-Pals1-Mpp4 complex;;Mouse;Q8VHS2,Q8VBX6,Q6P7F1,Q9JLB2;170788,17475,227157,56217;MI:0006- anti bait coimmunoprecipitation;15316081;36.25.01.01,40.01.03,42.06,47.03.02.02,70.06,77.03.02.02;"In Crb1-/- retinas before the onset of retinal degeneration, the complex between Mupp1, Pals1 and Mpp4 formed in the absence of Crb1, indicating that Crb1 is not essential for this interaction.";"";""
969;CRB3-PALS1-PATJ cell polarity complex;;Dog;Q8QZT4,Q63ZW7,Q9JLB2;224912,12695,56217;MI:0006- anti bait coimmunoprecipitation;12527193;40.01.03,41.05.19,42.06,70.06,75.03.09;"CRB3, PATJ and PALS1 form a ternary complex in MDCK epithelial cells.";"";"Since CRB3, INADL and MPP5 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
970;Rab11Fip2-Ap2a complex;;Mouse;Q3U366,(P17426,P17427);74998,(11771,11772);MI:0096- pull down;12364336;20.09.18.09.01.01;"Rab11-FIP2 influences endocytosis through its ability to interact with the adaptor complex AP-2.";"";""
971;Rab11-Fip2-Reps1 complex;;Mammalia;Q3U366,O54916;74998,19707;MI:0019- coimmunoprecipitation;12364336;14.04,20.09.18.09.01.01;"";"";""
972;MRN complex (MRE11-RAD50-NBS1 complex); RAD50-MRE11-p95 complex | MRE11 complex;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0226- ion exchange chromatography | MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;9590181;01.03.16.03,10.01.05.01,10.03.01.03,32.01.09,70.10;"The implication of hMre11/hRad50/p95 protein complex in NBS reveals a direct molecular link between DSB repair and cell cycle checkpoint functions. ";"Rad50-MRE11-p95 protein complex is involved in Nijmegen breakage syndrome.";""
973;Sec61alpha-CollagenIV-Hsp47 complex;;Mouse;P02463,P61620,P19324;12826,53421,12406;MI:0019- coimmunoprecipitation;12532224;14.04,14.10,70.07;"Sec61a may form complexes with Hsp47 and other ER proteins during the constitutive synthesis of collagen IV by F9 cells after retinoic acid treatment.";"";""
974;EED-EZH2 complex; ESC-E(Z) complex | H3-specific methyltransferase complex;Human;Q6ZN18,O75530,Q15910,Q09028,Q15022;121536,8726,2146,5928,23512;MI:0091- chromatography technologies | MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;12351676;10.01.09.05,11.02.03.04.07,14.07.09,42.10.03,70.10;"The results support a model in which ESC-E(Z)-mediated H3-K27 methylation serves as a signal for the recruitment of the PRC1 complex by facilitating PC binding.";"";""
975;Ocrl-Cdc42 complex;;Mouse;P60766,Q6NVF0;12540,320634;MI:0096- pull down;12915445;14.04,70.08;"Cdc42 associates significantly with OCRL1 RhoGAP in GST pulldown and membrane translocation assays, no interaction between endogenous OCRL1 and Cdc42 could be detected in coimmunoprecipitation experiments (PMID:12915445).";"";""
976;SNARE complex (Stx1a, Snap25, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0019- coimmunoprecipitation;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
977;SNARE complex (Stx2, Snap25, Vamp2);;Rat;P60881,P50279,P63045;25012,25130,24803;MI:0019- coimmunoprecipitation;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
978;SNARE complex (Stx3, Snap25, Vamp2);;Rat;P60881,Q08849,P63045;25012,81802,24803;MI:0019- coimmunoprecipitation;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
979;SNARE complex (Stx4, Snap25, Vamp2);;Rat;P60881,Q08850,P63045;25012,81803,24803;MI:0019- coimmunoprecipitation;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
980;SNARE complex (Stx4, Snap25, Vamp2, Syt1);;Rat;P60881,Q08850,P21707,P63045;25012,81803,25716,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
981;SNARE complex (Stx3, Snap25, Vamp2, Syt1);;Rat;P60881,Q08849,P21707,P63045;25012,81802,25716,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
982;SNARE complex (Stx2, Snap25, Vamp2, Syt1);;Rat;P60881,P50279,P21707,P63045;25012,25130,25716,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
983;SNARE complex (Stx1a, Snap25, Vamp2, Syt1);;Rat;P60881,P32851,P21707,P63045;25012,116470,25716,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
984;SNARE complex (Stx1a, Snap25, Vamp2, Cplx1);;Rat;P63041,P60881,P32851,P63045;64832,25012,116470,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
985;SNARE complex (Stx1a, Snap25, Vamp2, Cplx2);;Rat;P84087,P60881,P32851,P63045;116657,25012,116470,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
986;SNARE complex (Stx2, Snap25, Vamp2, Cplx1);;Rat;P63041,P60881,P50279,P63045;64832,25012,25130,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
987;SNARE complex (Stx2, Snap25, Vamp2, Cplx2);;Rat;P84087,P60881,P50279,P63045;116657,25012,25130,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
988;SNARE complex (Stx3, Snap25, Vamp2, Cplx2);;Rat;P84087,P60881,Q08849,P63045;116657,25012,81802,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
989;SNARE complex (Stx3, Snap25, Vamp2, Cplx1);;Rat;P63041,P60881,Q08849,P63045;64832,25012,81802,24803;MI:0047- far western blotting;15975093;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
990;Agap11-AP3 complex;;Mouse;Q8BXK8,Q9Z1T1,Q9JKC8,Q8R2R9,Q8BSZ2;347722,11774,55946,64933,11778;MI:0019- coimmunoprecipitation;12967569;20.09.07,70.22;"";"";""
991;Tubulin polyglutamylase complex;;Mouse;Q66JT5,Q99MS8,Q91YK0,Q9CQM0,Q91V51;66648,110012,102747,66257,319953;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;15890843;45.03.15,75.03.15;"";"";""
992;Kif5a-Dtnb-Dtna complex;;Rat;Q9D2N4,P84060,Q6QLM7;13527,362715,314906;MI:0019- coimmunoprecipitation;14600269;14.04,34.05,75.03.17;"The authors suggest that the interaction between dystrobrevins and Kif5a/b might be important for the transport of components of the DPC to the neuronal membrane.";"";"Since Dtna from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
993;Kif5b-Dtnb complex;;Mammalia;O70585,Q61768;13528,16573;MI:0096- pull down;14600269;14.04,34.05,75.03.17;"The authors suggest that the interaction between dystrobrevins and Kif5a/b might be important for the transport of components of the DPC to the neuronal membrane.";"";""
994;GAA1-GPI8-PIGT-PIG-PIGS complex;;Human;O43292,Q92643,Q96S52,Q969N2,Q9H490;8733,10026,94005,51604,128869;MI:0019- coimmunoprecipitation;14660601;01.06.02.01,70.02;"";"";""
995;Polycomb repressive complex 3 (PRC3);;Human;O75530,Q15910,Q09028,Q16576,Q15022;8726,2146,5928,5931,23512;MI:0091- chromatography technologies;15099518;10.01.09.05,11.02.03.04.07,14.07.09,42.10.03,70.10;"PRC3 associates with the two shortest isoforms of EED. PRC3 methylates nucleosomal H3-lysine 27, PRC2 methylates nucleosomal H1-lysine 26.";"";""
996;Polycomb repressive complex 2 (PRC2);;Human;O75530,Q15910,Q09028,Q16576,Q15022;8726,2146,5928,5931,23512;MI:0091- chromatography technologies;15099518;10.01.09.05,11.02.03.04.07,14.07.09,42.10.03,70.10;"PRC2 associates with all three EED isoforms, with the largest form of EED in highest abundance. PRC3 preferentially methylates nucleosomal H3-lysine 27, PRC2 preferentially methylates nucleosomal H1-lysine 26.";"";""
997;KIN17-PCNA-RPA70 complex;;Human;O60870,P12004,P27694;22944,5111,6117;MI:0040- electron microscopy | MI:0091- chromatography technologies;15831485;10.01.03,10.03.01.03,16.03.01,70.10.06;"This complex associates with DNA polymerase alpha.";"";""
998;SNARE complex (Snap25, Stx1a, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0047- far western blotting;15528447;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. Syntaxin, synaptosome-associated protein of 25kD (SNAP25), and vesicle-associated membrane protein/synaptobrevin are collectively called SNAP receptor (SNARE) proteins. They catalyze neuronal exocytosis by forming a "core complex".";"";""
999;p23 protein complex;;Human;P22626,Q86W51,Q15185;3181,10016,10728;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;14675759;40.10.02.04,16.01;"";"The expression of p23 is increased  after rat focal cerebral ischemia. DHNRPA2B1 is clinical marker of early lung cancer detection (PMID:10632338).";""
1000;TorsinA-TorsinB complex;;Human;O14656,O14657;1861,27348;MI:0019- coimmunoprecipitation;15147511;34.11.13.07,77.03.01.01.01;"";"";""
1001;DNA synthesome complex; MRC complex (Multiprotein DNA Replication Complex) | 17S DNA polymerase multiprotein complex | multiprotein form of DNA polymerase;Mouse;P37913,P17918,P33609,P33611,P52431,O35654,Q9EQ28,Q9CWP8,P20664,P33610,Q04750,(Q01320,Q64511);16881,18538,18968,18969,18971,18972,67967,69745,19075,19076,21969,(21973,21974);MI:0226- ion exchange chromatography;8126085;10.01.03,70.10;"This complex associates also with a not further characterized DNA helicase.";"";""
1002;Cask-Dlg1 complex;;Mouse;O70589,Q811D0;12361,13383;MI:0019- coimmunoprecipitation;15266631;36.25.03.03.01;"CASK and Dlg may act as a scaffold for organizing receptors and channels at the postsynaptic membrane of the neuromuscular junction (PMID:15266631).";"";""
1003;RC complex (Replication competent complex);;Human;P20248,P24941,P09884,Q14181,P35251,P35250,P40938,P35249,P40937;890,1017,5422,23649,5981,5982,5983,5984,5985;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients;12006500;10.01.03,10.03.01.03,16.03.01,70.10.03;"RC complex might be regulated by specific cyclin/Cdk complexes (PMID:12006500).";"";""
1004;RC complex during S-phase of cell cycle;;Human;P20248,P24941,P18858,P09874,P09884,P28340,Q07864,P35251,P35250,P27694,P15927,P35244,P11387;890,1017,3978,142,5422,5424,5426,5981,5982,6117,6118,6119,7150;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;12006500;10.01.03,10.03.01.03,16.03.01,70.10.03;"CDK2 associates with the RC complex only during the S-phase of the cell cycle, but disappeares in the G2-phase.";"";""
1005;RC complex during G2/M-phase of cell cycle;;Human;P20248,P14635,P06493,P09874,P09884,P28340,Q07864,P35251,P35250,P27694,P15927,P35244,P11387;890,891,983,142,5422,5424,5426,5981,5982,6117,6118,6119,7150;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;12006500;10.01.03,10.03.01.03,16.03.01,70.10.03;"CDK1 and cyclin B1 associate with RC complex only during G2/M-phase of cell cycle. DNA ligase I is not found in the RC complex during G2/M-phase.";"";""
1006;Caveolin complex;;Rat;P60711,P63259,P41350,P20070,Q9Z2S9,Q2IBC5;81822,287876,25404,25035,83764,363425;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;15293782;34.11.05,34.11.13.07,70.02,77.03.03.02,77.03.09.01;"";"";""
1007;CAK core complex (Cdk-activating kinase core complex);;Human;P51946,P50613;902,1022;MI:0004- affinity chromatography technologies;7533895;01.04,10.03,11.02.03,18.01.01,18.02.01.01.05,18.02.09,70.10;"CAK complex phosphorylates the carboxy-terminal domain of the largest subunit of RNA polymerase II.";"";""
1008;CAK complex (Cdk-activating kinase complex);;Human;P51946,P50613,P51948;902,1022,4331;MI:0019- coimmunoprecipitation;8521818;10.03,11.02.03,18.01.01,18.02.01.01.05,18.02.09,70.10;"MAT1 is required for stabilization and assembly of the active CAK complex.";"";""
1009;TFIIH transcription factor complex;;Human;P51946,P50613,P18074,P19447,P32780,Q13888,Q13889,Q92759,Q6ZYL4,P51948;902,1022,2068,2071,2965,2966,2967,2968,404672,4331;MI:0006- anti bait coimmunoprecipitation;15220921;01.04,10.01.05.01,10.03,11.02.03.01,11.02.03.04,18.01.01,18.02.01,70.10;"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair. The GTF2H5 gene product has a role in regulating the level of TFIIH.";"";""
1010;CAK complex (Cdk-activating kinase complex);;Human;P51946,P50613,P51948;902,1022,4331;MI:0091- chromatography technologies | MI:0071- molecular sieving;8692842;01.04,10.03,11.02.03,18.01.01,18.02.01.01.05,18.02.09,70.10;"MAT1 is required for stabilization and assembly of the active CAK complex.";"";""
1011;SNARE complex (Stx1a,1b,7,13, Rtn1, Vamp2);;Rat;Q64548,O70319,P32851,P61265,O70257,P63045;116644,65033,116470,24923,60466,24803;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;15086514;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. RTN1-C does apparently not bind to formed SNARE complexes, it might interfere with their formation.";"";""
1012;SNARE complex (Snap25, Stx1a, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0114- x-ray crystallography;9759724;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1013;SNARE complex (Snap25, Stx1a, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0114- x-ray crystallography;11533035;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1014;Pcdhga1-Pcdha4 complex;;Mouse;O88689,Q91XZ0;12936,93709;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1015;Pcdhga1-Pcdhgb2 complex;;Mouse;O88689,Q91XX7;12936,93700;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1016;Pcdhga1-Pcdhga3 complex;;Mouse;O88689,Q91XY5;12936,93711;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1017;Pcdhga1-Pcdhgb4 complex;;Mouse;O88689,Q91XX6;12936,93701;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1018;Pcdha7-Pcdhgb4 complex;;Mouse;Q91Y13,Q91XX6;12939,93701;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1019;Pcdha7-Pcdhga3 complex;;Mouse;Q91Y13,Q91XY5;12939,93711;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1020;Pcdha7-Pcdhgb2 complex;;Mouse;Q91Y13,Q91XX7;12939,93700;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1021;Pcdha7-Pcdhga1 complex;;Mouse;Q91Y13,Q91XZ0;12939,93709;MI:0019- coimmunoprecipitation;15347688;14.04,18.01.03,34.07,73.03.13,77.03.01.01.01;"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.";"";""
1022;Fgr-Pyk2-p190RhoGap complex;;Mouse;P14234,Q91YM2,Q9QVP9;14191,232906,19229;MI:0019- coimmunoprecipitation;15561106;34.05.01;"";"";""
1023;Tiam1-Par-3-aPKC-zeta complex;;Mouse;Q99NH2,Q02956,Q60610;93742,18762,21844;MI:0019- coimmunoprecipitation;16186252;30.01.05.05.01,40.01.03,41.05.19,42.06,70.06;"Tiam1 interacts with Par3 and aPKCzeta, which are two components of the conserved Par3-Par6-aPKC polarity complex, and triggers biogenesis of the TJ through the activation of Rac and aPKCzeta, which is independent of Cdc42.";"";""
1024;Tiam1-IRSp53 complex;;Rat;Q6GMN2,Q60610;117542,21844;MI:0019- coimmunoprecipitation;15899863;14.04,30.01.05.05.01,42.04.03,70.04.03;"Further experiments done in 293T cells and in NIH-3T3 cells. Stimulation of Tiam1 interaction with IRSp53, either through forced Tiam1 overexpression or Ras activation by growth factor, enhances IRSp53 interaction with WAVE2 and Rac and leads to its redistribution, recruiting IRSp53 effects toward a Rac phenotype (ruffles).";"";"Since Tiam1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
1025;Calreticulin-Tnfr1-Tradd complex;;Rabbit;P15253,P25118,Q3U0V2;100009050,21937,71609;MI:0019- coimmunoprecipitation;15284227;40.10.02.04;"";"";"Since Tradd, Tnrf1 from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
1026;Tiam1-spinophilin complex;;Rat;O35274,Q60610;84686,21844;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;12531897;14.10,18.02.01.01.05,30.01.05.05.01,70.02;"Spinophilin binding promotes the plasma membrane localization of Tiam1 and enhances the ability of Tiam1 to activate p70 S6 kinase.";"";"Since Tiam1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
1027;SNARE complex (Stx4, Vamp7, Snap23, Syt7);;Rat;O70377,Q08850,Q62747,Q9JHW5;64630,81803,59267,85491;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;14993220;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1028;HNF4A-SUB1 complex;;Human;P41235,P53999;3172,10923;MI:0024- confirmational text mining;17317687;11.02.03.04.01;"The hepatocellular inflammatory-redox (IR) state enhances PC4-HNF4 binding to upregulate transcription of target hepatocyte genes, such as iNOS.";"";""
1029;TFIIH transcription factor complex;;Human;P51946,P50613,P18074,P19447,P32780,Q13888,Q13889,Q92759,Q6ZYL4,P51948;902,1022,2068,2071,2965,2966,2967,2968,404672,4331;MI:0091- chromatography technologies | MI:0071- molecular sieving;8692842;01.04,10.01.05.01,10.03,11.02.03.01,11.02.03.04,18.01.01,18.02.09,70.10;"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair.";"";""
1030;CAK-ERCC2 complex;;Human;P51946,P50613,P18074,P51948;902,1022,2068,4331;MI:0091- chromatography technologies | MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;8692842;01.04,10.03,11.02.03,18.01.01,18.02.01.01.05,18.02.09,70.10;"CAK-ERCC2 can efficiently associate with core-TFIIH to reconstitute holo-TFIIH transcription activity.";"";""
1031;ORC complex (origin recognition complex);;Human;Q13415,Q13416,Q9UBD5,O43929,O43913,Q9Y5N6;4998,4999,23595,5000,5001,23594;MI:0006- anti bait coimmunoprecipitation;11323433;10.01.03.03,16.19.03,70.10.03;"HsOrc2, HsOrc3, and HsOrc4 form a core upon which the ordered assembly of HsOrc5 and HsOrc1 takes place. HsOrc6 appears to be the most weakly bound subunit in the complex.";"";""
1032;ORC 2-4 complex (origin recognition 2-4 complex);;Human;Q13416,Q9UBD5,O43929;4999,23595,5000;MI:0006- anti bait coimmunoprecipitation;11323433;10.01.03.03,16.19.03,70.10.03;"HsOrc2, HsOrc3, and HsOrc4 form a core upon which the ordered assembly of HsOrc5 and HsOrc1 takes place.";"";""
1033;ORC complex (origin recognition complex);;Human;Q13415,Q13416,Q9UBD5,O43929,O43913,Q9Y5N6;4998,4999,23595,5000,5001,23594;MI:0006- anti bait coimmunoprecipitation;10945994;10.01.03.03,16.19.03,70.10.03;"Only a small fraction of human ORC1 and ORC6 is associated with a subcomplex of ORC2, 3, 4, and 5.";"";""
1034;ORC 2-5 complex (origin recognition 2-5 complex);;Human;Q13416,Q9UBD5,O43929,O43913;4999,23595,5000,5001;MI:0006- anti bait coimmunoprecipitation;10945994;10.01.03.03,16.19.03,70.10.03;"Only a small fraction of human ORC1 and ORC6 is likely to be associated with a subcomplex of ORC2, 3, 4, and 5.";"";""
1035;OAP-1-OSP/claudin-11-ITGB1 complex;;Mouse;Q60771,P09055,Q9QY33;18417,16412,56434;MI:0006- anti bait coimmunoprecipitation | MI:0663- confocal microscopy;11309411;34.05.01,43.03.13,45.03.17,47.03.01.01,70.02,73.03.13,75.03.17,77.03.01.01;"Surface biotinylation and immunoelectron microscopy demonstrated the presence of OSP/claudin-11 and OAP-1 on the oligodendrocyte membrane surface, but it is still not clear whether OSP/claudin-11 complexes with OAP-1 and ß1 integrin at TJs.";"";""
1036;TFIIH transcription factor complex;;Human;P51946,P50613,P18074,P19447,P32780,Q13888,Q13889,Q92759,P51948;902,1022,2068,2071,2965,2966,2967,2968,4331;MI:0091- chromatography technologies;9118947;01.04,10.01.05.01,10.03,11.02.03.01,11.02.03.04,18.01.01,18.02.01,70.10;"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair.";"";""
1037;TFIIH transcription factor core complex;;Human;P19447,P32780,Q13888,Q13889,Q92759;2071,2965,2966,2967,2968;MI:0006- anti bait coimmunoprecipitation;9118947;01.04,10.01.05.01,10.03,11.02.03.01,11.02.03.04,18.01.01,18.02.01,70.10;"";"";""
1038;ORC 1-5 complex (origin recognition 1-5 complex);;Human;Q13415,Q13416,Q9UBD5,O43929,O43913;4998,4999,23595,5000,5001;MI:0029- cosedimentation through density gradients | MI:0071- molecular sieving;15618391;10.01.03.03,16.19.03,70.10.03;"ATP-binding motifs of Orc1, Orc4, Orc5 are all essential for the replication activity of the ORC complex.";"";""
1039;PCNA-PAF complex;;Human;Q15004,P12004;9768,5111;MI:0019- coimmunoprecipitation;16288740;10.01.05.01,10.03,40.10.02,70.10,70.16;"";"";""
1040;p33ING1b-PCNA complex;;Human;Q9UK53,Q15004;3621,9768;MI:0019- coimmunoprecipitation;16288740;10.01.05.01,10.03,40.10.02,70.10,70.16;"p15(PAF) forms part of a larger protein complex potentially involved in the regulation of DNA repair, apoptosis and cell cycle progression.";"";""
1041;Alpha-dystrobrevin-ZO-1-actin complex;;Mammalia;Q9Y4J8,Q07157,(P60709,P63261);1837,7082,(60,71);MI:0006- anti bait coimmunoprecipitation;15834686;42.06,70.06,75.03.09;"The TJ- protein ZO-1 and actin were demonstrated in immunoprecipitates of alpha-DB from MDCK I and HT 29 cell lines. These findings suggest that alpha-DB is specifically associated with the reorganizing TJ.";"";""
1042;SRA-SRC-1 ribonucleoprotein complex;;Human;Q15788,Q9HD15;8648,10011;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;10199399;11.02.03.04.01,30.01.11,70.10;"The authors conclude that SRA exists in a ribonucleoprotein complex containing SRC-1 and that this complex is recruited by a steroid receptor.";"";""
1043;Car-Lnx2 complex;;Mouse;P97792,Q91XL2;13052,140887;MI:0019- coimmunoprecipitation | MI:0018- two hybrid | MI:0004- affinity chromatography technologies;15979067;16.01,34.07.01;"";"";""
1044;Car-Jam3 complex;;Mouse;P97792,Q9D8B7;13052,83964;MI:0019- coimmunoprecipitation;16410001;16.01,43.03.02;"";"";""
1045;Snurportin-CRM1-RanGTP complex;;Human;P62826,O95149,O14980;5901,10073,7514;MI:0096- pull down;10209022;20.01.10,20.01.21,20.09.01,70.03,70.10;"The complex is exported from the nucleus to the cytoplasm where  RanGTP is removed from CRM1 through the action of RanBP1 and RanGAP.";"";""
1046;Lnx1-Jam4 complex;;Mouse;Q7TSN7,O70263;72058,16924;MI:0019- coimmunoprecipitation;16832352;16.01,20.09.18.09.01;"Ligand-of-Numb protein X1 facilitates endocytosis of JAM4 and is involved in  transforming growth factor beta-induced redistribution of JAM4 in mammary  epithelial cells.";"";""
1047;Lnx1-Jam4-Numb complex;;Mammalia;Q7TSN7,O70263,Q9QZS3;72058,16924,18222;MI:0096- pull down;16832352;16.01,20.09.18.09.01;"Numb is necessary for the LNX1-mediated endocytosis of JAM4.";"";""
1048;Hnf4-Pc4 complex;;Mouse;P49698,P11031;15378,20024;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;16003322;11.02.03.04.03;"Redox-mediated upregulation of hepatocyte iNOS transcription requires an HNF-4alpha-PC4 transcriptional complex.";"";""
1049;SNARE complex (Snap25, Stx1a, Vamp2);;Rat;P60881,P32851,P63045;25012,116470,24803;MI:0004- affinity chromatography technologies;9671503;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. A minimal core of the synaptic SNARE complex sufficient for reversible assembly, one of the key steps in mediating exocytosis of synaptic vesicles.";"";""
1050;Vdr-Med4 complex;;Mouse;Q9CQA5,P48281;67381,22337;MI:0019- coimmunoprecipitation;16003322;11.02.03.04,16.01;"";"";""
1051;Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, RBX1);;Human;Q13616,P62877,P63208,Q13309;8454,9978,6500,6502;MI:0029- cosedimentation through density gradients | MI:0069- mass spectrometry studies of complexes;10230406;14.07.05,14.13.01.01,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha.";"";""
1052;Ubiquitin E3 ligase (FBXW11, SKP1A, CUL1, RBX1);SCF(HOS)-ROC1  complex;Human;Q13616,Q9UKB1,P62877,P63208;8454,23291,9978,6500;MI:0004- affinity chromatography technologies;10230406;14.07.05,14.13.01.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. This complex catalyzes the phosphorylation-dependent ubiquitination of NF-kappa-B inhibitor alpha.";"";""
1054;ESR1-RELA-BCL3-NCOA3 complex;;Human;P20749,P03372,Q9Y6Q9,Q04206;602,2099,8202,5970;MI:0019- coimmunoprecipitation;16331275;11.02.03.04,30.01.11;"";"";""
1055;ZNF198-PML complex;;Human;P29590,Q9UBW7;5371,7750;MI:0019- coimmunoprecipitation;17027752;11.02.03.04,70.10;"The authors show by coimmunoprecipitation that PML and sumoylated ZNF198 are in a protein complex in the cell. ";"ZMYM2 is involved in myeloproliferative disorder.";""
1056;ZNF198-SUMO1 complex;;Human;P63165,Q9UBW7;7341,7750;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;17027752;11.02.03.04,70.10;"The results show that ZNF198 is covalently modified by SUMO-1.";"ZMYM2 is involved in myeloproliferative disorder.";""
1057;DIPA-MCRS1 complex;;Human;Q15834,Q96EZ8;11007,10445;MI:0019- coimmunoprecipitation;17014843;11.02.03.04.03,70.10.03;"";"";""
1058;SNX complex (SNX1, SNX6);;Human;Q13596,Q9UNH7;6642,58533;MI:0019- coimmunoprecipitation;17148574;20.09.07.07,70.22;"SNX1 and SNX6 exist in a stable, endosomally associated complex that is required for retromer-mediated retrieval of the cation-independent mannose-6-phosphate receptor.";"";""
1059;Retromer complex (SNX1, SNX2, VPS35, VPS29, VPS26A);;Human;Q13596,O60749,O75436,Q9UBQ0,Q96QK1;6642,6643,9559,51699,55737;MI:0018- two hybrid | MI:0047- far western blotting;11102511;20.09.07.07;"";"";""
1060;Retromer complex (SNX1, SNX2, VPS35, VPS29, VPS26B);;Human;Q13596,O60749,Q4G0F5,Q9UBQ0,Q96QK1;6642,6643,112936,51699,55737;MI:0018- two hybrid | MI:0047- far western blotting;11102511;20.09.07.07;"";"";""
1062;BAR-BCL2-CASP8 complex;;Human;P10415,Q9NZS9,Q14790;596,51283,841;MI:0019- coimmunoprecipitation;10716992;40.10.02.02.04;"BAR can bridge procaspase-8 and Bcl-2 into a protein complex. The BAR protein is anchored in intracellular membranes where Bcl-2 resides. BAR therefore may represent a scaffold protein capable of bridging two major apoptosis pathways (intrinsic and extrinsic).";"";""
1063;GRASP-GRP1 complex;;Human;Q7Z6J2,O43739;160622,9265;MI:0019- coimmunoprecipitation;10828067;30.01.05.05.01,70.02;"The authors propose that GRASP may aid in the localization of GRP1 to discrete signaling networks and facilitate stimulation of ARF-mediated events at the plasma membrane.";"";""
1064;IFP35-NMI complex;;Human;P80217,Q13287;3430,9111;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;10950963;14.13.01.01,18.01.07;"The authors show that IFP 35 is degraded in a proteasome-mediated process, and that a novel function of Nmi is to prevent IFP 35 degradation.";"";""
1066;mPar6c-Mlgl-aPKCz complex;;Mouse;Q80Y17,Q9Z101,Q02956;16897,56513,18762;MI:0006- anti bait coimmunoprecipitation;12629547;40.01.03,41.05.19,45.03.09;"The data suggest that the phosphorylation of Mlgl by aPKC is important for appropriate cell polarization in the wounding assay. The authors propose that an interaction between Mlgl, mPar-6C and aPKC, and the consequent phosphorylation of Mlgl, may regulate Mlgl in a polarized fashion such that it can exert localized effects on protein trafficking and secretion.";"";""
1067;CD8A-LCK complex;;Human;P01732,P06239;925,3932;MI:0019- coimmunoprecipitation;11034334;30.05.01.12,36.25.16,70.02.01;"The authors found that newly synthesized p56lck binds rapidly to CD8-alpha throughout the exocytic pathway and about 50% of complexed p56lck reaches the cell surface.";"";""
1068;12S U11 snRNP;;Human;Q9BV90,Q6IEG0,Q8N8D1,Q9H875,Q16629,P14678,P62314,P62316,P62318,P62304,P62306,P62308,Q96GM8,Q16560,P67809;79622,154007,10081,79706,6432,6628,6632,6633,6634,6635,6636,6637,114034,11066,4904;MI:0029- cosedimentation through density gradients | MI:0069- mass spectrometry studies of complexes;15146077;11.04.03,70.10;"U12-type spliceosomes excise U12-type introns, which comprise less than 1% of all human introns.";"";""
1069;FIF-FGR2 complex;;Human;Q9BZZ5,P09038;8539,2247;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;11075807;16.01;"";"";""
1070;SNX complex (SNX1a, SNX2, SNX4);;Human;Q13596,O60749,O95219;6642,6643,8723;MI:0019- coimmunoprecipitation;9819414;20.01.10;"";"";""
1071;PKD2-FPC complex;;Human;Q13563,Q8TCZ9;5311,5314;MI:0019- coimmunoprecipitation | MI:0096- pull down;17008358;18.02.10,20.01.01.01,20.03.01.01,34.01.01.01,75.03.09,75.03.12.03,77.03.07.01;"The study shows that fibrocystin is another partner of PC2, which functionally up-regulates its channel function through KIF3B. Interestingly, although KIF3B directly binds PC2, it has no significant effect on PC2 channel function, indicating that it primarily serves as a linker protein.";"PKD2-FPC complex is involved in polycystic kidney disease (PKD).";""
1072;SNX complex (SNX2), oligomeric;;Human;O60749;6643;MI:0019- coimmunoprecipitation;9819414;20.01.10;"";"";"SNX2 is able to oligomerize with itself. The exact number of components is not mentioned in paper."
1073;Pkd2-Fpc complex;;Mouse;O35245,Q8CIS7;18764,241035;MI:0019- coimmunoprecipitation | MI:0096- pull down;17008358;18.02.10,20.01.01.01,20.03.01.01,34.01.01.01,75.03.09;"The study shows that fibrocystin is another partner of PC2, which functionally up-regulates its channel function through KIF3B. Interestingly, although KIF3B directly binds PC2, it has no significant effect on PC2 channel function, indicating that it primarily serves as a linker protein.";"PKD2-FPC complex is involved in polycystic kidney disease (PKD).";""
1074;Pkd2-Fpc-Kif3b complex;;Mouse;Q61771,O35245,Q8CIS7;16569,18764,241035;MI:0047- far western blotting | MI:0096- pull down | MI:0019- coimmunoprecipitation;17008358;18.02.10,20.01.01.01,20.03.01.01,34.01.01.01,75.03.09,77.03.07.01;"Using a combination of in vitro and in vivo approaches, including yeast two-hybrid, GST pull-down and Far WB, the authors have demonstrated that the kinesin-2 motor subunit KIF3B acts as a linker protein, which enables the formation of a triplex, presumably in the form of PC2-KIF3B-FPC. Thus, KIF3B represents the first molecular linker between ADPKD and ARPKD proteins, suggesting that the protein complex PC2-KIF3B-FPC is part of a common molecular pathway implicated in renal cystic diseases. Using the lipid bilayer electrophysiology assay, it was demonstrated that FPC is capable of increasing PC2 channel function in the presence, but not in the absence of KIF3B.";"Pkd2-Fpc-Kif3b complex is involved in polycystic kidney disease (PKD).";""
1076;Pkhd1-Pkd2 complex;;Mouse;O35245,Q8CIS7;18764,241035;MI:0019- coimmunoprecipitation;17283055;20.01.01.01,20.03.01.01,34.01.01.01,34.11.05,70.02,77.03.07.01;"Coimmunoprecipitation of FPC and PC2 done in MDCK cells and mouse kidney tissues. Expression of FPC at the basolateral membrane both in the kidney tubules and in cultured cells suggests a role for FPC in cell-cell and cell-matrix interactions, where it may function as an adhesive molecule in concert with other junction molecules, such as the cadherin family members.";"Pkhd1-Pkd2 complex  is involved in autosomal recessive polycystic kidney disease (PKD). ";""
1077;Pkd2-Fpc-Kif3a complex;;Dog;P28741,O35245,Q8CIS7;16568,18764,241035;MI:0006- anti bait coimmunoprecipitation;17283055;20.01.01.01,20.03.01.01,34.01.01.01,34.11.05,70.02;"The results show that Kif3a but not Kif3b was coimmunoprecipitated by both FPC and PC2 antibodies. This indicates that Kif3a is likely to be one of the molecular candidates mediating the interaction between FPC and PC2.  Disruption of either FPC or the PC1/PC2 complex at the primary cilium results in defects in mechanosensation of fluid flow.";"Pkd2-Fpc complex is involved in autosomal recessive polycystic kidney disease (PKD).";"Since Pkd2, Kif3a and Pkhd1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
1078;MSH2-MSH6 complex;;Human;P43246,P52701;4436,2956;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;9428522;10.01.05.01,16.03.01,16.19,70.10;"The MSH2-MSH6 complex binds to mismatched nucleotides only in the ADP-bound form.";"";""
1079;P-TEFb.1 complex; transcription elongation factor b.1 complex;Human;O60563,P50750;904,1025;MI:0007- anti tag coimmunoprecipitation;9499409;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"Cyclin T activates CDK9 in the P-TEFb complex. P-TEFb works as a protein kinase that phosphorylates the C-terminal domain of the RNAPII largest subunit.";"";""
1080;P-TEFb.2 complex; transcription elongation factor b.2 complex;Human;O60583,P50750;905,1025;MI:0007- anti tag coimmunoprecipitation;9499409;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"Cyclin T activates CDK9 in the P-TEFb complex. P-TEFb works as a protein kinase that phosphorylates the C-terminal domain of the RNAPII largest subunit.";"";""
1081;MRN complex (MRE11-RAD50-NBN complex);;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0019- coimmunoprecipitation;15039997;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"After irradiation, the MRN complex rapidly migrates to sites of double strand breaks, forming foci which remain until DSB repair is complete. Mre11 and Rad50 play direct roles in DSB repair, while Nbs1 appears to be involved in damage signaling. Heat shock, alone or in combination with ionizing radiation, induces a reversible translocation of each of these proteins from the nucleus to the cytoplasm. ";"";""
1082;P-TEFb.1 complex; transcription elongation factor b.1 complex;Human;O60563,P50750;904,1025;MI:0018- two hybrid | MI:0071- molecular sieving;10574912;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"Cyclin T activates CDK9 in the P-TEFb complex. P-TEFb works as a protein kinase that phosphorylates the C-terminal domain of the RNAPII largest subunit.";"";""
1083;P-TEFb.4 complex; transcription elongation factor b.4 complex;Human;O75909,P50750;8812,1025;MI:0018- two hybrid | MI:0071- molecular sieving;10574912;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"Cyclin K functions as regulatory subunit of CDK9.";"";""
1084;Tiam2-PAR-3-aPKC-PAR-6-Rac1-GTP complex;;Rat;Q9Z340,Q6B4M5,P97701,Q6RUV5,Q6ZPF3;81918,307799,84006,363875,24001;MI:0096- pull down;15723051;30.01.05.05.01,40.01.03,41.05.13,41.05.19,43.03.13,73.03.13;"";"";"Since Tiam2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
1085;DNA repair complex NEIL2-PNK-Pol(beta)-LigIII(alpha)-XRCC1;;Human;P49916,Q969S2,O00764,P06746,P18887;3980,252969,8566,5423,7515;MI:0006- anti bait coimmunoprecipitation;16982218;10.01.05.01,16.03.01,70.10;"";"";""
1086;DNA repair complex NEIL1-PNK-Pol(beta)-LigIII(alpha)-XRCC1;;Human;P49916,Q96FI4,O00764,P06746,P18887;3980,79661,8566,5423,7515;MI:0006- anti bait coimmunoprecipitation;15260972;10.01.05.01,16.03.01,70.10;"";"";""
1087;BIRC5-AURKB-INCENP-EVI5 complex;;Human;Q96GD4,O15392,O60447,Q9NQS7;9212,332,7813,3619;MI:0019- coimmunoprecipitation | MI:0096- pull down;16764853;10.03.03;"";"";""
1088;PRNP-ApolopoproteinE3 complex;;Human;Q13791,P04156;348,5621;MI:0019- coimmunoprecipitation | MI:0096- pull down;16764853;16.01;"";"";""
1089;VAM1-VELI1 complex;;Human;O14910,Q9NZW5;8825,51678;MI:0096- pull down;11311936;16.01,18.01.07,75.03.09,75.03.17;"VAM-1 may function by promoting the assembly of a Veli-1 containing protein complex in neuronal as well as epithelial cells (PMID:11311936).";"";""
1090;APLG1-Rababtin5 complex;;Human;O43747,(Q15276,Q9H5N1);164,(9135,79874);MI:0019- coimmunoprecipitation | MI:0018- two hybrid | MI:0096- pull down;11872161;20.09.07;"The gamma1-adaptin-Rabaptin-5 complex may play a role in membrane trafficking between the TGN and endosomes.";"";""
1091;SNX complex (SNX1a, SNX2, SNX4, LEPR); Leptin receptor complex;Human;P48357,Q13596,O60749,O95219;3953,6642,6643,8723;MI:0019- coimmunoprecipitation;9819414;20.01.10,20.09.18.09.01.01,30.05.01;"";"";""
1092;PCNA-KU antigen complex; PCNA-Ku70-Ku80 complex;Human;P12004,P13010,P12956;5111,7520,2547;MI:0006- anti bait coimmunoprecipitation;11239001;10.01.05.01,16.03.01,16.19.03,32.01.09;"Interaction of PCNA with Ku70 and Ku80 heterodimer increases after DNA damage.";"";""
1093;SNX complex (SNX1a, SNX2, SNX4, INSR); Insulin receptor complex;Human;P06213,Q13596,O60749,O95219;3643,6642,6643,8723;MI:0019- coimmunoprecipitation;9819414;20.01.10,20.09.18.09.01.01,30.05.01.12.05;"";"";""
1094;Frataxin complex;;Mammalia;Q9Y4W6,O75964,Q16595,P38646,P10809,Q9HD34,P31040;10939,10632,2395,3313,3329,57128,6389;MI:0019- coimmunoprecipitation;17331979;16.01,70.16;"";"";""
1095;SNX complex (SNX1a, SNX2, SNX4, EGFR); EGF receptor complex;Human;P00533,Q13596,O60749,O95219;1956,6642,6643,8723;MI:0019- coimmunoprecipitation;9819414;20.01.10,20.09.18.09.01.01,30.05.01.12.01;"";"";""
1096;SNX complex (SNX1,1a,2,4, PDGF receptor); PDGF receptor complex;Human;P16234,Q13596,O60749,O95219;5156,6642,6643,8723;MI:0019- coimmunoprecipitation;9819414;20.01.10,20.09.18.09.01.01,30.05.01;"";"";"At the time of annotation, the additional member SNX1a of the protein complex was not found in the UniProt database."
1097;eIF3 complex (EIF3S6, EIF3S5, EIF3S4, EIF3S3, EIF3S6IP, EIF3S2, EIF3S9, EIF3S12,  EIF3S10, EIF3S8,  EIF3S1, EIF3S7, PCID1);;Human;Q14152,P55884,Q99613,O15371,P60228,Q9Y262,O00303,O75821,O15372,Q13347,O75822,Q9UBQ5,Q7L2H7;8661,8662,8663,8664,3646,51386,8665,8666,8667,8668,8669,27335,10480;MI:0069- mass spectrometry studies of complexes;17322308;12.04.01;"Four eIF3 subunits (h, i, k, and m) were found to dissociate preferentially and are therefore likely to be on the periphery of the complex (PMID:17322308).";"";"Each of 13 subunits of this complex present in stoichiometric amounts (PMID:17322308)."
1098;DNA synthesome complex (13 subunits);;Human;P12004,P09884,Q14181,P28340,P49005,Q15054,Q9HCU8,P49642,P49643,P35251,P27694,P11387,(P11388,Q02880);5111,5422,23649,5424,5425,10714,57804,5557,5558,5981,6117,7150,(7153,7155);MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients;9279361;10.01.03,70.10;"";"";""
1099;DNA synthesome complex (17 subunits);;Human;P12004,P09884,Q14181,P28340,P49005,Q15054,Q9HCU8,Q07864,P56282,Q9NRF9,Q9NR33,P49642,P49643,P35251,P27694,P11387,(P11388,Q02880);5111,5422,23649,5424,5425,10714,57804,5426,5427,54107,56655,5557,5558,5981,6117,7150,(7153,7155);MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients;9114436;10.01.03,70.10;"";"";""
1100;DNA polymerase alpha-primase complex;;Human;P09884,Q14181,P49642,P49643;5422,23649,5557,5558;MI:0226- ion exchange chromatography;12220650;10.01.03.03,70.10;"DNA polymerase alpha-primase can initiate DNA synthesis de novo.";"";""
1101;TFIIIC containing complex TFIIIC2;;Human;Q12789,Q8WUA4,Q9Y5Q9,Q9UKN8,Q9Y5Q8;2975,2976,9330,9329,9328;MI:0006- anti bait coimmunoprecipitation;10373544;11.02.03.04,16.03.01,70.10;"";"";""
1103;Wave1-Bcl-xl-Pancortin-2 complex, focal ischemic stroke induced;;Mouse;Q61337,O88998,Q8R5H6;12015,56177,83767;MI:0019- coimmunoprecipitation;17301160;40.10.02.02.01,70.16,73.03.13,77.03.01.01.01;"Under normal conditions, pancortin-2 is enriched in the adult cerebral cortex but does not interact with WAVE1 and Bcl-xL. The results show that focal ischemic stroke caused the enhancement of the interactions between WAVE1, pancortin-2, and Bcl-xL, which was not attributable to a change in the amounts of these proteins in the cells. The binding of Bcl-xL to WAVE1 is dependent on pancortin-2, and pancortin-2 serves a proapoptotic role in focal ischemic stroke by a mechanism related to its binding to WAVE1 and Bcl-xL. The pancortin-2-WAVE1-Bcl-xL protein complex is associated with mitochondria, and Bax translocation to mitochondria and cytochrome c release is suppressed after brain ischemia in pancortin-/- mice.";"Wave1-Bcl-xl-Pancortin-2 complex is involved in ischemic stroke.";""
1104;SNX complex (SNX1a, SNX2, SNX4, TFRC); Transferrin receptor complex;Human;Q13596,O60749,O95219,P02786;6642,6643,8723,7037;MI:0019- coimmunoprecipitation;9819414;20.01.10,20.09.07.29,20.09.18.09.01.01;"";"";"At the time of annotation, the additional member SNX1a of the protein complex was not found in the UniProt database."
1105;TFIIIC containing complex;;Human;Q12789,Q8WUA4,Q9Y5Q9,Q9UKN8,Q9Y5Q8;2975,2976,9330,9329,9328;MI:0029- cosedimentation through density gradients;9660958;11.02.03.04,16.03.01,70.10;"The authors differentiate two forms of the isolated complexes, the sucrose gradient centrifugation isolated complex and the immunopurified complex of Hela S3 cell line (C alpha 12), which is called holo TFIIIC. Only the holo TFIIIC shows the further additional components topo I and PC4.";"";"At the time of annotation, the additional members of subcomplex TFIIIC1, 70 kDa, 50 kDa, 45kDa and 40 kDa protein were unidentified. "
1106;TFIIIC containing-TOP1-SUB1 complex;;Human;Q12789,Q8WUA4,Q9Y5Q9,Q9UKN8,Q9Y5Q8,P53999,P11387;2975,2976,9330,9329,9328,10923,7150;MI:0007- anti tag coimmunoprecipitation;9660958;11.02.03.04,16.03.01,70.10;"The authors differentiate two forms of the isolated complexes, the sucrose gradient centrifugation isolated complex and the immunopurified complex of Hela S3 cell line (C alpha 12), which is called holo TFIIIC. Only the holo TFIIIC shows the further additional components topo I and PC4.";"";"At the time of annotation, the additional members of subcomplex TFIIIC1, 70 kDa, 50 kDa, 45kDa -and 40 kDa protein were unidentified. "
1107;DNA synthesome core complex;;Human;P12004,P09884,Q14181,P28340,P49005,Q15054,Q9HCU8,P49642,P49643,P35251;5111,5422,23649,5424,5425,10714,57804,5557,5558,5981;MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients;9563011;10.01.03,70.10;"";"";""
1108;DNA synthesome complex (15 subunits);;Human;P18858,P12004,P09884,Q14181,P28340,P49005,Q15054,Q9HCU8,Q07864,P56282,Q9NRF9,Q9NR33,P49642,P49643,P35251;3978,5111,5422,23649,5424,5425,10714,57804,5426,5427,54107,56655,5557,5558,5981;MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;9563011;10.01.03,70.10;"";"";""
1109;DNA polymerase alpha;;Mouse;P33609,P33611;18968,18969;MI:0091- chromatography technologies | MI:0004- affinity chromatography technologies;2226860;10.01.03,70.10;"Analysis of the DNA products with poly(dA)-oligo(dT)10 as template-primer revealed that both primase-free DNA polymerase-alpha and the DNA polymerase-alpha-primase complex predominantly synthesized short DNA with less than 30 nucleotides (PMID:2226860).";"";""
1110;DNA polymerase alpha-primase complex;;Mouse;P33609,P33611,P20664,P33610;18968,18969,19075,19076;MI:0004- affinity chromatography technologies;2383257;10.01.03,70.10;"";"";""
1111;DNA synthesome complex (17 subunits);;Human;P12004,P09884,Q14181,P28340,P49005,Q15054,Q9HCU8,Q07864,P56282,Q9NRF9,Q9NR33,P49642,P49643,P35251,P27694,P11387,(P11388,Q02880);5111,5422,23649,5424,5425,10714,57804,5426,5427,54107,56655,5557,5558,5981,6117,7150,(7153,7155);MI:0226- ion exchange chromatography | MI:0029- cosedimentation through density gradients | MI:0276- blue native page;11968016;10.01.03,70.10;"This complex associates also with a not further characterized DNA helicase.";"";""
1112;Psd3-Actn1 complex;;Mouse;Q7TPR4,Q2PFD7;109711,234353;MI:0019- coimmunoprecipitation | MI:0018- two hybrid | MI:0096- pull down;17298598;18.02,73.03.13;"EFA6A may form a protein complex with alpha-actinin and activate ARF6 in close proximity of the actin cytoskeleton and membrane proteins in the dendritic spines (PMID:17298598).";"";""
1113;5S-DNA-TFIIIA-TFIIIC2 subcomplex;;Human;Q92664,Q12789,Q8WUA4,Q9Y5Q9,Q9UKN8,Q9Y5Q8;2971,2975,2976,9330,9329,9328;MI:0071- molecular sieving | MI:0004- affinity chromatography technologies;12711686;11.02.03.04,16.03.01,70.10;"This complex could be complemented with TFIIIB beta, TFIIIC1 and RNA polymerase III (pol III) for transcriptional activity.";"";""
1114;5S-DNA-TFIIIA-TFIIIC2-TFIIIB subcomplex;;Human;A6H8Y1,Q92994,Q92664,Q12789,Q8WUA4,Q9Y5Q9,Q9UKN8,Q9Y5Q8,P20226;55814,2972,2971,2975,2976,9330,9329,9328,6908;MI:0071- molecular sieving | MI:0004- affinity chromatography technologies;12711686;11.02.03.04,16.03.01,70.10;"This complex could be complemented with TFIIIC1 and RNA polymerase III (pol III) for full transcriptional activity. Adding pol III to an isolated quaternary 5S-DNA-TFIIIA-TFIIIC2-TFIIIB-beta complex does not suffice for transcription, but the further addition of TFIIIC1 is absolutely required.";"";""
1115;Cdk5/p35 complex (Cdk5-Cdk5r1 complex);;Mouse;P49615,P61809;12568,12569;MI:0019- coimmunoprecipitation;17295212;14.07.03,16.01,47.03.01,73.03.13,77.03.01.01.01;"Astrocytic Cdk5 is involved in  process elongation of scratched  astrocytes.";"The Cdk5-Cdk5r1 complex (also often called Cdk5/p35 complex) is suggested to be involved in Alzheimer's disease (OMIM: 104300). Compare also the CIDER database.";""
1116;CRM1-Survivin-AuroraB mitotic complex;;Human;Q96GD4,O15392,O14980;9212,332,7514;MI:0006- anti bait coimmunoprecipitation;17099693;10.03.01.01,20.09.01,70.10.04;"Crm1 could be recovered in a complex with endogenous Survivin-Aurora-B from mitotic cells, whereas complex formation was abolished on pretreatment with LMB (leptomycin B).";"";""
1117;CRM1-Survivin mitotic complex;;Human;O15392,O14980;332,7514;MI:0007- anti tag coimmunoprecipitation;17099693;10.03.01.01,20.09.01,70.10.04;"The Survivin-Crm1 interaction is essential for chromosomal passenger complex localization and function.";"";""
1118;Chromosomal passenger complex CPC (INCENP, CDCA8, BIRC5, AURKB);;Human;Q96GD4,O15392,Q53HL2,Q9NQS7;9212,332,55143,3619;MI:0007- anti tag coimmunoprecipitation;17099693;10.03.01.01,10.03.04.05,70.10.04;"Borealin forms a complex with Survivin, which can bind to Aurora-B kinase and is incorporated into the CP-holocomplex by interacting with INCENP (PMID:16571674). The NES in Survivin mediates the recruitment of Crm1-Ran-GTP, which seems to be involved in guiding the CPC to the centromeres in early prophase by an unknown mechanism.";"";""
1119;Chromosomal passenger complex CPC (INCENP, CDCA8, BIRC5, AURKB);;Human;Q96GD4,O15392,Q53HL2,Q9NQS7;9212,332,55143,3619;MI:0007- anti tag coimmunoprecipitation;16571674;10.03.01.01,10.03.04.05,16.03.01,70.10.04;"Yeast two hybrid analysis pointed out that Aurora B associates with the C terminus of INCENP via the IN-box, Survivin and Borealin interact with the N-terminal 58 amino acids of INCENP and bind to each other.";"";""
1120;Chromosomal passenger complex CPC (INCENP, CDCA8, BIRC5);;Human;O15392,Q53HL2,Q9NQS7;332,55143,3619;MI:0007- anti tag coimmunoprecipitation;16571674;10.03.01.01,10.03.04.05,16.03.01,70.10.04;"Yeast two hybrid analysis pointed out that Survivin and Borealin interact with the N-terminal 58 amino acids of INCENP and bind to each other. The authors showed that a ternary complex between Borealin, Survivin, and the first 58 amino acids of INCENP (INCENP1-58) exists in vivo. This subcomplex was found to be essential and sufficient for targeting to the centromere. Notably, AuroraB kinase, the enzymatic core of the CPC, was not required for centromere localization of the subcomplex.";"";""
1121;WNK1-OSR1 complex;;Human;O95747,Q9H4A3;9943,65125;MI:0019- coimmunoprecipitation;17190791;16.01,18.02,34.11.03.13;"WNK1 and OSR1 regulate NKCC activity (sodium, potassium, two chloride cotransporter) (PMID:16832045).";"WNK1 is mutated in Gordon's hypertension syndrome. ";""
1122;Smcb-Smcd-PW29 complex;;Mouse;Q61550,Q9CU62,Q9CW03;19357,24061,13006;MI:0006- anti bait coimmunoprecipitation;10375619;10.03.01.01,10.03.04.05,70.10.03;"The authors show that overexpression of a PW29-GFP fusion protein in mouse fibroblasts leads to inhibition of proliferation, implicating this protein and its complex with SMC proteins in the control of mitotic cycle progression.";"";""
1123;WNK1-SPAk complex;;Human;Q9UEW8,Q9H4A3;27347,65125;MI:0019- coimmunoprecipitation;17190791;16.01,18.02,34.11.03.13;" ";"WNK1 is mutated in Gordon's hypertension syndrome.";""
1124;SNARE complex (Snap25, Stx1a, Vamp2, Cplx1, Cplx3);;Mammalia;P63041,Q8R1B5,P60881,P32851,P63045;64832,235415,25012,116470,24803;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1125;SNARE complex (Snap25, Stx1a, Vamp2, Cplx3, Cplx4);;Mammalia;Q8R1B5,Q80WM3,P60881,P32851,P63045;235415,225644,25012,116470,24803;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1126;SNARE complex (Snap25, Stx1a,3, Vamp2, Cplx1, Cplx3, Cplx4);;Mammalia;P63041,Q8R1B5,Q80WM3,P60881,P32851,Q08849,P63045;64832,235415,225644,25012,116470,81802,24803;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The interaction between the SNARE complex and CPX4 indicates a lower binding affinity.";"";""
1127;Shps1-Fyb-Skap55r complex;;Mammalia;O35601,P97797,Q3UND0;23880,19261,54353;MI:0019- coimmunoprecipitation;10469599;30.01.05,34.07,36.25.16.01.03;"Analysis done in randomly growing normal cells and bone marrow derived macrophages (BMM) from mice homozygotic for the motheaten (me) mutation and in transfected COS-7 cell line. Formation of the complex was independent of SHP-1 and tyrosine phosphorylation of SHPS-1.";"";""
1128;Shps1-Pyk2 complex;;Mammalia;Q9QVP9,P97797;19229,19261;MI:0019- coimmunoprecipitation;10469599;30.01.05.01.05,34.07,36.25.16.01.03;"Analysis done in randomly growing normal cells and bone marrow derived macrophages (BMM) from mice homozygotic for the motheaten (me) mutation and in transfected COS-7 cell line. Formation of the complex was independent of SHP-1 and tyrosine phosphorylation of SHPS-1.";"";""
1129;Complexin complex (Stx3, Cplx1, Cplx3);;Mammalia;P63041,Q8R1B5,Q08849;64832,235415,81802;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"All known CPXs interact with SNARE complexes. They may therefore play a role in neurotransmitter release.";"";""
1130;Hip1R-cortactin complex;;Human;Q14247,O75146;2017,9026;MI:0007- anti tag coimmunoprecipitation;17318189;16.07,20.09.14.02,70.03;"The Hip1R-cortactin complex negatively regulates actin assembly associated with endocytosis.";"";""
1131;RFC2-RIalpha complex;;Human;P30153,P35250;5518,5982;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0096- pull down;15655353;16.01;"";"";""
1132;RFC2-RIalpha complex;;Human;P30153,P35249;5518,5984;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0096- pull down;15655353;16.01;"";"";""
1133;ATR-HDAC2 complex;;Human;Q13535,Q92769;545,3066;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;10545197;10.01.09.05,14.07.04,42.10.03;"The ATR-HDAC2 complex is a robust biochemical entity that withstands ammonium sulfate precipitation and anion exchange chromatography.";"";""
1134;ATR-HDAC2-CHD4 complex;;Human;Q13535,Q14839,Q92769;545,1108,3066;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;10545197;10.01.09.05,10.03.01.03,14.07.04,32.01.09,42.10.03,70.10;"Other members of the NRD complex HDAC1, MTA-1, and MTA-2 are also detectable in ATR immunoprecipitates.";"";""
1135;Mss4-Itga3 complex;;Mouse;Q62470,Q91X96;16400,98710;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;17172637;16.01,18.02,70.02;"Mss4 binds to the cytosolic membrane proximal conserved region of {alpha}-integrin chains and this interaction is essential for MT1-MMP-mediated activation of MMP-2 and -9 as well as for ECM organization (PMID:17172637).";"";""
1136;Mss4-Itga7 complex;;Mouse;Q61738,Q91X96;16404,98710;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;17172637;16.01,18.02,70.02;"Mss4 binds to the cytosolic membrane proximal conserved region of {alpha}-integrin chains and this interaction is essential for MT1-MMP-mediated activation of MMP-2 and -9 as well as for ECM organization (PMID:17172637).";"";""
1137;SNARE complex (VAMP2, SNAP25, STX1a, CPLX1, CPLX3);;Human;O14810,Q8WVH0,P60880,Q16623,P63027;10815,594855,6616,6804,6844;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1138;SNARE complex (VAMP2, SNAP25, STX1a, CPLX3, CPLX4);;Human;Q8WVH0,Q7Z7G2,P60880,Q16623,P63027;594855,339302,6616,6804,6844;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The interaction between the SNARE complex and CPX4 indicates a lower binding affinity.";"";""
1139;SNARE complex (VAMP2, SNAP25, STX1a, STX3, CPLX1, CPLX3, CPLX4);;Human;O14810,Q8WVH0,Q7Z7G2,P60880,Q16623,Q13277,P63027;10815,594855,339302,6616,6804,6809,6844;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The interaction between the SNARE complex and CPX4 indicates a lower binding affinity.";"";""
1140;Complexin complex (STX3, CPLX1, CPLX3);;Human;O14810,Q8WVH0,Q13277;10815,594855,6809;MI:0027- cosedimentation;15911881;20.09.07.27,20.09.16.09.05;"";"";""
1141;CF IIAm complex (Cleavage factor IIAm complex);;Human;Q14444,Q92989,Q9UKF6,Q16630,Q8N684,O60231,P19447,Q92759,P49959,O43809,O94913,P26599,P23246,Q07157,Q01081,P26368;4076,10978,51692,11052,79869,8449,2071,2968,4361,11051,51585,5725,6421,7082,7307,11338;MI:0226- ion exchange chromatography;11060040;11.04.03.05,70.10;"Eukaryotic mRNA precursors (pre-mRNAs) undergo a number of processing steps before they are exported to the cytoplasm. Six different protein factors are required in vitro for 3' end formation of mammalian pre-mRNAs by endonucleolytic cleavage and polyadenylation. One of these factors is cleavage factor IIm (CF IIm). During purification of CF IIm, the activity separated into an essential fraction (CF IIAm) and an apparently non-essential, but stimulatory component (CF IIBm).";"";""
1142;SMN complex;;Human;Q9UHI6,O14893,Q16637,P14678,P62314,P62316,P62318,P62304,P62306,P62308;11218,8487,6606,6628,6632,6633,6634,6635,6636,6637;MI:0019- coimmunoprecipitation;10601333;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"Assembly of the Sm-class of U-rich small nuclear ribonucleoprotein particles (U snRNPs) is a process facilitated by the macromolecular survival of motor neuron (SMN) complex. Spinal muscular atrophy (SMA) is the most common genetic cause of infant mortality. Deletions or mutations in the survival of motor neurons (SMN1) gene, the SMA-causing gene, are detected in over 95% of SMA patients. The SMN complex is found both in the cytoplasm and in the nucleus, where it is concentrated in gems, nuclear bodies similar in size and number to Cajal (coiled) bodies and often associated with them.";"Spinal muscular atrophy (SMA)";"Several other subunits of the complex were found in the analysis, which have not been further characterized:  p175, p95, p60, p50 using anti-SMN (2B1) or p175, p115, p95, p50 using anti-Gemin3 (11G9). "
1143;SMN complex;;Human;Q9UHI6,P57678,Q8TEQ6,Q8WXD5,Q9H840,Q9NWZ8,O14893,Q16637,P14678,P62314,P62316,P62318,P62304,P62306,P62308,Q9Y3F4;11218,50628,25929,79833,79760,54960,8487,6606,6628,6632,6633,6634,6635,6636,6637,11171;MI:0019- coimmunoprecipitation;17178713;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"Assembly of the Sm-class of U-rich small nuclear ribonucleoprotein particles (U snRNPs) is a process facilitated by the macromolecular survival of motor neuron (SMN) complex.  Spinal muscular atrophy (SMA) is the most common genetic cause of infant mortality. Deletions or mutations in the survival of motor neurons (SMN1) gene, the SMA-causing gene, are detected in over 95% of SMA patients. The SMN complex is found both in the cytoplasm and in the nucleus, where it is concentrated in gems, nuclear bodies similar in size and number to Cajal (coiled) bodies and often associated with them. Nine factors, including the SMN protein, the product of the spinal muscular atrophy (SMA) disease gene, Gemins 2-8  and unrip have been identified as the major components of the SMN complex. Interaction studies in the present article revealed a framework of the SMN complex with SMN, Gemin7, and Gemin8 as its backbone.";"Spinal muscular atrophy (SMA)";""
1144;Cleavage and polyadenylation factor (CPSF);;Human;Q10570,Q9P2I0,Q9UKF6,O95639,Q6UN15;29894,53981,51692,10898,81608;MI:0019- coimmunoprecipitation;14749727;11.04.03.05,16.03.03,18.01.07,18.02.01,70.10;"In mammals, polyadenylation of mRNA precursors (pre-mRNAs) by poly(A) polymerase (PAP) depends on cleavage and polyadenylation specificity factor (CPSF). CPSF is a multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.";"";""
1145;Mammalian cleavage factor I (CF Im);;Mammalia;Q16630,O43809;11052,11051;MI:0019- coimmunoprecipitation;17172643;11.04.03.05,16.03.03,70.10;"Eukaryotic mRNA precursors (pre-mRNAs) undergo a number of processing steps before they are exported to the cytoplasm. The binding of CF Im to the pre-mRNA is thought to be one of the earliest steps in the assembly of the cleavage and polyadenylation machinery and facilitates the recruitment of other processing factors.";"";"Since NUDT21 and CPSF6 from green monkey were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1146;Cleavage stimulation factor;;Human;Q05048,P33240,Q12996;1477,1478,1479;MI:0019- coimmunoprecipitation;10669729;11.04.03.05,16.03.03,70.10;"Polyadenylation of mRNA precursors is a two-step reaction requiring multiple protein factors. Cleavage stimulation factor (CstF) is a heterotrimer necessary for the first step, endonucleolytic cleavage, and it plays an important role in determining the efficiency of polyadenylation. The cleavage and polyadenylation specificity factor (CPSF) recognizes the highly conserved hexanucleotide AAUAAA, whereas CstF binds to GU- or U-rich elements downstream of the poly(A) site.";"";""
1147;Polyadenylation complex (CSTF1, CSTF2, CSTF3, SYMPK CPSF1, CPSF2, CPSF3);;Human;Q10570,Q9P2I0,Q9UKF6,Q05048,P33240,Q12996,Q92797;29894,53981,51692,1477,1478,1479,8189;MI:0019- coimmunoprecipitation;10669729;11.04.03.05,16.03.03,70.10;"Polyadenylation of mRNA precursors is a two-step reaction requiring multiple protein factors. The polyadenylation complex (containing Cstf1, Cstf2, Cstf3, Sympk, Cpsf1, Cpsf2 and Cpsf3), which contains the cleavage stimulation factor (CstF) and subunits of the cleavage and polyadenylation specificity factor (CPSF) might consist of more protein components.";"";""
1148;snRNP-free U1A (SF-A) complex;;Human;P17844,Q15233,P23246,P09012;1655,4841,6421,6626;MI:0096- pull down;16373496;11.04.03.05,16.03.03,70.10;"The formation of mRNAs in the nuclei of eukaryotic cells involves several co- and post-transcriptional processing events, including 5' end capping, RNA splicing, and 3' end formation. The SF-A complex was found to be involved in cleavage of the mRNA precursor, an essential step of the 3' end formation process.";"";""
1149;Histone H3.1 complex;;Human;Q9Y294,Q9NVP2,Q13111,Q13112,O14929,P68431,P62805,Q8TEX9,P49321,Q09028;25842,55723,10036,8208,8520,8350,554313,79711,4678,5928;MI:0019- coimmunoprecipitation;14718166;14.10,70.10;"The H3.1 and H3.3 complexes contain distinct histone chaperones, CAF-1 and HIRA, that were shown to be necessary to mediate DNA-synthesis-dependent and -independent nucleosome assembly, respectively.";"";""
1150;Histone H3.3 complex;;Human;Q9Y294,Q9NVP2,P84243,O14929,P54198,P62805,Q8TEX9,P49321,Q09028;25842,55723,3020,8520,7290,554313,79711,4678,5928;MI:0019- coimmunoprecipitation;14718166;14.10,70.10;"The H3.1 and H3.3 complexes contain distinct histone chaperones, CAF-1 and HIRA, that were shown to be necessary to mediate DNA-synthesis-dependent and -independent nucleosome assembly, respectively.";"";""
1151;Sycp1-Syce1-Syce2 complex;;Mouse;Q9D495,Q505B8,Q62209;74075,71846,20957;MI:0019- coimmunoprecipitation;15944401;10.03.02,70.10;"Completion of meiosis in mammals depends on the formation of the synaptonemal complex, a tripartite structure that physically links homologous chromosomes during prophase I. The function of the Sycp1-Syce1-Syce2 complex is not entirely clear, experiments suggest a role in synaptonemal-complex assembly, and perhaps also stability and recombination.";"";""
1152;FA complex (Fanconi anemia complex);;Human;O15360,Q8NB91,Q00597,Q9HB96,Q9NPI8,O15287,Q9NW38,Q8IYD8;2175,2187,2176,2178,2188,2189,55120,57697;MI:0019- coimmunoprecipitation;16116422;14.07.05,32.01.09,70.10;"The Fanconi complex normally promotes a cascade of changes in a biochemical pathway that ultimately leads to the repair of cellular DNA damage. But if any of the proteins within the complex are mutated, the enzyme FancL is disabled and the DNA repair pathway is disrupted. ";"FA complex is involved in Fanconi anemia (FA) disease.";""
1153;Integrator complex;;Human;Q5TA45,Q8N201,Q9NVR2,Q96CB8,Q9H0H0,Q68E01,Q96HW7,Q6P9B9,Q9UL03,Q9NVH2,Q75QN2,Q9NV88;54973,26173,55174,57117,57508,65123,92105,80789,26512,25896,55656,55756;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;16239144;11.04,70.10;"The Intergrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3' box-dependent processing. The Integrator complex is recruited to the U1 and U2 snRNA genes and mediates the snRNAs 3' cleavage.";"";""
1154;DSS1 complex;;Human;P51587,Q5TA45,Q9NVR2,Q9H0H0,Q96HW7,Q6P9B9,Q9UL03,Q9NVH2,Q75QN2,Q9NV88,Q96PV6,A6H687,P60896;675,54973,55174,57508,92105,80789,26512,25896,55656,55756,114823,66406,7979;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;16239144;70.10;"";"";"Since human SAC3D1 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
1155;Integrator-RNAPII complex;;Human;Q5TA45,Q8N201,Q9NVR2,Q96CB8,Q9H0H0,Q68E01,Q96HW7,Q6P9B9,Q9UL03,Q9NVH2,Q75QN2,Q9NV88,P24928,P30876;54973,26173,55174,57117,57508,65123,92105,80789,26512,25896,55656,55756,5430,5431;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;16239144;11.02,11.04,70.10;"The integrator complex interacts with the C-terminal domain of the RNA Polymerase II. The integrator-RNAPII complex mediates RNAPII-dependent transcription of at least U1 and U2 snRNA genes.";"";""
1156;PS1-E-cadherin-catenin complex, epithelial;;Dog;P09803,P26231,Q02248,P49769;12550,12385,12387,19164;MI:0006- anti bait coimmunoprecipitation | MI:0029- cosedimentation through density gradients;10635315;34.07.01,42.06.04,70.06.04,75.03.09;"Disruption of Ca(2+)-dependent cell-cell contacts reduces surface PS1 and the levels of PS1-E-cadherin complexes. PS1 concentrates at intercellular contacts in epithelial tissue- in brain it forms complexes with both E- and N-cadherin and concentrates at synaptic adhesions.";"";"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
1157;PS1-E-cadherin-catenin complex, brain;;Mouse;P09803,P15116,Q02248,P49769;12550,12558,12387,19164;MI:0006- anti bait coimmunoprecipitation;10635315;16.17.01,34.07.01,42.06.04,70.06.04,73.03.13,77.03.01.01.01;"PS1 concentrates at intercellular contacts in epithelial tissue- in brain it forms complexes with both E- and N-cadherin and concentrates at synaptic adhesions.";"";""
1158;p33ING1b-p300 complex;;Human;Q09472,Q9UK53;2033,3621;MI:0006- anti bait coimmunoprecipitation;12015309;10.01.09.05,10.03.01,14.07.04,42.10.03,70.10.03;"Anti-p300 immunoprecipitates contained p33ING1b, but not p47ING1a.";"";""
1159;p33ING1b-HDAC1 complex;;Human;Q13547,Q9UK53;3065,3621;MI:0006- anti bait coimmunoprecipitation;12015309;10.01.09.05,10.03.01,14.07.04,42.10.03,70.10.03;"HDAC1 interacts as well with p33ING1b as with p47ING1a.";"";""
1160;ING1-p300-PCNA complex;;Human;Q09472,Q9UK53,P12004;2033,3621,5111;MI:0006- anti bait coimmunoprecipitation;12015309;10.01.05.01,10.01.09.05,10.03.01,14.07.04,42.10.03,70.10.03;"p33ING1b affects the degree of physical association between proliferating cell nuclear antigen (PCNA) and p300.";"";""
1161;Smrt-Sin3A-Hdac7 complex;;Mouse;Q8C2B3,Q9WU42,Q60520;56233,20602,20466;MI:0007- anti tag coimmunoprecipitation;10640276;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"";"";""
1162;Ubiquitin E3 ligase (DDB1, DDB2, CUL4A, CUL4B, RBX1);;Human;Q13619,Q13620,Q16531,Q92466,P62877;8451,8450,1642,1643,9978;MI:0071- molecular sieving | MI:0226- ion exchange chromatography;16678110;14.07.05,18.01.01,32.01.09,32.01.13,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The CUL4-DDB-ROC1 complex is a ubiquitin E3 ligase for histones H3 and H4. CUL4-DDB-ROC1-mediated H3 and H4 ubiquitylation was shown to facilitate cellular response to UV damage by affecting nucleosome stability.";"";""
1163;ING1-PCNA complex;;Human;Q9UK53,P12004;3621,5111;MI:0006- anti bait coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11682605;32.01.09,32.01.13,40.10,70.10.03;"UV rapidly induces p33ING1b, but not p47ING1a isoform, to bind PCNA.";"";""
1164;ActRIIA-ActRIB-Smad3-Arip1 complex;;Mouse;Q61271,P27038,Q9WVQ1,Q8BUN5;11479,11480,50791,17127;MI:0007- anti tag coimmunoprecipitation;10681527;30.05.01.18,73.03.13,75.03.17,77.03.01;"When COS-7 cells cotransfected with ActRIIA, ActRIB(K234R), 6Myc-ARIP1, and FLAG-Smad3 were incubated in the presence of (125)I-activin A, the (125)I-labeled receptor complex could be precipitated by either of the anti-Myc and anti-FLAG antibodies. Therefore, ARIP1 is capable of forming a complex with ActRIIA, ActRIB, and Smad3 in the presence of ligand.";"";""
1165;RNF20-RNF40-UbE2E1 complex; RNF20/40 complex;Human;Q5VTR2,O75150,P51965;56254,9810,7324;MI:0096- pull down;16307923;11.02.03.04,14.07.05,70.10;"In humans, the 600 kDa RNF20/40 complex is the E3 ligase and UbcH6 is the ubiquitin E2-conjugating enzyme for H2B-Lys120 monoubiquitination.";"";""
1166;p400-associated complex;;Human;P60709,Q96L91,Q9Y265,Q9Y230,Q9Y4A5,(O96019,O94805);60,57634,8607,10856,8295,(86,51412);MI:0004- affinity chromatography technologies;11509179;01.04,10.01.02,10.01.09.05,16.01,42.10.03,70.10;"";"";""
1167;Paf complex; hPAF complex;Human;Q6P1J9,Q6PD62,Q8WVC0,Q8N7H5,Q9GZS3;79577,9646,123169,54623,80349;MI:0096- pull down;16307923;11.02.03.01,70.10;"hPAF participates in histone H2B monoubiquitiation. In addition, hPAF coordinates events during transcription (initiation, promoter clearance, and elongation) and also events in RNA quality control. The hPAF complex interacts with the hSKI complex.";"";""
1168;SKI complex; hSKI complex;Human;Q15477,Q6PGP7,Q9GZS3;6499,9652,80349;MI:0071- molecular sieving | MI:0019- coimmunoprecipitation;16024656;11.02.03.01,11.02.03.04,70.03,70.10;"hSKI complex is present at transcriptionally active genes with recruitment dependent on hPAF complex.";"";""
1169;SNARE complex (STX4, VAMP8, VAMP3, SNAP23);;Human;O00161,Q12846,Q15836,Q9BV40;8773,6810,9341,8673;MI:0019- coimmunoprecipitation;12130530;20.09.07.27,20.09.16.09.05,73.03.07.03;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. VAMP-3 and VAMP-8 form SNARE complexes with platelet syntaxin 4 and are required for platelet granule secretion.";"";""
1170;cMYC-ATPase-helicase complex;;Human;O96019,P01106,Q9Y265,Q9Y230,Q9Y4A5;86,4609,8607,10856,8295;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;10882073;10.01.02,10.01.09.05,11.02.03.04,14.07.04,16.03.01,42.10.03,70.10;"TIP49 and TIP48 are complexed with c-Myc in vivo, and binding is dependent on a c-Myc domain essential for oncogenic activity. TIP49 protein is an essential mediator of c-Myc oncogenic transformation.";"";"BAF53 and beta-actin have been described in this paper as p45 and p41. Both subunits were identified in the succeeding paper PMID:11839798."
1171;c-MYC-ATPase-helicase complex;;Human;O96019,P01106,Q9Y265,Q9Y230,Q9Y4A5;86,4609,8607,10856,8295;MI:0006- anti bait coimmunoprecipitation;11839798;10.01.02,10.01.09.05,11.02.03.04,14.07.04,16.03.01,42.10.03,70.10;"";"";""
1172;CBC complex (cap binding complex);;Human;Q09161,P52298;4686,22916;MI:0413- electrophoretic mobility shift assay;10786834;16.03.03,20.01.21,20.09.01,70.10;"The heterodimeric nuclear cap binding complex (CBC) binds to 5'-capped polymerase II transcripts. It enhances the efficiency of several mRNA maturation steps and is essential for U snRNA nuclear export in multicellular eukaryotes.";"";""
1173;TIP49-TIP48-BAF53 complex;;Human;O96019,Q9Y265,Q9Y230;86,8607,10856;MI:0007- anti tag coimmunoprecipitation;11839798;10.01.02,70.10;"";"";""
1174;PHAX-CBC complex (cap binding complex);;Human;Q09161,P52298,Q9H814;4686,22916,51808;MI:0413- electrophoretic mobility shift assay;10786834;16.03.03,20.01.21,20.09.01,70.03,70.10;"In metazoa, assembly of spliceosomal U snRNPs requires nuclear export of U snRNA precursors. Export depends upon the RNA cap structure, nuclear cap-binding complex (CBC), the export receptor CRM1/Xpo1, and RanGTP. PHAX (phosphorylated adaptor for RNA export) is an additional factor required for U snRNA export complex assembly in vitro. In vivo, PHAX is required for U snRNA export but not for CRM1-mediated export in general. PHAX is phosphorylated in the nucleus and then exported with RNA to the cytoplasm, where it is dephosphorylated. PHAX phosphorylation is essential for export complex assembly while its dephosphorylation causes export complex disassembly. The compartmentalized PHAX phosphorylation cycle can contribute to the directionality of export. PHAX binding to CBC is greatly increased by the presence of capped RNA.";"";""
1175;TRRAP-BAF53-HAT complex;;Human;O96019,Q9Y4A5;86,8295;MI:0007- anti tag coimmunoprecipitation;11839798;10.01.09.05,11.02.03.04,14.07.04,42.10.03,70.10;"TRRAP and BAF53 associate with an up to now not identified histone acetyltransferase activity which does not contain TIP60, TIP49 or TIP48.";"";""
1176;CRM1-RAN-PHAX-CBC complex (cap binding complex);;Human;Q09161,P52298,P62826,Q9H814,O14980;4686,22916,5901,51808,7514;MI:0413- electrophoretic mobility shift assay | MI:0430- nucleic acid uv cross-linking assay;10786834;16.03.03,20.01.21,20.09.01,70.03,70.10;"In metazoa, assembly of spliceosomal U snRNPs requires nuclear export of U snRNA precursors. Export depends upon the RNA cap structure, nuclear cap-binding complex (CBC), the export receptor CRM1/Xpo1, and RanGTP. PHAX (phosphorylated adaptor for RNA export) is an additional factor required for U snRNA export complex assembly in vitro. PHAX binding to CBC is greatly increased by the presence of capped RNA. Phosphorylated PHAX can bind to RanGTP/Xpo1 but does so more strongly in the presence of CBC and even more in the presence of both CBC and RNA. Thus, every step in U snRNA export complex formation involves some degree of cooperativity.";"";""
1177;Polycomb repressive complex 4 (PRC4);;Human;O75530,Q15910,Q96EB6;8726,2146,23411;MI:0071- molecular sieving | MI:0226- ion exchange chromatography;15684044;10.01.09.05,11.02.03.04.07,14.07.09,42.10.03,70.10;"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. They are methylating histones at lysine residues. PRC4 methylates preferentially the histone H1b isoform, whereas PRC2 methylated preferentially the histone H1d isoform. The PRC3 complex exclusively targets methylation of histone H3-K27, and the activity is repressed in the presence of histone H1. PRC2 also methylates histone H3-K27 but in the presence of histone H1, PRC2 methylates both H3-K27 and H1-K26. ";"PRC complexes are overexpressed in breast, colon, and prostate cancers.";""
1178;BCOR complex; Ubiquitin E3 ligase;Human;Q6W2J9,Q8NHM5,P11142,Q9BSM1,Q06587,Q99496,Q8N488,P63208;54880,84678,3312,84759,6015,6045,23429,6500;MI:0019- coimmunoprecipitation;16943429;14.07.05,18.01.01,18.02.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The BCOR complex contains E3 ligase activity for histone H2A. Monoubiquitylated H2A is present together with the BCOR complex at BCL6 target genes in B cells. This strongly suggests a role of BCOR as regulator of BCL6, a sequence-specific transcriptional repressor, that probably plays an important role in lymphomagenesis.";"";""
1179;CENP-A NAC-CAD complex;;Human;Q8N2Z9,Q03188,Q9H3R5,Q9BS16,Q8N0S6,Q9NSP4,Q96H22,Q9BU64,Q6IPU0,Q7L2Z9,Q96BT3,Q13352,Q71F23;378708,1060,64946,64105,91687,79019,55839,79172,401541,55166,80152,23421,79682;MI:0676- tandem affinity purification;16622419;10.01.09.07,10.03.04.01,10.03.04.05,10.03.05.01,70.10.04;"Assembly of CENP-A NAC complex at centromeres is dependent on CENP-M, CENP-N and CENP-T.";"";""
1180;Sur2 subcomplex of mediator;;Mouse;Q6PGF3,Q80YQ2,Q99K74;216154,70208,23989;MI:0019- coimmunoprecipitation;11934987;11.02.03.04.01,18.01.07,18.02.09,30.01.05.01.03,70.10;"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. In the absence of Sur2 murine Med100 and Med95 were reduced. The results suggest that the mammalian Mediator contains a Sur2 subcomplex that includes Sur2, Med100, and Med95. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";""
1181;C complex spliceosome;;Human;O60306,Q8WUQ7,O60508,Q99459,Q9BZJ0,Q9P013,Q9HCG8,Q9BUQ8,Q9UJV9,P17844,Q96DF8,Q9H5Z1,Q92620,Q14562,Q15029,P38919,Q14331,Q9BRR8,P09651,P22626,P51991,P07910,P52597,P31943,P61978,P52272,O43390,Q00839,Q9ULR0,Q9Y333,P62310,P61326,Q9BRX9,P11940,O43660,Q9H307,Q9UNP9,Q9Y3C6,Q9H2H8,Q96BP3,Q9UMS4,Q13523,O94906,Q6P2Q9,Q9UKM9,Q9NW64,Q9Y5S9,P38159,O43290,Q6UX04,Q15459,Q15428,Q12874,O75533,Q13435,Q15393,Q07955,P42285,O95391,O75643,Q96DI7,P09661,P14678,P08579,P62314,P62316,P62318,P62304,P62306,P62308,Q13573,Q8IYB3,Q9UQ35,O95926,O60506,Q9UBB9,Q86V81,Q01081,Q9HCS7,Q6NZY4;9716,58509,51362,988,51340,51503,57703,9416,51428,1655,8220,60625,9785,1659,9343,9775,2483,55094,3178,3181,220988,3183,3185,3187,3190,4670,10236,3192,57461,57819,27258,4116,84292,26986,5356,5411,10450,51645,53938,23398,27339,8899,24148,10594,22913,55696,9939,27316,9092,10283,10291,8175,10946,23451,10992,23450,6426,23517,10569,23020,9410,6627,6628,6629,6632,6633,6634,6635,6636,6637,22938,10250,23524,25949,10492,24144,10189,7307,56949,55596;MI:0028- cosedimentation in solution | MI:0096- pull down;11991638;16.03.03,11.04.03.01,70.10;"In eukaryotes, the removal of introns from nascent transcripts is mediated by a highly dynamic, macromolecular machine called the spliceosome.";"";""
1182;CDC5L core complex;;Human;O75934,Q99459,Q92616,P11142,O43660,Q9UMS4;10286,988,10985,3312,5356,27339;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;11101529;11.04.03.01,16.03.03,70.10;"The CDC5L complex incorporates into the spliceosome in an ATP-dependent step. This complex is required for the second catalytic step of pre-mRNA splicing. Immunodepletion of the CDC5L complex from HeLa nuclear extract inhibits the formation of pre-mRNA splicing products in vitro but does not prevent spliceosome assembly. Experiments indicate that there exists a CDC5L core complex in HeLa nuclear extract containing at least six proteins that interact with each other and with other splicing factors and enzymes.";"";""
1183;CDC5L complex;;Human;O75934,Q7L1Q6,Q99459,Q9P013,Q14204,Q92616,P11142,Q12905,O43660,O15297,P62136,P78527,Q9UMS4,Q9UPN6,P38159,O75533,Q13435,Q15427,A8K8P3,P23246,Q07955,Q01130,P09012,P09661,P62314,P62316,P62318,Q8IYB3,P15884,P11388;10286,9689,988,51503,1778,10985,3312,3608,5356,8493,5499,5591,27339,22828,27316,23451,10992,10262,9814,6421,6426,6427,6626,6627,6632,6633,6634,10250,6925,7153;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;11101529;11.04.03.01,16.03.03,70.10;"The CDC5L complex incorporates into the spliceosome in an ATP-dependent step. This complex is required for the second catalytic step of pre-mRNA splicing. Immunodepletion of the CDC5L complex from HeLa nuclear extract inhibits the formation of pre-mRNA splicing products in vitro but does not prevent spliceosome assembly.";"";""
1184;Mediator complex; Mediator of transcriptional regulation;Mouse;Q62447,Q5U427,Q925J9,Q6PGF3,Q80YQ2,Q99K74,Q921D4,Q569Z6,(A2AGH6,A2AGH8,A2AGH9);51813,264064,19014,216154,70208,23989,69792,230753,(59024,0,0);MI:0019- coimmunoprecipitation | MI:0071- molecular sieving | MI:0069- mass spectrometry studies of complexes;11934987;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10;"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.";"";"At the time of annotation, the additional member med200 of the protein complex was not found in the UniProt database. "
1185;EGFR-containing signaling complex;;Human;P00533,P04626,O00443,O00750;1956,2064,5286,5287;MI:0019- coimmunoprecipitation;10805725;30.05.01.12.01;"EGF stimulation recruits both PI3K-C2alpha  and PI3K-C2beta  to the EGFR-containing signaling complex, together with ErbB-2.";"";""
1186;ESCRT-III complex;;Human;Q9HD42,Q7LBR1,O43633,Q9UQN3,Q9BY43,Q9H444,Q96CF2,Q9NZZ3,Q96FZ7,Q9Y3E7;5119,57132,27243,25978,29082,128866,92421,51510,79643,51652;MI:0007- anti tag coimmunoprecipitation;14519844;14.04,20.01.10,20.09.07,70.03;"The ESCRT-III complex is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-III complex is probably involved in the concentration of MVB cargo. In the ESCRT-III complex, it probably serves as an acceptor for ESCRT-II complex on endosomal membranes. In case of infection, the HIV-1 virus takes advantage of the ESCRT-III complex for budding and exocytic cargos of viral proteins.";"";""
1187;ESCRT-II complex;;Human;Q96H20,Q9BRG1,Q86VN1;11267,84313,51028;MI:0007- anti tag coimmunoprecipitation;14519844;14.04,20.01.10,20.09.07,70.03;"The ESCRT-II complex is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.";"";""
1188;SMRT core complex; TBL1-SMRT-HDAC3 complex;Human;O15379,Q9Y618,O60907;8841,9612,6907;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes | MI:0019- coimmunoprecipitation;10809664;10.01.09.05,11.02.03.04.03,14.07.04,30.01.09.08,30.01.11,42.10.03,70.10;"HDAC3 did not interact directly with TBL1. However, addition of SMRT to the mixture of HDAC3 and TBL1 allowed formation of a stable TBL1-SMRT-HDAC3 complex in vitro, suggesting that SMRT mediates the association of TBL1 and HDAC3 in a single complex in vivo.";"TBL1 is involved in deafness.";""
1189;DNA double-strand break end-joining complex;;Human;P49917,P49959,O60934,Q92878,Q13426,P13010,P12956;3981,4361,4683,10111,7518,7520,2547;MI:0091- chromatography technologies | MI:0071- molecular sieving;11809878;10.01.05.01,16.03.01,32.01.09,70.10;"";"";""
1190;NCBP-NIP1 complex;;Human;Q09161,Q96P71;4686,63941;MI:0018- two hybrid;7478990;16.03.03,18.02,70.10;"";"";""
1191;RNA pol II containing coactivator complex Tat-SF;;Human;P50750,O43719,P19338,P24928,O00267;1025,27336,4691,5430,6829;MI:0071- molecular sieving | MI:0019- coimmunoprecipitation;10393184;11.02.03.04,16.03.01,70.10;"All fractions with Tat stimulatory activity contained these components as well as CDK9.";"";""
1192;ESCRT-I complex;;Human;Q99816,Q9UK41,A5D8V6;7251,51160,55048;MI:0007- anti tag coimmunoprecipitation;15509564;14.04,20.01.10,20.09.07,70.03,70.07;"ESCRT-I is one of three defined protein complexes in the class E vacuolar protein sorting (VPS) pathway required for the sorting of ubiquitinated transmembrane proteins into internal vesicles of multivesicular bodies.";"";""
1193;Rap1 complex;;Human;P49959,P09874,Q92878,Q15554,Q9NYB0,P13010,P12956;4361,142,10111,7014,54386,7520,2547;MI:0007- anti tag coimmunoprecipitation;15100233;16.03.01,32.01.09,42.10.03,70.10;"This complex is responsible for proper maintenance of telomere length and structure. Rad50, Mre11 and Ku86 are recruited to Rap1 independent of TRF2. PARP1, however, most likely interacts with Rap1 through TRF2.";"";""
1194;E2F-6 complex; E2F6.com-1 complex;Human;O75461,Q9H9B1,Q96KQ7,O75712,Q969R5,P61244,Q8IWI9,Q9BYE7,Q06587,Q99496,Q14186,Q8IY57;1876,79813,10919,2707,83746,4149,23269,84108,6015,6045,7027,10138;MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;12004135;11.02.03.04.03,14.07.09,16.03.01,70.10;"The E2F-6 complex occupies target promoters like E2F binding elements and contains chromatin modifiers such as histone methyltransferases. Data suggest that these chromatin modifiers contribute to silencing of E2F- and Myc-responsive genes in quiescent cells.";"";""
1195;Exon junction complex (mRNA splicing-dependent);;Human;Q6P2Q9,Q8IYB3;10594,10250;MI:0029- cosedimentation through density gradients | MI:0019- coimmunoprecipitation | MI:0430- nucleic acid uv cross-linking assay;10809668;11.04.03.01,16.03.03,70.10;"The results indicate that splicing alters the complement of proteins associated with exon-exon junctions regardless of the nature of the photoreactive group, the position of this group relative to the exon-exon junction, or the exact sequence of the 5' exon, even though changing the position or the nature of the photoreactive group can affect exactly which proteins are detected by this method.";"";"At the time of annotation, the additional members p50 and p20 of the protein complex remained unidentified. "
1196;RAD51C-XRCC3 complex;;Human;O43502,O43542;5889,7517;MI:0004- affinity chromatography technologies | MI:0018- two hybrid;11331762;10.01.05.01,10.01.05.03,16.03.01,16.19.03,32.01.09,70.10,77.03.01.01.01;"Rad51C protein alone catalyzes homologous pairing, suggesting that Rad51C is the catalytic subunit of the complex. The DNA-binding activity of Rad51C-Xrcc3 complex drastically decreases in the absence of Xrcc3, indicating that Xrcc3 is important for the DNA binding activity of the complex.";"";""
1197;TRF1-TIN2 complex;;Human;Q96AP0,Q9NUX5,P54274,Q15554,Q9NYB0,Q9BSI4;65057,25913,7013,7014,54386,26277;MI:0007- anti tag coimmunoprecipitation;15181449;16.03.01,42.10.03,70.10;"PTOP binds to the carboxyl terminus of POT1 and recruits it to telomeres.";"";""
1198;TIN2 complex;;Human;Q96AP0,Q9NUX5,Q15554,Q9BSI4;65057,25913,7014,26277;MI:0226- ion exchange chromatography | MI:0071- molecular sieving;15181449;16.03.01,42.10.03,70.10;"This complex regulates telomere length. PTOP binds to the carboxyl terminus of POT1 and recruits it to telomeres.";"";""
1199;Oligosaccharyltransferase complex (Stt3A variant); OST complex;Human;P61803,P39656,Q9H0U3,P04843,P04844,P46977;1603,1650,84061,6184,6185,3703;MI:0028- cosedimentation in solution | MI:0226- ion exchange chromatography;12887896;14.07.02.02,70.07;"Oligosaccharyltransferase (OST) is an integral membrane protein that catalyzes N-linked glycosylation of nascent proteins in the lumen of the endoplasmic reticulum. Genomes of most multicellular eukaryotes encode two homologs of Stt3p and mammals express two homologs of Ost3p. Tissue and cell type-specific differences in expression of the Stt3p homologs suggest that the enzymatic properties of oligosaccharyltransferase are regulated in eukaryotes to respond to alterations in glycoprotein flux through the secretory pathway and may contribute to tissue-specific glycan heterogeneity.  Iag2 appears to be weakly associated with the OST complex and dissociates from the other subunits at various stages during enzyme purification.";"";""
1200;Oligosaccharyltransferase complex (Stt3B variant);OST complex;Human;P61803,P39656,Q9H0U3,P04843,P04844,Q8TCJ2,Q13454;1603,1650,84061,6184,6185,201595,7991;MI:0028- cosedimentation in solution | MI:0226- ion exchange chromatography;12887896;14.07.02.02,70.07;"Oligosaccharyltransferase (OST) is an integral membrane protein that catalyzes N-linked glycosylation of nascent proteins in the lumen of the endoplasmic reticulum. Genomes of most multicellular eukaryotes encode two homologs of Stt3p and mammals express two homologs of Ost3p. Tissue and cell type-specific differences in expression of the Stt3p homologs suggest that the enzymatic properties of oligosaccharyltransferase are regulated in eukaryotes to respond to alterations in glycoprotein flux through the secretory pathway and may contribute to tissue-specific glycan heterogeneity.  Tusc3 and Iag2 appear to be weakly associated with the OST complex and dissociate from the other subunits at various stages during enzyme purification.";"";""
1201;TRF1-TIN2 complex;;Human;Q96AP0,Q9NUX5,P54274,Q9BSI4;65057,25913,7013,26277;MI:0007- anti tag coimmunoprecipitation;15231715;16.03.01,42.10.03,70.10;"This complex regulates telomere length.";"";""
1202;TRF1 telomere length regulation complex;;Human;P54274,Q9BSI4,O95271;7013,26277,8658;MI:0006- anti bait coimmunoprecipitation;15133513;42.10.03,70.10;"Inhibition of TRF1 by tankyrase 1 is controlled by TIN2.";"";""
1203;Oligosaccharyltransferase OSTC-I;;Dog;P61803,Q9NRP0,Q05052,Q8N6L1,P04843,P04844,P46977;1603,58505,404012,200185,6184,6185,3703;MI:0069- mass spectrometry studies of complexes | MI:0028- cosedimentation in solution | MI:0276- blue native page;15835887;14.07.02.02,70.07;"Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen. ";"";"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1204;Rap1 complex;;Human;Q96AP0,Q9NUX5,Q92878,P54274,Q15554,Q9NYB0,Q9BSI4;65057,25913,10111,7013,7014,54386,26277;MI:0007- anti tag coimmunoprecipitation;15316005;16.03.01,42.10.03,70.10;"TIN2 was found to bind TRF1 and TRF2 simultaneously, showing that TIN2 can link these telomeric proteins. This connection appeared to stabilize TRF2 on the telomeres as the treatment of cells with TIN2 small interfering RNA resulted in a decreased presence of TRF2 and hRap1 at chromosome ends. Only 5-10% of the endogenous TRF1 could be recovered in association with the hRap1 complex.";"";""
1205;TRF2-Rap1 complex III;;Human;Q15554,Q9NYB0;7014,54386;MI:0071- molecular sieving;15316005;16.03.01,42.10.03,70.10;"The TRF2 complex is primarily involved in telomere protection and contains the TRF2 interacting partner human (h)Rap1 as well as several factors involved in the DNA damage response.";"";""
1206;TRF-Rap1 complex I, 2MD;;Human;Q9NUX5,P54274,Q15554,Q9NYB0,Q9BSI4,O95271;25913,7013,7014,54386,26277,8658;MI:0071- molecular sieving;15316005;16.03.01,42.10.03,70.10;"";"";""
1207;TRF2-Rap1 complex II;;Human;Q9NUX5,Q15554,Q9NYB0,Q9BSI4;25913,7014,54386,26277;MI:0071- molecular sieving;15316005;16.03.01,42.10.03,70.10;"";"";""
1208;Oligosaccharyltransferase OSTC-II;;Dog;P61803,Q9NRP0,Q05052,Q8N6L1,P04843,P04844,P38377,P60467,P60058,P46977;1603,58505,404012,200185,6184,6185,404006,404018,404017,3703;MI:0069- mass spectrometry studies of complexes | MI:0028- cosedimentation in solution | MI:0276- blue native page;15835887;14.07.02.02,70.07;"Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen. ";"";"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1209;Oligosaccharyltransferase OSTC-III;;Dog;P61803,Q9NRP0,Q05052,Q8N6L1,P04843,P04844,P38377,P60467,P16967,Q9UNL2,P46977;1603,58505,404012,200185,6184,6185,404006,404018,403951,6747,3703;MI:0069- mass spectrometry studies of complexes | MI:0028- cosedimentation in solution | MI:0276- blue native page;15835887;14.07.02.02,70.07;"Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen. ";"";"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1210;Sec61-Sec62-Sec63 complex;;Bovine;P60468,Q3T104,Q99442,Q9UGP8,(Q5EA68,Q2KHX4);10952,615778,7095,11231,(505064,614128);MI:0019- coimmunoprecipitation;10799540;20.01.10,20.03.01,20.09.05,70.07;"The Sec61-Sec62-Sec63 complex plays a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. The complex is thightly associated with membrane-bound ribosomes, either directly or through adapter proteins. ";"";"Since bovine SEC61B,TLOC1 and  SEC63 were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1211;Ubiquitin E3 ligase (AHR, ARNT, DDB1, TBL3, CUL4B, RBX1); CUL4AhR complex;Human;P35869,P27540,Q13620,Q16531,P62877,Q12788;196,405,8450,1642,9978,10607;MI:0007- anti tag coimmunoprecipitation;17392787;14.07.05,14.13.01.01,30.07,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. In the CUL4B(AhR) ubiquitin E3 ligase complex, ligand-activated dioxin receptor AhR acts as a substrate-specific adaptor component that targets sex steroid receptors for degradation. Thus, experiments uncover a function for AhR as an atypical component of the ubiquitin ligase complex and demonstrate a non-genomic signalling pathway in which fat-soluble ligands regulate target-protein-selective degradation through a ubiquitin ligase complex.";"";""
1212;SNARE complex (Stx4, Vamp8, Snap23);;Mouse;O09044,P70452,O70404;20619,20909,22320;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;15363411;20.09.07.27,20.09.16.09.05,77.03.11.07,77.03.11.09;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. VAMP8/endobrevin  is a major player in regulated exocytosis of the exocrine pancreas (pancreatic acinar cells). It is enriched on the membrane of zymogen granules.";"";""
1213;SNARE complex (Stx4, Vamp2, Snap23);;Mouse;O09044,P70452,P63044;20619,20909,22318;MI:0004- affinity chromatography technologies;15363411;20.09.07.27,20.09.16.09.05,77.03.11.09;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1214;Ubiquitin E3 ligase (DET1, DDB1, CUL4A, RBX1, COP1);DCXhDET1-hCOP1 complex;Human;Q13619,Q16531,Q7L5Y6,P62877,Q8NHY2;8451,1642,55070,9978,64326;MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;14739464;14.07.05,14.13.01.01,30.07,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Human DET1 (hDET1) promotes ubiquitination and degradation of the proto-oncogenic transcription factor c-Jun by assembling a multisubunit ubiquitin E3 ligase. Ablation of any subunit by RNA interference stabilized c-Jun and increased c-Jun-activated transcription.";"";""
1215;Ubiquitin E3 ligase (FBXW7, CUL1, SKP1A, RBX1);;Human;Q13616,Q969H0,P62877,P63208;8454,55294,9978,6500;MI:0019- coimmunoprecipitation;11585921;14.07.05,14.13.01.01,30.05.02.14,30.07;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. FBXW7 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation.";"";""
1216;Hspb2-Hspb3 complex;;Rat;O35878,Q9QZ58;161476,78951;MI:0071- molecular sieving | MI:0019- coimmunoprecipitation;10625651;16.01;"";"";""
1217;WRN-TRF2 complex;;Human;Q15554,Q14191;7014,7486;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;12181313;10.01.02,40.20,42.10.03;"TRF2 interaction with WRN results in a stimulation of WRN-helicase activity.";"";""
1218;BLM-TRF2 complex;;Human;P54132,Q15554;641,7014;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;12768206;10.01.02,40.20,42.10.03;"";"BLM is involved in Bloom syndrome (BS) (PMID:12444098).";""
1219;Tankyrin 1-tankyrin 2-TRF1 complex;;Human;P54274,O95271,Q9H2K2;7013,8658,80351;MI:0004- affinity chromatography technologies;12080061;42.10.03,70.10;"TRF1 binding allows tankyrase to regulate telomere dynamics. Mouse TRF1 lacks the binding motif for tankyrase.";"";""
1220;TRF2-Ku complex;;Human;Q15554,P13010,P12956;7014,7520,2547;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;10984620;16.03.01,42.10.03,70.10;"";"";""
1221;TFIIA-TRF2 complex;;Human;P52655,P52657,Q15554;2957,2958,7014;MI:0007- anti tag coimmunoprecipitation;10570139;11.02.03.04,70.10;"TRF2-TFIIA complex is able to replace TBP or TFIID in basal or activated transcription from various RNA polymerase II promoters.";"";""
1222;Irs1-Grb2-Ptpn1 complex;;Rat;P62994,P35570,P20417;81504,25467,24697;MI:0019- coimmunoprecipitation;10660596;14.07.03,30.05.01.12.05;"The authors suggest that PTP1B and GRB2 may influence the steady-state capacity of IRS-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling.";"";""
1223;H2AX complex, isolated from cells without IR exposure;;Human;P62158,P27797,Q9Y262,P16104,P62805,Q8N257,O43390,P11021,P06748,P11940,P05455,Q08945,Q9Y5B9;805,811,51386,3014,554313,128312,10236,3309,4869,26986,6741,6749,11198;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes;16522924;10.01.09.05,10.03.01.03,11.02.03.01.04,42.10.03,70.10;"";"";""
1224;Ubiquitin E3 ligase (BMI1, SPOP, CUL3);;Human;P35226,Q13618,O43791;648,8452,8405;MI:0019- coimmunoprecipitation;15897469;10.03.04.06,14.07.05,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. X inactivation involves the stable silencing of one of the two X chromosomes in XX female mammals. Initiation of this process occurs during early development and involves Xist (X-inactive-specific transcript) RNA coating and the recruitment of Polycomb repressive complex (PRC) 2 and PRC1 proteins. This recruitment results in an inactive state that is initially labile but is further locked in by epigenetic marks such as DNA methylation, histone hypoacetylation, and MACROH2A deposition. The ubiquitin E3 ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone H2AFY.";"";""
1225;Ubiquitin E3 ligase (H2AFY, SPOP, CUL3);;Human;Q13618,O75367,O43791;8452,9555,8405;MI:0019- coimmunoprecipitation;15897469;10.03.04.06,14.07.05,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. X inactivation involves the stable silencing of one of the two X chromosomes in XX female mammals. Initiation of this process occurs during early development and involves Xist (X-inactive-specific transcript) RNA coating and the recruitment of Polycomb repressive complex (PRC) 2 and PRC1 proteins. This recruitment results in an inactive state that is initially labile but is further locked in by epigenetic marks such as DNA methylation, histone hypoacetylation, and MACROH2A deposition. The ubiquitin E3 ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone H2AFY.";"";""
1226;H2AX complex I;;Human;P27797,Q7L2E3,P16104,Q8N257,P11021,P06748,P09874;811,22907,3014,128312,3309,4869,142;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes;16522924;10.01.05.01,10.01.09.05,10.03.01.03,11.02.03.01.04,32.01.09,42.10.03,70.10;"This complex has been isolated from cells after IR exposure and recovery for 30 minutes.";"";""
1227;H2AX complex II;;Human;P27797,P16989,P16104,P33778,Q99879,P62805,Q8N257,P11021,P06748,Q96EY7;811,8531,3014,3018,8342,554313,128312,3309,4869,55037;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes;16522924;10.01.05.01,10.01.09.05,10.03.01.03,11.02.03.01.04,32.01.09,42.10.03,70.10;"This complex has been isolated from cells after IR exposure and recovery for 2.5h.";"";""
1228;Epsin-clathrin complex;;Rat;O08838,P18484,P84092,O88339,Q05140;60668,81637,116563,117277,65178;MI:0096- pull down;10692452;20.09.18.09.01,70.03,77.03.01.01.01;"AP-2, clathrin, amphiphysin, eps15, and beta -arrestin, epsin form a multivalent protein network that probably influences the endocytic process.";"";""
1229;RACK1-containing mRNP complex;;Rat;P63245,Q9EPH8,Q6AY21,Q9JIR1;83427,171350,305240,266780;MI:0006- anti bait coimmunoprecipitation;12388589;12.07,16.03.03,34.03.01,70.02,77.03.01.01.01;"";"";""
1230;WINAC complex; WSTF containing complex;Human;O96019,O14497,Q9UIG0,Q13111,P51531,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3,Q9Y5B9,Q02880,P11473;86,8289,9031,10036,6595,6597,6598,6599,6601,6602,6605,11198,7155,7421;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;12837248;10.01.03,10.01.09.05,10.03.01.01.05,11.02.03.04,16.01.01,42.10.03,70.10;"WINAC mediates the recruitment of unliganded VDR to VDR target sites in promoters, while subsequent binding of coregulators requires ligand binding.";"";""
1231;FIB-associated protein complex;;Human;Q07021,P22087,Q99873,O14744,Q71U36,Q9H4B7;708,2091,3276,10419,7846,81027;MI:0007- anti tag coimmunoprecipitation;14583623;11.04.01,11.06.01,12.01,70.10,77.03.07.01;"FIB-associated protein complexes contain a number of ribosomal proteins and potential trans-acting factors involved in ribosome biogenesis, and the complexes are dependent on RNA integrity.";"";""
1232;REST-CoREST-mSIN3A complex;;Human;Q9UKL0,Q13127,Q96ST3;23186,5978,25942;MI:0007- anti tag coimmunoprecipitation;10734093;11.02.03.04.03,41.05.13,43.03.13,45.03.17,70.10,73.03.13;"The REST-mSin3A association involves the NH(2)-terminal repressor domain of REST and the paired amphipathic helix 2 domain of mSin3A. REST forms complexes with endogenous mSin3A in mammalian cells, and both mSin3A and CoREST interact with REST in intact mammalian cells.";"";""
1233;CoREST-HDAC2 complex;;Human;Q92769,Q9UKL0;3066,23186;MI:0019- coimmunoprecipitation;11516394;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10,73.03.13;"In the presence of REST, the CoREST/HDAC2 complex represses transcription of the Nav1.2 sodium channel gene.";"";""
1235;SNARE complex (Vamp2, Snap25, Stx1a, Syt1, Cplx1);;Rat;P63041,P60881,P32851,P21707,P63045;64832,25012,116470,25716,24803;MI:0029- cosedimentation through density gradients;10051208;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1236;SNARE complex (Vamp2, Snap25, Stx1a, Syt1, Cplx2);;Rat;P84087,P60881,P32851,P21707,P63045;116657,25012,116470,25716,24803;MI:0029- cosedimentation through density gradients;10051208;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1237;BAF complex; SWI/SNF complex A;Human;O96019,O14497,P51531,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3;86,8289,6595,6597,6598,6599,6601,6602,6605;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;11073988;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10;"BAF250 confers specificity to the human BAF complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions.";"";"Another subunit of the complex was found in the analysis, which has not been further characterized: BAF110."
1238;PBAF complex (Polybromo- and BAF containing complex); SWI/SNF-B complex;Human;O96019,Q68CP9,Q86U86,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3;86,196528,55193,6597,6598,6599,6601,6602,6605;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;11780067;10.01.09.05,11.02.03.04.01,16.03.01,30.01.09.08,30.01.11,42.10.03,70.10.03;"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome. ";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: BAF110 and BAF240."
1239;EBAFb complex; ENL-associated BAF250b-containing SWI/SNF complex;Human;O96019,Q8NFD5,Q03111,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q969G3;86,57492,4298,6597,6598,6599,6601,6602,6603,6605;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;12665591;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10.03,73.03.07.02.01.02;"ENL associates and cooperates with SWI/SNF complexes to activate transcription of the promoter of HoxA7, a downstream target essential for oncogenic activity of ENL.";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized: EBAF140, EBAF100 and EBAF70."
1240;SC5bp-7 complex;;Rabbit;P06684,Q9QXT7,P10643,P48747,P22458,(P98136,P98137);15139,12274,730,100009197,100009128,(100009076,100009385);MI:0004- affinity chromatography technologies | MI:0004- affinity chromatography technologies;410885;;"";"";"Since C5, C6 and C7 from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from human and mouse were used."
1241;Esr1-Pit1 complex;;Rat;P06211,P10037;24890,25517;MI:0019- coimmunoprecipitation;10809776;11.02.03.04,47.03.21.03.05,77.03.21.03.05;"The authors report that estrogen may regulate the interaction between Pit-1 and ER-alpha  proteins through diverse pathways depending on the pituitary cell types. The results also indicate that accessory factor(s) are involved in the synergistic interaction between Pit-1 and ER-alpha  proteins and that synthesis of these factors is likely to be estrogen-induced.";"";""
1243;Ubiquitin E3 ligase (SPOP, DAXX, CUL3);;Human;Q13618,Q9UER7,O43791;8452,1616,8405;MI:0007- anti tag coimmunoprecipitation;16524876;11.02.03.04,14.07.05,14.13.01.01,40.10.02.04,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. SPOP serves as an adaptor of Daxx for the ubiquitination by Cul3-based ubiquitin ligase and subsequent degradation by the proteasome. Experiments suggest that SPOP/Cul3-ubiquitin ligase plays an essential role in the control of Daxx level and, thus, in the regulation of Daxx-mediated cellular processes, including transcriptional regulation and apoptosis.";"";""
1244;SNARE complex (STX1A, STX1B, SNAP25, RAB3A, SYT1, VAMP2); Docking/fusion complex;Bovine;Q9TRF1,P11023,P32850,P61267,P48018,P63026;540853,282029,788566,282377,281511,282116;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;7654227;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. VAMP/synaptobrevin-2 exists exclusively on the synaptic vesicle membrane and serves as a v-SNARE, while syntaxins 1A and 1 B are mostly on the presynaptic plasma membrane and thus t-SNAREs. The SNARE hypothesis proposes that fusion in membrane transport occurs by combination between a SNARE in the transport vesicle (v-SNARE) and a SNARE in the target membrane (t-SNARE).";"";""
1245;Protein phosphatase 4 complex;PPP4 |PPP4c;Human;P60510,Q9NY27;5531,151987;MI:0028- cosedimentation in solution;10769191;14.07.03,70.05;"Protein phosphatase 4 (PPP4) is a protein serine/threonine phosphatase that has been implicated in microtubule organization at centrosomes.";"";""
1246;ERdj3-BiP complex;;Mouse;Q99KV1,P20029;67838,14828;MI:0007- anti tag coimmunoprecipitation;15525676;14.01,32.01.07,70.07;"ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for interactions of the chaperone BiP with unfolded substrates.";"";""
1247;SNARE complex (STX1a, STX1b, SNAP25, RAB3a, SYT1, VAMP2, CPLX2);;Bovine;Q9TRF1,P84088,P11023,P32850,P61267,P48018,P63026;540853,281711,282029,788566,282377,281511,282116;MI:0019- coimmunoprecipitation;7654227;18.01.07,20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. Synaphin (19a component) constantly copurifies with the docking/fusion complex irrespective of detergent. It seems to regulate the efficiency of the docking/fusion complex.";"";""
1248;Apoptosome;;Human;O14727,P99999;317,54205;MI:0114- x-ray crystallography;16271896;40.10.02.03,70.03;"The apoptosome is a multiprotein complex mediating the mitochondrial pathway of cell death. Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. In the absence of an apoptotic signal, Apaf-1 exists in a monomeric form.";"";""
1250;pRB-E2F-1 complex;;Human;Q01094,P06400;1869,5925;MI:0019- coimmunoprecipitation;17380128;10.03.01.02,32.01.09,70.10;"The phosphorylation of pRB at Ser612 is induced by ATM-Chk1/2 kinase after DNA damage, leading to enhancement of the formation of a complex between pRB and E2F-1. It is proposed, that in asynchronously growing cells, pRB exists in a predominantly phosphorylated state, which is dissociated from E2F, allowing E2F-dependent transcription. DNA damage induces dephosphorylation of pRB at Cdk phosphorylation sites, leading to the complex pRB-E2F-1 being formed. DNA damage also activates ATM kinase and transduces signals to the checkpoint kinases Chk1 and Chk2. Activated Chk1 and Chk2 phosphorylate Ser612 of pRB and this phosphorylation enhances the formation of a complex between pRB and E2F-1, leading to repression of the transcriptional activity of E2F-1. Consequently, pRB-dependent cell cycle arrest and repression of apoptosis occur.";"";""
1251;BAF complex; SWI/SNF-A complex;Human;O96019,O14497,Q12824,Q92922,Q8TAQ2,Q96GM5,Q969G3,(P51531,P51532);86,8289,6598,6599,6601,6602,6605,(6595,6597);MI:0071- molecular sieving;12665591;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10.03;"BAF complex belongs to chromatin remodeling complexes.";"";""
1252;EBAFa complex; ENL-associated BAF250a-containing SWI/SNF complex;Human;O96019,O14497,Q03111,P51532,Q12824,Q92922,Q8TAQ2,Q96GM5,Q92925,Q969G3;86,8289,4298,6597,6598,6599,6601,6602,6603,6605;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;12665591;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10.03,73.03.07.02.01.02;"ENL associates and cooperates with SWI/SNF complexes to activate transcription of the promoter of HoxA7, a downstream target essential for oncogenic activity of ENL.";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized: EBAF140, EBAF100 and EBAF70."
1253;Ubiquitin E3 ligase (FBXW7, CUL1, SKP1A, RBX1);;Human;Q13616,Q969H0,P62877,P63208;8454,55294,9978,6500;MI:0019- coimmunoprecipitation;11565034;14.07.05,14.13.01.01,30.05.02.14,30.07;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. FBXW7 targets cyclin E, one of the activators of the cyclin-dependent kinase Cdk2 for proteolysis and is mutated in a breast cancer cell line.";"";""
1254;Menin-associated histone methyltransferase complex; menin HMTase complex;Human;Q9UBL3,Q9C005,O00255,P30876,Q15291,Q9UMN6,P61964;9070,84661,4221,5431,5929,9757,11091;MI:0006- anti bait coimmunoprecipitation | MI:0029- cosedimentation through density gradients;14992727;10.01.09.05,10.01.09.07,11.02.03.04.01,14.07.09,42.10.03,43.03,70.10;"The menin-associated complex methylates histone H3 on lysine 4, suggesting menin activates the transcription of differentiation-regulating genes by covalent histone modification, and that this activity is related to tumor suppression by MEN1. ";"MEN1 gene is mutated in familial multiple endocrine neoplasia type 1.";""
1255;Ubiquitin E3 ligase (SIAH1, SIP, SKP1A, TBL1X);;Human;Q9HB71,Q8IUQ4,P63208,O60907;27101,6477,6500,6907;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;11389839;14.07.05,14.13.01.01,30.07;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Conditional degradation of beta-catenin represents a central event in the Wnt signaling pathways controlling cell fate and proliferation. A network of protein interactions in which Siah, SIP (a novel Siah-interacting protein), Skp1, and Ebi collaborate in a pathway controlling beta-catenin levels, affecting activity of beta-catenin-dependent Tcf/LEF transcription factors.";"";""
1256;MLL-HCF complex;;Human;Q9UBL3,P51610,O00255,Q03164,Q15291,P05546,P61964;9070,3054,4221,4297,5929,3053,11091;MI:0226- ion exchange chromatography | MI:0006- anti bait coimmunoprecipitation;15199122;10.01.09.05,10.01.09.07,11.02.03.04,14.07.09,42.10.03,70.10;"This complex links the menin tumor suppressor protein to the MLL histone methyltransferase machinery.";"";""
1257;ALL-1 supercomplex;;Human;O60341,Q12873,Q9P2I0,Q15029,Q13547,Q92769,O95983,Q03164,O94776,P62826,Q09028,Q15291,Q16576,O00422,O75446,Q96ST3,P51531,O60264,Q12824,Q92922,Q8TAQ2,Q92797,P21675,Q16514,P49848,Q16594,P20226,P61964;23028,1107,53981,9343,3065,3066,53615,4297,9219,5901,5928,5929,5931,10284,8819,25942,6595,8467,6598,6599,6601,8189,6872,6883,6878,6880,6908,11091;MI:0004- affinity chromatography technologies | MI:0071- molecular sieving;12453419;10.01.09.05,11.02.03.04,14.07.04,14.07.09,42.10.03,70.10;"The proteins associated with ALL-1 can be classified into eight groups.  (1) BRM, BAF170, BAF155, and INI1, the core components of the ATP-dependent SWI/SNF nucleosome remodeling complex,  (2) Mi2, MTA1-L1, HDAC1, HDAC2, RbAp46, RbAp48, MBD3, and KIAA0601, all components of the NuRD complex,  (3) Sin3A, SAP30, SAP18, HDAC1, HDAC2, RbAp48, and RbAp46, components of the histone deacetylase Sin3A complex,  (4) hSNF2H, homolog of ISWI, an ATP-dependent nucleosome remodeling and assembly factor,  (5) TAFII250, TAFII80, TAFII31, TAFII20, and TBP, components of the TFIID complex,  (6) RbBP5  and WDRP5, components of the yeast Set1 complex,  which methylates H3-K4.  (7) Proteins involved in RNA processing, CPSF, Symplekin and EFTUD2.  (8) Ran, which functions in nucleocytoplasmic transport and in spindle assembly during mitosis.";"";""
1258;Ubiquitin E3 ligase (GLMN, FBXW8, SKP1A, RBX1);;Human;Q8N3Y1,Q92990,P62877,P63208;26259,11146,9978,6500;MI:0019- coimmunoprecipitation;12904573;14.07.05,14.13.01.01,47.03.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Experiments suggest that ubiquitin E3 ligase (containing GLMN, FBXW8, SKP1A and RBX1) plays an important role in vascular morphogenesis.";"";""
1259;Chromatin assembly complex (CAF-1 complex);;Human;Q13111,Q13112,Q09028;10036,8208,5928;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;7600578;10.01.03,10.01.09.05,10.03.01.01.05,42.10.03,70.10;"Caf-1 complex assembles nucleosomes in a replication-dependent manner.";"";""
1260;Neddylin ligase (FBXO11, SKP1, CUL1, RBX1);;Human;Q13616,Q86XK2,P62877,P63208;8454,80204,9978,6500;MI:0007- anti tag coimmunoprecipitation;17098746;14.07.07,18.01.01,18.02.09,70.10;"FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity.";"";""
1261;SRm160/300 complex;;Human;P08621,P09661,Q8IYB3,Q9UQ35,P62995;6625,6627,10250,23524,6434;MI:0019- coimmunoprecipitation;10339552;11.04.03.01,16.03.03,70.10;"Exonic splicing enhancer (ESE) sequences are important for the recognition of splice sites in pre-mRNA. These sequences are bound by specific serine-arginine (SR) repeat proteins that promote the assembly of splicing complexes at adjacent splice sites. In a study, it was shown that SRm160/300 is required for a purine-rich ESE to promote the splicing of a pre-mRNA derived from the Drosophila doublesex gene. Results suggest a model for ESE function in which the SRm160/300 splicing coactivator promotes critical interactions between ESE-bound "activators" and the snRNP machinery of the spliceosome.";"";""
1287;HNRPF-HNRPH1 complex;;Human;P52597,P31943;3185,3187;MI:0019- coimmunoprecipitation;9858532;11.04.03.01,16.03.03,70.10;"The complex is involved in alternative splicing.";"";""
1288;DCS complex (PTBP1, PTBP2, HNRPH1, HNRPF);;Human;P52597,P31943,P26599,Q9UKA9;3185,3187,5725,58155;MI:0226- ion exchange chromatography | MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;11003644;11.04.03.01.10,16.03.03,70.10;"";"";""
1293;IPO13-RBM8A-MAGOH complex;;Human;O94829,P61326,Q9Y5S9;9670,4116,9939;MI:0004- affinity chromatography technologies;11447110;20.01.21,20.09.01,70.10;"";"";""
1296;DCP1A-DCP2 Decapping complex;;Human;Q9NPI6,Q8IU60;55802,167227;MI:0019- coimmunoprecipitation;12417715;01.03.16.01,70.03;"Although the authors suggest the existence of a protein complex containing DCP proteins and UPF proteins they also state that there is currently no direct evidence for the significance of a strong interaction between hUpf1 and hDcp proteins.";"";""
1297;MKK4-ARRB2-ASK1 complex;;Human;P32121,P45985,Q99683;409,6416,4217;MI:0019- coimmunoprecipitation;11090355;30.01.05.01.02,30.01.05.01.03;"The data suggest that ASK1 binds directly to beta -arrestin 2, and MKK4 interacts indirectly with beta -arrestin 2 via ASK1 or JNK3, thus forming a complete MAPK module.";"";""
1298;MKK4-ARRB2-JNK3 complex;;Human;P32121,P45985,P53779;409,6416,5602;MI:0019- coimmunoprecipitation;11090355;30.01.05.01.02,30.01.05.01.03;"The data suggest that ASK1 binds directly to beta -arrestin 2, and MKK4 interacts indirectly with beta -arrestin 2 via ASK1 or JNK3, thus forming a complete MAPK module.";"";""
1299;POSH-MLK3 complex;;Human;Q16584,Q7Z6J0;4296,57630;MI:0019- coimmunoprecipitation;14504284;30.01.05.01.02;"A POSH mutant unable to bind to Akt2 exhibits increased binding to MLK3. This increased binding of MLK3 to POSH is accompanied by increased activation of the JNK signaling pathway.";"";""
1300;CRLR-RAMP1 complex;;Human;Q16602,O60894;10203,10267;MI:0019- coimmunoprecipitation;11387328;30.05.02.24,70.02;"The results demonstrate that RAMP2 and RAMP3 and not only RAMP1 can promote the full maturation of CRLR, leading to its terminal glycosylation, and only the fully processed receptors were found to bind AM (adrenomedullin) and CGRP (calcitonin gene-related peptide).";"";""
1301;CRLR-RAMP1 complex;;Human;Q16602,O60894;10203,10267;MI:0019- coimmunoprecipitation | MI:0054- fluorescence-activated cell sorting;11535606;30.05.02.24,70.02;"When RAMP1 is expressed with CRLR, it is targeted to the cell surface as a heterodimer. CGRP (calcitonin gene-related peptide) binding and receptor activation lead to the phosphorylation of CRLR and the internalization of the receptor as a stable complex.";"";""
1306;PIN1-AUF1 complex;;Human;Q14103,Q13526;3184,5300;MI:0019- coimmunoprecipitation;16273101;40.02.03.01,70.03;"Immunoprecipitation of eosinophil cytoplasmic lysates demonstrated an interaction between Pin1 and all four AUF1 isoforms. Pin1 regulated the association of the AU-rich element–binding proteins AUF1 and hnRNP C with GM-CSF mRNA, accelerating or slowing decay, respectively. The authors propose that moderately serine-phosphorylated p40 and p45 AUF1, in physical association with serine-phosphorylated Pin1 and unphosphorylated p42 and p37 AUF1, form a ribonucleoprotein complex with GM-CSF mRNA in resting eosinophils.";"";""
1307;Multiprotein complex (mRNA turnover);;Human;O75534,Q14103,P11940,Q9H074,O60506;7812,3184,26986,10605,10492;MI:0029- cosedimentation through density gradients | MI:0047- far western blotting;11051545;01.03.16.01,70.03;"";"";""
1308;PABPC1-HSPA8-HNRPD-EIF4G1 complex;;Human;Q59EJ3,Q04637,Q14103,P11142,P11940;3303,1981,3184,3312,26986;MI:0019- coimmunoprecipitation;10205060;01.03.16.01;"Cytokine and proto-oncogene messenger RNAs (mRNAs) are rapidly degraded through AU-rich elements in the 39 untranslated region. Rapid decay involves AU-rich binding protein AUF1, which complexes with heat shock proteins hsc70-hsp70, translation initiation factor eIF4G, and poly(A) binding protein.";"";""
1310;Rab27a-Mlph-Myo5a complex;;Mouse;Q91V27,Q99104,Q9ERI2;171531,17918,11891;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;11980908;20.01.10;"The melanophilin interacts with Rab27a and myosin Va on melanosomes in melanocytes. The melanophilin can associate simultaneously with activated Rab27a and myosin Va via distinct regions, and serve as a linker between these proteins (PMID:11980908).";"";""
1318;Transcription initiation factor complex (TAF1, TAF5, TAF11, TAF12, TBP);;Human;P21675,Q15544,Q16514,Q15542,P20226;6872,6882,6883,6877,6908;MI:0019- coimmunoprecipitation;9045704;11.02.03.01.01;"Human transcription initiation factor TFIID contains the TATA-binding protein (TBP) and several TBP-associated factors (TAFs). The authors suggest that hTAFII100 may help stabilize interactions of the histonelike TAFs, perhaps within an octamer structure.";"";""
5703;Bash-Bnas2/Cmtm3-Btk-Erk2 complex;;Mouse;Q9QUN3,P35991,Q99LJ5,P63085;17060,12229,68119,26413;MI:0019- coimmunoprecipitation;15087455;30.05;"";"";""
1321;Transcription initiation factor complex (TAF5, TAF6, TAF9, TAF11, TBP);;Human;Q15544,Q15542,P49848,Q16594,P20226;6882,6877,6878,6880,6908;MI:0019- coimmunoprecipitation;9045704;11.02.03.01.01;"Human transcription initiation factor TFIID contains the TATA-binding protein (TBP) and several TBP-associated factors (TAFs). The authors suggest that hTAFII100 may help stabilize interactions of the histonelike TAFs, perhaps within an octamer structure.";"";""
1332;Large Drosha complex;;Human;Q92499,Q92841,O00571,P17844,Q8WYQ5,O43143,Q01844,P35637,P31943,P52272,Q00839,Q9BUJ2,O14979,Q12905,Q12906,Q9UKM9,Q9NRR4,Q96SB4,Q92804,Q13148;1653,10521,1654,1655,54487,1665,2130,2521,3187,4670,3192,11100,9987,3608,3609,22913,29102,6732,8148,23435;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving;15531877;11.04,16.03.03,70.10;"The large Drosha complex shows only weak pri-miRNA processing activity. It might be involved in pri-ribosomal RNA processing. ";"DGCR8 is deleted in DiGeorge syndrome. EWS is involved in Ewing's sarcoma disease.";""
1335;SNW1 complex;;Human;Q9UG63,Q99459,Q16531,Q9BUQ8,P68104,P26641,Q15029,Q00839,P11021,P43243,P43246,P17858,Q6P2Q9,P23246,O75643,Q13573,P07437,O95071;10061,988,1642,9416,1915,1937,9343,3192,3309,9782,4436,5211,10594,6421,23020,22938,203068,51366;MI:0007- anti tag coimmunoprecipitation;12840015;11.02.03.04.01,11.04.03.01,70.10;"Identified subunits of the SNW1 complex represent components of the spliceosome as well as other nuclear matrix-associated proteins. Evidence was found that the complex couples vitamin D receptor-mediated transcription and RNA splicing.";"";""
1338;FOXO3-PCAF complex, oxidative stress stimulated;;Human;O43524,Q92831;2309,8850;MI:0007- anti tag coimmunoprecipitation;14976264;11.02.03.04,32.01.01,70.10;"";"";""
1345;Septin complex;;Human;Q9NVA2,Q15019,Q16181,Q92599,Q9UHD8;55752,4735,989,23176,10801;MI:0047- far western blotting;15485874;10.03.05,43.01.03.05;"Septins are members of a conserved family of cytoskeletal GTPases, filament-forming and cell division cycle regulatory proteins.";"";""
1347;NPC subcomplex (NUP98, NUP107, NUP133, NUP160);;Human;P57740,Q8WUM0,Q12769,P52948;57122,55746,23279,4928;MI:0019- coimmunoprecipitation;11564755;10.03.01.01,20.01.10,20.03.01.05,20.09.01,70.10.04;"All trafficking of macromolecules between the cytoplasm and the nucleus occurs through nuclear pore complexes (NPCs), which are supramolecular assemblies at points of fusion between the inner and outer nuclear membranes. NPCs are composed of an eightfold symmetric spoke-ring complex, cytoplasmic fibers, and a nuclear basket. NUP133 and NUP107 are localized on both sides of the NPC to which they are stably associated at interphase and remain associated as part of a NPC subcomplex during mitosis. They are targeted at early stages to the reforming nuclear envelope.";"";""
1348;GLE1-NUPL2-NUP155 complex;;Human;Q53GS7,O75694,O15504;2733,9631,11097;MI:0004- affinity chromatography technologies;16000379;14.04;"";"";""
1352;ING4 complex (ING4, MYST2, C1orf149, PHF17);;Human;Q9HAF1,Q9UNL4,O95251,Q6IE81;64769,51147,11143,79960;MI:0069- mass spectrometry studies of complexes | MI:0004- affinity chromatography technologies;16387653;10.03.01,41.05.16;"ING4 associates with the HBO1 HAT required for normal progression through S phase and the majority of histone H4 acetylation in vivo. ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
1371;Gata1-Tal1-Tcf3-Lmo2 complex;;Mouse;P17679,P25801,P22091,P15806;14460,16909,21349,21423;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;7568177;11.02.03.04,43.03.07,70.10;"Complexes involving RBTN2, TAL1, and GATA1 (or -2), together with E47, the basic helix-loop-helix heterodimerization partner of TAL1, could be demonstrated. Thus, a molecular link exists between three proteins crucial for erythropoiesis, and the data suggest that variations in amounts of complexes involving RBTN2, TAL1, and GATA1 (or -2) could be important for erythroid differentiation.";"";""
1372;Rb-tal-1-E2A-Lmo2-Ldb1 complex;;Human;Q86U70,P25791,P06400,P17542,P15923;8861,4005,5925,6886,6929;MI:0019- coimmunoprecipitation;10866689;11.02.03.04.03,43.03.07,70.10;"Data indicate that this pentameric complex assembled in maturing erythroblasts plays an important regulatory role in c-kit downmodulation- hypothetically, the complex may regulate the expression of other critical erythroid genes.";"";""
1373;Ldb1-Lmo2-Gata-1-Tal1-E47 complex;;Mouse;P17679,P70662,P25801,P22091,P15806;14460,16825,16909,21349,21423;MI:0019- coimmunoprecipitation;9214632;11.02.03.04,16.03.01,43.03.07,70.10,73.03.07.01;"In erythroid cells Lmo2 forms a novel DNA-binding complex, with GATA-1, TAL1 and E2A, and the recently identified LIM-binding protein Ldb1/NLI. This oligomeric complex binds to a unique, bipartite DNA motif comprising an E-box, CAGGTG, followed approximately 9 bp downstream by a GATA site. The protein complex may play a role in haematopoiesis.";"";""
1375;Pyruvate dehydrogenase complex;;Bovine;P11180,P09622,P08559,P11966,P22439;0,1738,5160,613610,517402;MI:0401- biochemical;14638692;01.05.07.07,02.08,70.16;"The mitochondrial pyruvate dehydrogenase complex (PDC)1 catalyzes the irreversible conversion of pyruvate to acetyl-CoA along with the reduction of NAD+. PDCs from all known sources contain the pyruvate dehydrogenase (E1), the dihydrolipoyl acetyltransferase (E2), and the dihydrolipoyl dehydrogenase (E3) components. ";"";"Since bovine Pdha1 and Dld were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1377;hASC-1 complex;;Human;Q8N9N2,Q9H1I8,Q8N3C0,Q15650;51008,84164,10973,9325;MI:0029- cosedimentation through density gradients;12077347;11.02.03.04.01,30.01.11,70.10;"Endogenous hASC-1 complex appears to play an essential role in AP-1, SRF, and NF-kappaB transactivation and to mediate the transrepression between nuclear receptors and either AP-1 or NF-kappaB in vivo.";"";""
1378;Translocon-associated protein (TRAP) complex;;Dog;P16967,P23438,Q9UNL2,P51571;403951,403950,6747,6748;MI:0276- blue native page;10471800;14.04,16.17.01,20.01.10,20.09.05,70.07;"TRAP complex regulates the retention of ER resident proteins.";"";"Since SSR3 and SSR4 from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
1379;GALNS-lysosomal hydrolase 1.27 MDa complex;;Human;P10619,P34059,P16278,Q99519;5476,2588,2720,4758;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;8910459;01.05.03,70.25;"The 1.27-MDa complex of lysosomal hydrolases is essential for keratan sulfate catabolism. Disruption of this complex may be responsible for the KS accumulation in beta-galactosidosis and galactosialidosis patients. Association of GALNS with the three other lysosomal hydrolases protects GALNS in lysosomes.";"";""
1380;Elongator holo complex;;Human;Q6IA86,Q9H9T3,Q96EB1,O95163;55250,55140,26610,8518;MI:0029- cosedimentation through density gradients;11714725;11.02.03.01.04,14.07.04,70.10;"The holo-Elongator complex has histone acetyltransferase activity directed against histone H3 and H4. Holo-Elongator interacts with RNA polymerase II.  ";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: p38, p30."
1385;DICER1-NCOA6-AGO2 complex;;Human;Q9UPY3,Q9UKV8,Q14686;23405,27161,23054;MI:0019- coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;15973356;11.02.03.04.05,11.04,70.03;"Results support a role of the Dicer-TRBP complex not only in miRNA processing but also as a platform for RISC assembly.";"";""
1386;TTP-AGO4 complex;;Human;Q9HCK5,P26651;192670,7538;MI:0019- coimmunoprecipitation;15766526;01.03.16.01,11.02.03.04.05,16.03.03,70.03;"In analogy to the TTP-AGO2 complex the TTP-AGO4 complex is presumably involved in the miRNA-mediated degradation of RNAs containing AU-rich elements (AREs).";"";""
1387;TTP-AGO2 complex;;Human;Q9UKV8,P26651;27161,7538;MI:0019- coimmunoprecipitation;15766526;01.03.16.01,11.02.03.04.05,16.03.03,70.03;"The TTP-AGO2 complex is involved in the miRNA-mediated degradation of RNAs containing AU-rich elements (AREs).";"";""
1388;RB1-TFAP2A complex;;Dog;Q9XSY1,P05549;0,7020;MI:0019- coimmunoprecipitation;9632747;11.02.03.04.01;"";"";"Since TFAP2A from dog was not available in the UniProt database at the time of annotation, the orthologous protein from human was used."
1390;Rb1-Runx2 complex;;Mouse;P13405,Q08775;19645,12393;MI:0096- pull down;11545733;43.03.17;"pRb physically interacts with the osteoblast transcription factor, CBFA1, and associates with osteoblast-specific promoters in vivo in a CBFA1-dependent fashion. Association of pRb with CBFA1 and promoter sequences results in synergistic transactivation of an osteoblast-specific reporter.";"";""
1399;WDR5-ASH2L-RBBP5-MLL2 complex;3 H4 methyltransferase complex;Human;Q9UBL3,O14686,Q15291,P61964;9070,8085,5929,11091;MI:0019- coimmunoprecipitation;15960974;11.02.03.04.01,14.07.09,70.10;"The WDR5-ASH2L-RBBP5-MLL2 complex performs methylation of lysine 4 (K4) of histone H3. Knockdown of xWDR5 during Xenopus development leads to somitic, gut, and hematopoetic defects.";"";""
1400;ASCOM complex; ASC-2 complex;Human;Q9UBL3,O14686,Q8NEZ4,Q14686,Q15291,P68366,P07437;9070,8085,58508,23054,5929,7277,203068;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;12482968;10.01.09.05,11.02.03.04.01,16.03.01,42.10.03,70.10;"ASCOM exhibit very weak but specific H3-lysine 4 methylation activities in vitro, and transactivation by retinoic acid receptor appears to involve ligand-dependent recruitment of ASCOM and subsequent transient H3-lysine 4 methylation of the promoter region in vivo. Thus, ASCOM may represent a distinct coactivator complex of nuclear receptors. MALDI-TOF mass spectrometry analyses identified also ALR-2, the splicing isoform of ALR-1.";"";""
1401;MOF complex;;Human;Q03164,O14686,Q9H7Z6,Q15291,Q99496,O15047,P21675,P49848,Q16594,P61964;4297,8085,84148,5929,6045,9739,6872,6878,6880,11091;MI:0226- ion exchange chromatography | MI:0007- anti tag coimmunoprecipitation;15960975;70.10;"";"";"Immunoprecipitation of the three step purified complex by anti-MOF antibodies. The complex was not functionally characterized."
1408;Ets2-Smarca4-Smarcb1-Smarce1 complex;;Mouse;P15037,O35845,Q9Z0H3,O54941;23872,20586,20587,57376;MI:0007- anti tag coimmunoprecipitation;12637547;11.02.03.04.03,16.03.01,70.10;"Ets-2 has previously been characterized as an activator of gene expression. In contrast, in this study, ets-2 directly interacted with Brg-1, the ATPase component of the mSWI/SNF complex, and Brg-1 behaved as a transcriptional co-repressor along with ets-2.";"";""
1413;NCOR1 complex;;Human;O15379,O75376,Q15459,Q15393,P51532,Q12824,Q92922,Q8TAQ2,Q6ZRS2,Q13263;8841,9611,10291,23450,6597,6598,6599,6601,10847,10155;MI:0071- molecular sieving | MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;11013263;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,70.10;"Transcriptional silencing by many transcription factors is mediated by the nuclear receptor corepressor (N-CoR). The mechanism by which N-CoR represses basal transcription involves the direct or indirect recruitment of histone deacetylases (HDACs). Two multiprotein N-CoR complexes have been isolated, designated N-CoR-1 and N-CoR-2, which possess histone deacetylase activity that is mediated by distinct HDACs. Results suggest that N-CoR is found in distinct multiprotein complexes, which are involved in multiple pathways of transcriptional repression.";"";""
1423;L-periaxin-Drp2 complex;;Mouse;Q62165,P11531,Q05AA6,O55103,Q61636;13138,13405,13497,19153,22288;MI:0019- coimmunoprecipitation;11430802;70.02;"Disruption of the DRP2-dystroglycan complex is followed by hypermyelination and destabilization of the Schwann cell-axon unit in Prx(-/-) mice. Hence, the DRP2-dystroglycan complex likely has a distinct function in the terminal stages of PNS myelinogenesis, possibly in the regulation of myelin thickness. The dystroglycan precursor DAG1 includes alpha-dystroglycan and beta-dystroglycan polypeptides.";"";""
1439;PTGS2 homodimer complex;;Human;P35354;5743;MI:0114- x-ray crystallography;10811226;01.06;"";"";""
1442;Transporter (Ncx1) - receptor complex; Plasma membrane - cytoskeleton - endoplasmic reticulum complex;Rat;P97582,P11507,P29994,Q01728,P16086;362036,29693,25262,29715,64159;MI:0019- coimmunoprecipitation;14593108;30.01.09.03;"The experimental data support the idea that in neurons and glia PM microdomains containing Ncx1 and Na+  pumps with alpha2 or alpha3 subunits form Ca2+ signaling complexes with underlying ER containing Serca2 (=Atp2a2) and IP(3)R-1 (=Itpr1).";"";""
1448;LIN2-LIN7-SAP97 complex;;Mammalia;O14936,Q12959,O14910;8573,1739,8825;MI:0019- coimmunoprecipitation;11865057;14.04,40.01.03,41.05.19,45.03.09,75.03.09;"";"";""
1449;Dlg3-Lin7-SAP97 complex;;Mammalia;Q811D0,P70175,Q8JZS0;13383,53310,108030;MI:0019- coimmunoprecipitation;12351654;14.04,40.01.03,41.05.19,75.03.09;"";"";""
1452;MCM2-MCM6-MCM7 complex;;Human;P49736,Q14566,P33993;4171,4175,4176;MI:0006- anti bait coimmunoprecipitation;15448696;10.01.03,70.10;"";"";""
1457;AFF1-MLLT1-CBX8 complex;;Human;P51825,Q9HC52,Q03111;4299,57332,4298;MI:0027- cosedimentation;15856011;11.02.03.04,70.10.09;"";"";""
1458;SNF2h-HDAC12 complex;;Human;Q92769,O60264;3066,8467;MI:0019- coimmunoprecipitation;15775975;10.01.11,14.07.04,42.10.03;"SNF2h-HDAC1/2 complex coordinates G1-specific chromatin remodeling and histone deacetylation with the DNA replication initiation process at OriP.";"";""
1462;hPRC1L complex; human Polycomb repressive complex 1-like;Human;P35226,Q8IXK0,Q06587,Q99496;648,1912,6015,6045;MI:0071- molecular sieving | MI:0226- ion exchange chromatography;15386022;10.01.09,11.02.03.04.05,14.07.05,70.10;"The hPRC1L complex silences transcription by ubiquinating histone H2A at Lys 119.";"";""
1464;Mis12 centromere complex;;Human;P45973,Q9H410,Q9H081,Q96IY1,Q6P1K2,O95229;23468,79980,79003,25936,11243,11130;MI:0019- coimmunoprecipitation;15502821;10.03.04.05,70.10.04;"";"";""
1469;E2f5-Rbl2-Hdac1 complex; E2F5-p130-HDAC1 complex;Mouse;Q61502,O09106,Q64700;13559,433759,19651;MI:0019- coimmunoprecipitation;11319226;10.03.01.02,16.03.01,43.03.04;"Induction of differentiation in mouse keratinocytes results in formation of E2f5-Rbl2-Hdac1 complex, which can trigger keratinocyte entry into quiescence.";"";""
1470;pRb2/p130-multimolecular complex (DNMT1, E2F5, SuV39H1, HDAC1, RBL2);;Human;P26358,Q15329,Q13547,Q08999,O43463;1786,1875,3065,5934,6839;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;12789259;11.02.03.01;"";"";""
1471;pRb2/p130-multimolecular complex (RB2, E2F5, HDAC1, SUV39H1, P300);;Human;Q15329,Q09472,Q13547,Q08999,O43463;1875,2033,3065,5934,6839;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;12789259;11.02.03.01;"";"";""
1473;E2F5-RB2-DP1 complex;;Human;Q15329,Q08999,Q14186;1875,5934,7027;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;7760804;11.02.03.01;"";"";""
1474;SMAD3/4-E2F4/5-p107-DP1 complex;;Human;Q16254,Q15329,P28749,P84022,Q13485,Q14186;1874,1875,5933,4088,4089,7027;MI:0007- anti tag coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;12150994;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"E2F4/5 and p107 act as signal cotransducers that enable a SMAD complex to recognize and repress c-Myc transcription.";"";""
1475;S-phase-specific E2F-p107 complex;;Mouse;P97377,Q8R0K9,Q64701,Q08639,(Q61456,P51943);12566,104394,19650,21781,(12427,12428);MI:0047- far western blotting | MI:0019- coimmunoprecipitation;10082561;10.03.01.01.05,47.03.11.07;"The authors describe the cdk2-DP1-E2F-p107-cyclin A complex but don't specify cyclin A. Uniprot gives two cyclins: A1 and A2. The formation of E2F-p107 complexes during prenatal liver development in mice is dependent on C/EBPa.";"";""
5658;Nrp1-PlexinD1 complex;;Human;O14786,Q9Y4D7;8829,23129;MI:0007- anti tag coimmunoprecipitation;15239958;30.05.02,40.01.03.03,41.05.16,45.03.12.03,47.03.03.02;"PlexinD1-Npn1 form a functional receptor for Sema3C.";"";""
5708;Dok1-Map4k4-Nck1-Rasa1 complex;;Mouse;P97465,P97820,Q8BMV0,Q91YX7;13448,26921,17973,218397;MI:0019- coimmunoprecipitation;10669731;14.07.03,30.05.01.12;"";"";""
1488;DNMT1-RB1-HDAC1-E2F1 complex;;Human;P26358,Q01094,Q13547,P06400;1786,1869,3065,5925;MI:0027- cosedimentation;10888886;11.02.03.04.03;"";"";""
1490;DAXX-DNMT1-DMAP1 complex;;Human;Q9UER7,Q9NPF5,P26358;1616,55929,1786;MI:0019- coimmunoprecipitation;14978102;11.02.03.04.03;"";"";""
1491;RGS6-DNMT1-DMAP1 complex;;Human;Q9NPF5,P26358,P49758;55929,1786,9628;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;14734556;11.02.03.04;"This complex inhibits DMAP1 transcriptional repressor activity.";"";""
1492;BHC110 complex;;Human;O60341,Q14687,Q13547,Q92769,Q9P0W2,Q96BD5,Q9UKL0,Q9UBW7,O75362,Q92618;23028,23199,3065,3066,10362,51317,23186,7750,7764,9658;MI:0019- coimmunoprecipitation;16079794;10.01.09.05,14.07.04,14.07.09,70.10;"The BHC110 complex performs demethylation of histone H3 lysine 4 (H3K4). The related BHC complex (CORUM ID 636) is recruited by a neuronal silencer, REST (RE1-silencing transcription factor), and mediates the repression of REST-responsive genes. Depletion of the CoREST (RCOR1) subunit of the BHC110 complex and the BHC complex results in de-repression of REST-responsive gene expression and increased methylation of H3K4.";"";""
1495;PID complex;;Human;Q14839,Q13547,O95983,O94776,Q09028;1108,3065,53615,9219,5928;MI:0007- anti tag coimmunoprecipitation;11099047;14.07.04,18.01.01,18.02.09,70.10;"PID complex-mediated repression of p53 transactivation functions acts, in part, through deacetylation of p53 at the C terminus. Experiments  show that PID is involved in the regulation of p53-mediated growth arrest and apoptosis.";"";""
1503;Hdac1-Mecp2-Rcor1-Sin3a complex;;Mouse;O09106,Q9Z2D6,Q8CFE3,Q60520;433759,17257,217864,20466;MI:0019- coimmunoprecipitation;15907476;11.02.03.04.03;"";"";""
1505;NCOR2 complex;;Human;Q13547,Q92769,O15379,O75376,Q9Y618,O75446,Q96ST3;3065,3066,8841,9611,9612,8819,25942;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;11013263;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.04,42.10.03,70.10;"Transcriptional silencing by many transcription factors is mediated by the nuclear receptor corepressor (N-CoR). The mechanism by which N-CoR represses basal transcription involves the direct or indirect recruitment of histone deacetylases (HDACs). Two multiprotein N-CoR complexes have been isolated, designated N-CoR-1 and N-CoR-2, which possess histone deacetylase activity that is mediated by distinct HDACs. Results suggest that N-CoR is found in distinct multiprotein complexes, which are involved in multiple pathways of transcriptional repression. Only weak amounts of HDAC3 could be detected in the N-CoR-2 complex.";"";""
1508;BCL6-ZBTB17 complex;;Human;P41182,Q13105;604,7709;MI:0096- pull down;16142238;11.02.03.04.03;"BCL6 interacted with the transcriptional activator Miz-1 and, via Miz-1, bound to the promoter and suppressed transcription of the cell cycle arrest gene CDKN1A.";"";""
1514;IL4-IL4R complex;;Human;P05112,P24394;3565,3566;MI:0030- cross-linking studies;8266078;16.01,30.05.01.05;"";"";""
1515;IL4-IL4R-IL2RG complex;;Human;P31785,P05112,P24394;3561,3565,3566;MI:0030- cross-linking studies;8266078;30.05.01.05;"";"";""
1519;IL6ST-PRKCD-STAT3 complex;;Human;P40189,Q05655,P40763;3572,5580,6774;MI:0019- coimmunoprecipitation;12361954;18.01.07;"PKCdelta  is recruited to the receptor gp130 via Stat3, which not only stabilizes the Stat3 and gp130 receptor interaction, but may also phosphorylate gp130.";"";""
1520;STAT3-NLK-MAP3K7 complex;;Human;O43318,Q9UBE8,P40763;6885,51701,6774;MI:0019- coimmunoprecipitation;15764709;30,70.10;"The complex is involved in the TAK1-Nemo-like kinase (NLK) pathway.";"";""
1521;p300-SMAD1-STAT3 complex;;Mammalia;Q09472,Q15797,P40763;2033,4086,6774;MI:0007- anti tag coimmunoprecipitation;10205054;11.02.03.04.01,30.05.01,43.03.11,77.03.01.01.01;"P300 acts as an adaptor linking SMAD1 and STAT3. ";"";""
1522;STAT3 homodimer copmplex;;Human;P40763;6774;MI:0019- coimmunoprecipitation;15653507;11.02.03.04,16.03.01;"Lys685 acetylation was critical for Stat3 to form stable dimers required for cytokine-stimulated DNA binding and transcriptional regulation, to enhance transcription of cell growth-related genes, and to promote cell cycle progression in response to treatment with oncostatin M.";"";""
1523;Stat3-Crebbp complex;;Mouse;P45481,P42227;12914,20848;MI:0402- chromatin immunoprecipitation assays;15852015;47.03.01.01.01;"";"";""
1530;Girdin homo-oligomer complex;;Human;Q3V6T2;55704;MI:0019- coimmunoprecipitation;16139227;34.05,42.04.03;"Girdin is essential for the integrity of the actin cytoskeleton and cell migration.";"";"Oligomer"
1537;Heterotrimer complex (Rnd1, Rras, Plxnb1);;Mammalia;Q8CJH3,Q8BLR7,P10833;235611,223881,20130;MI:0019- coimmunoprecipitation;15297673;16.01.01,18.02.01.01.01,30.05,34.07;"";"";""
1539;G protein complex (GNG2, GNB2L1, RAF1);;Human;P63244,P59768,P04049;10399,54331,5894;MI:0047- far western blotting | MI:0018- two hybrid;7782277;30.01.05.05,30.05.02.24;"Raf-1 is a serine-threonine protein kinase critically positioned in a cascade linking activated growth factor receptors with the nucleus and ultimatively regulating the mitogenic response.";"";""
1543;PPP2CA-PPP2R1A complex;;Human;P67775,P30153;5515,5518;MI:0019- coimmunoprecipitation;12370081;18.02.01;"";"";""
1544;PPP2CA-PPP2R1A-PPP2R3A complex;;Human;P67775,P30153,Q06190;5515,5518,5523;MI:0019- coimmunoprecipitation;12506124;18.02.01;"";"";""
1549;Kpna2-Kpnb1 complex;;Mouse;P52293,P70168;16647,16211;MI:0114- x-ray crystallography | MI:0027- cosedimentation | MI:0016- circular dichroism;11448961;20.01.10,20.09.18,70.10;"The importin-alpha/beta complex binds representative monopartite NLS (simian virus 40 large T-antigen) and bipartite NLS (nucleoplasmin) with affinities (K(D) = 3.5 x 10(-8) m and 4.8 x 10(-8) m, respectively).";"";""
1551;IPO13-RAN-EIF1AX complex;;Human;P47813,O94829,P62826;1964,9670,5901;MI:0004- affinity chromatography technologies;11447110;20.01.10,20.09.01,70.03,70.10;"Imp13 operates differently from typical exportins in that the binding of eIF1A to Imp13 is only regulated indirectly by RanGTP, and the cytoplasmic release of eIF1A from Imp13 is triggered by the loading of import substrates onto Imp13 (PMID:11447110).";"";""
1552;TNPO2-RAN-NXF1 complex;;Human;Q9UBU9,P62826,O14787;10482,5901,30000;MI:0019- coimmunoprecipitation;12384575;16.03.03,20.01.21,20.09.01,70.03,70.10;"Kap beta2B participates directly in the export of a large proportion of cellular mRNAs, and TAP connects Kap beta2B to the mRNAs to be exported (PMID:12384575).";"";""
1554;RANBP1-RAN-KPNB1 complex;;Human;Q14974,P62826,P43487;3837,5901,5902;MI:0007- anti tag coimmunoprecipitation;10037787;20.01.10,20.09.01;"This complex is exported as a complex from the nucleus to the cytoplasm in living cells. The binding of RanBP1 to the Ran-importin beta  complex is required for the dissociation of the complex in the cytoplasm and that the released Ran is recycled to the nucleus, which is essential for the nuclear protein transport (PMID:10037787).";"";""
1555;Nmi-Rpa2-Rrn3 complex;;Mouse;O35309,Q62193,Q7TNE7;64685,19891,106298;MI:0019- coimmunoprecipitation;15558034;11.02.01;"";"";""
1556;Rpa2-Rrn3 complex;;Mouse;Q62193,Q7TNE7;19891,106298;MI:0019- coimmunoprecipitation;15558034;11.02.01;"";"";""
1557;NMI-POLR1B-RRN3 complex;;Human;Q13287,Q9H9Y6,Q9NYV6;9111,84172,54700;MI:0019- coimmunoprecipitation;15558034;11.02.01;"";"";""
1558;POLR1B-RRN3 complex;;Human;Q9H9Y6,Q9NYV6;84172,54700;MI:0019- coimmunoprecipitation;15558034;11.02.01;"";"";""
1560;Nmi-Rrn3 complex;;Mouse;O35309,Q7TNE7;64685,106298;MI:0019- coimmunoprecipitation;15558034;11.02.01;"";"";""
1561;NMI homodimer complex;;Human;Q13287;9111;MI:0019- coimmunoprecipitation;11916966;14.10;"Homodimerization of Nmi enhanced its association with BRCA1.";"";""
1571;Vigilin-DNA-PK-Ku antigen complex; vigilin-Ku70-Ku86-DNA-PKcs complex;Human;Q00341,P78527,P13010,P12956;3069,5591,7520,2547;MI:0007- anti tag coimmunoprecipitation;15723802;10.03.04.05,14.07.03,16.03.03,70.10.03;"The authors describe, that in the presence of RNA, the Vigilin complex recruits the DNA-PKcs enzyme, which appears to phosphorylate a discrete set of targets, some or all of which are known to participate in chromatin silencing.";"";""
5757;PLXNA1-RANBPM complex;;Human;Q9UIW2,Q96S59;5361,10048;MI:0007- anti tag coimmunoprecipitation;16672672;20.09.07.07,30.05.02,40.01.03.03;"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.";"";""
1589;Junb-Sumo1 complex;;Mouse;P09450,P63166;16477,22218;MI:0019- coimmunoprecipitation;10788439;11.02.03.04;"";"";""
1595;Cdk5-c-Abl-Cables complex;;Mouse;P00520,Q9ESJ1,P49615;11350,63955,12568;MI:0019- coimmunoprecipitation;10896159;14.07.03,47.03.01;"Data suggest that Cables and Cdk5 tyrosine phosphorylation are involved in axon growth regulation.";"";""
1602;Cdk5-p35-CaMKII(alpha)-(alpha)actinin1 complex;;Rat;Q9Z1P2,P11275,Q03114,P61810;81634,25400,140908,116671;MI:0096- pull down;12223541;10.03.01,30.01.05.01,34.05.01,41.05.13,43.03.13,47.03.01.01.01,77.03.01.01.01;"";"Cdk5 might be a potential drug target for the treatment of neurodegenerative diseases.";""
1608;Kir3.2 homotetramer complex;;Mouse;P48542;16522;MI:0004- affinity chromatography technologies;15723059;20.01.01.01,20.03.01.01;"";"";""
1609;G protein complex (Gngt2, Kcnj3, Gnb1);;Mouse;P62874,Q61017,P63250;14688,14710,16519;MI:0096- pull down;12743112;30.01.05.05,30.05.02.30;"";"";""
1610;G protein complex (Gngt2, Kcnj6, Gnb1);;Mouse;P62874,Q61017,P48542;14688,14710,16522;MI:0096- pull down;12743112;30.01.05.05,30.05.02.30;"";"";""
1612;Heterotrimeric G protein complex (GNG2, GNB1, GNAS);;Human;P63092,P62873,P59768;2778,2782,54331;MI:0051- fluorescence technologies;15782186;30.01.05.05.03;"Guanine nucleotide-binding proteins  (G proteins) are composed of 3  units, alpha, beta and gamma and  are involved in various transmembrane  signaling systems.";"";""
1614;G protein complex (MCF2, GNB1, GNG2);;Human;P62873,P59768,P10911;2782,54331,4168;MI:0019- coimmunoprecipitation;10518015;30.01.05.05;"";"";""
1615;G protein complex (BTK, GNG1, GNG2);;Human;Q06187,P62873,P59768;695,2782,54331;MI:0047- far western blotting;7972043;30.01.05.05,43.03.07.02.01;" ";"Deficient expression or function of Bruton tyrosine kinase (Btk) causes human X chromosome-linked agammaglobulinemia (XLA) or murine X chromosome-linked immunodeficiency (XID).";""
1617;G protein complex (CACNA1A, GNB1, GNG2);;Human;O00555,P62873,P59768;773,2782,54331;MI:0047- far western blotting;9238069;30.01.05.05,30.05.02.24;"The direct interaction of the G proteins (beta, gamma) with the Ca-channel alpha 1 subunit  is responsible for the channel inhibition by  G protein-coupled receptors.";"";""
1618;G protein complex (PTHR1, GNB1, GNG2);;Human;P62873,P59768,Q03431;2782,54331,5745;MI:0047- far western blotting;16099817;30.01.05.05;"The G protein-coupled receptor for PTH-related protein (PTH1R) signals via many intracellular pathways.";"";""
1619;G protein complex (HDAC5, GNB1, GNG2);;Human;P62873,P59768,Q9UQL6;2782,54331,10014;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;16221676;11.02.03.04.03,30.01.05.05;"The class II HDAC5 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.";"";""
1620;G protein complex (HDAC4, GNB1, GNG2);;Human;P62873,P59768,P56524;2782,54331,9759;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;16221676;11.02.03.04.03,30.01.05.05;"The class II HDAC4 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.";"";""
1623;FA core complex 1 (Fanconi anemia core complex 1);;Human;O15360,Q00597,Q9HB96,Q9NPI8,O15287;2175,2176,2178,2188,2189;MI:0027- cosedimentation;12093742;32.01.09,14.07.05,70.10;"FANCE functions to target cytoplasmic FANCC to the nucleus. ";"FA complex is involved in Fanconi anemia (FA) disease.";""
1624;FA core complex (Fanconi anemia core complex);;Human;Q0VG06,O15360,Q8NB91,Q00597,Q9HB96,Q9NPI8,O15287,Q9NW38,Q8IYD8;80233,2175,2187,2176,2178,2188,2189,55120,57697;MI:0007- anti tag coimmunoprecipitation;15502827;14.07.05,32.01.09,70.10;"";"FA complex is involved in Fanconi anemia (FA) disease.";""
1625;FA core complex (Fanconi anemia core complex);;Human;O15360,Q8NB91,Q00597,Q9HB96,Q9NPI8,O15287,Q8IYD8;2175,2187,2176,2178,2188,2189,57697;MI:0006- anti bait coimmunoprecipitation;16116434;14.07.05,32.01.09,70.10;"";"FA complex is involved in Fanconi anemia (FA) disease.";""
1633;CyclinD1-CDK4-CDK6 complex;;Human;P24385,P11802,Q00534;595,1019,1021;MI:0007- anti tag coimmunoprecipitation;8930396;10.03.01.01,10.03.01.01.03,30.01.05.01,41.05.15;"Upon myocyte differentiation subunit composition of the CDK4/6 complex is altered. Interaction with cyclinD1 is reduced but interaction with cyclinD3 and p21 is enhanced thus inhibiting the kinase activity of CDK4/6.";"";""
1634;CyclinD1-CDK4-p21 complex;;Mammalia;P24385,P11802,P38936;595,1019,1026;MI:0006- anti bait coimmunoprecipitation;9467962;10.03.01.02,30.01.05.01;"";"";"Since CCND1 and CDK4 from hamster were not available in the Uniprot database at the time of annotation, the orthologous human proteins were used."
1637;Ccnd1-Cdk4 complex;;Mouse;P25322,P30285;12443,12567;MI:0019- coimmunoprecipitation;8534916;10.03.01.02;"";"";""
1642;p16-cyclin D2-CDK4 complex;;Human;P30279,P11802,P42771;894,1019,1029;MI:0006- anti bait coimmunoprecipitation;7739547;10.03.01,30.01.05.01;"p16 binds to preassembled cyclinD-CDK complex in vitro and inhibits their activity without replacing Cyclin D. However, affinity for p16 to the uncomplexed CDK4 is higher.";"";""
1652;Ccna2-Cdk2 complex;;Mouse;P51943,P97377;12428,12566;MI:0019- coimmunoprecipitation;8534916;10.03.01.02;"";"";""
1656;p27-cyclinE-CDK2 complex;;Human;P24864,P24941,P46527;898,1017,1027;MI:0007- anti tag coimmunoprecipitation;17409098;10.03.01.01.03,18.02,70.10;"p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes. Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. ";"Overexpression of p27 in certain cancer cells prevents DNA replication and tumor formation in nude mice, whereas the loss of p27 has been reported in many human cancers and predicts a poor prognosis in breast, prostate, colon, gastric, lung, and esophageal cancers.";""
1661;E2F4-p107-cyclinA complex;;Human;P20248,Q16254,P28749;890,1874,5933;MI:0412- electrophoretic mobility supershift assay;12096339;10.03.01.01.03,70.10;"In proliferating MCF-7 cells the complex contains mostly cyclin A. After overexpression of cyclin E most of the complexes contain cyclin E. ";"";""
5712;FAK-beta5 integrin complex, VEGF induced;;Human;P18084,Q05397;3693,5747;MI:0006- anti bait coimmunoprecipitation;12844492;30.05.01.12,41.05.16,42.06.03,77.03.01.01.01;"VEGF induces the formation of FAK-beta5 integrin complex.";"";""
1695;SCAMP1-SCAMP2 complex;;Human;O15126,O15127;9522,10066;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;9224770;20.01.10,20.09.07.06;"";"";""
1700;ABL2-HRAS-RIN1 complex;;Human;P42684,P01112,Q13671;27,3265,9610;MI:0019- coimmunoprecipitation;15886098;30.01.05.01;"The formation of this stable complex is consistent with a pathway connecting RAS proteins with the cytoplasmic functions of ABL-family tyrosine kinases through RIN1.  ";"";""
1703;IGHM-VPREB1-IGLL1 complex;;Human;P01871,P15814,P12018;3507,3543,7441;MI:0019- coimmunoprecipitation;11564802;43.03.07.02.01.01;"";"";""
1707;IL2-IL2RA-IL2RB complex;;Human;P60568,P01589,P14784;3558,3559,3560;MI:0019- coimmunoprecipitation;2303462;30.05.01.05;"";"";""
1714;TICAM1-TICAM2-TLR4 complex;;Human;Q8IUC6,Q86XR7,O00206;148022,353376,7099;MI:0019- coimmunoprecipitation;14519765;40.02.03.01;"TICAM-2 physically bridges TLR4 and TICAM-1 and functionally transmits LPS-TLR4 signaling to TICAM-1, which in turn activates IRF-3.";"";""
1723;Pax3-Lef1-Tle4 complex;;Mouse;P27782,P24610,Q62441;16842,18505,21888;MI:0019- coimmunoprecipitation;15729346;30.05.02.20;"";"";""
1724;Spen-Hivep1 complex;;Mouse;Q03172,Q62504;110521,56381;MI:0096- pull down | MI:0019- coimmunoprecipitation | MI:0018- two hybrid;15778499;11.02.03.04.05,47.03.17;"MINT and CRYBP1 form a complex on the Col2a1 enhancer.";"";""
1728;CTCF-nucleophosmin-PARP-HIS-KPNA-LMNA-TOP complex;;Human;P49711,P0C0S5,Q6FI13,P52294,O00505,P02545,P06748,P09874,P11388;10664,3015,723790,3836,3839,4000,4869,142,7153;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;14759373;11.02.03.04,70.10;"Nucleophosmin is the most prominent binding partner of CTCF.";"";""
1729;TLE1 corepressor complex (MASH1 promoter-corepressor complex);;Human;P60709,P34932,P35580,P19338,Q15233,P06748,P09874,Q92878,Q04724,Q02880;60,3308,4628,4691,4841,4869,142,10111,7088,7155;MI:0676- tandem affinity purification | MI:0007- anti tag coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;15607978;11.02.03.04.03,16.01,16.03.01,18.01.07,18.02.09,43.03.13,70.10,77.03.01.01.01;"The TLE1 complex is required for HES1-mediated transcription repression. PARP1 is inactive in the TLE1 complex. After Ca(2+) induction, kinase CaMKII-delta activates PARP1 leading to dismissal of the TLE1 corepresspor complex from HES1.";"";""
1730;Nfatc2ip-Prmt1;;Mouse;Q60591,O09130,Q9JIF0;18019,18020,15469;MI:0019- coimmunoprecipitation;15327772;01.02.03.04.01;"NFATc2, NIP45, and PRMT1 form a ternary complex as evidenced by the fact that PRMT1 and NFATc2 association is substantially promoted by the presence of full-length NIP45 but much less so by the presence of ?N-NIP45. he amino terminus of NIP45 may serve a dual function in supporting NFAT interaction and recruiting PRMT1 to the NFAT transcription-activating complex.";"";""
1731;PRMT1 complex;;Human;Q99873;3276;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;11152681;14.07.09,70.10;"PRMT1 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer.";"";""
1734;SF3A1-SF3A2-SF3A3 complex;;Human;Q15459,Q15428,Q12874;10291,8175,10946;MI:0019- coimmunoprecipitation;11533230;11.04.03.01,70.10;"All SF3A subunits are essential for the formation of the mature 17S U2 snRNP and the prespliceosome.";"";""
1737;SF3b complex;;Human;Q86XP3,Q7RTV0,O75533,Q9Y3B4,Q13435,Q15393,Q15427,Q9BWJ5;11325,84844,23451,51639,10992,23450,10262,83443;MI:0019- coimmunoprecipitation;12234937;11.04.03.01,70.10;"The splicing factor SF3b is a multiprotein complex essential for the accurate excision of introns from pre-messenger RNA (PMID:12738865).";"";""
1743;(E.F.G) complex;;Human;P62304,P62306,P62308;6635,6636,6637;MI:0114- x-ray crystallography | MI:0028- cosedimentation in solution;9020971;11.04.03.01,70.10;"All four spliceosomal small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/U6 and U5 contain a common structural element called the snRNP core. This core is assembled from the common snRNP proteins and the small nuclear RNA (snRNA). The RNA-free (E.F.G) complex contains the smallest U1 and U5 snRNP core proteins, i.e. E, F and G.";"";""
1745;SMN complex;;Human;Q9UHI6,P57678,Q8TEQ6,Q8WXD5,Q9H840,O14893,P09012,P14678,P62314,P62316,P62318,P62304,P62306,P62308,P63162;11218,50628,25929,79833,79760,8487,6626,6628,6632,6633,6634,6635,6636,6637,6638;MI:0007- anti tag coimmunoprecipitation;11748230;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"Assembly of the Sm-class of U-rich small nuclear ribonucleoprotein particles  (U snRNPs) is a process facilitated by the macromolecular survival of motor  neuron (SMN) complex.  The SMN complex is found both in the cytoplasm and in the nucleus, where it is concentrated in gems, nuclear bodies similar in size and number to Cajal (coiled) bodies and often associated with them. ";"Spinal muscular atrophy (SMA) is the most common genetic cause of infant mortality.  Deletions or mutations in the survival of motor neurons (SMN1) gene, the SMA-causing gene, are detected in over 95% of SMA patients. ";""
1746;SMN containing complex;;Human;P57678,P09382,P17931,O14893,Q16637,P62314,P62316,P62318;50628,3956,3958,8487,6606,6632,6633,6634;MI:0019- coimmunoprecipitation;11522829;11.04.03.01,11.04.05,14.10,16.03.03,70.10;"Evidence suggests a role for SMN containing complex in spliceosome assembly. ";"Spinal muscular atrophy (SMA), (PMID:10601333)";""
1748;PRMT5 complex;;Human;O14744;10419;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;11152681;14.07.09,70.03;"PRMT5 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer. Recombinant PRMT5 protein methylates myelin basic protein, histone, and the amino terminus of fibrillarin.";"";""
1749;SMN-PolII-RHA complex;;Human;Q9UHI6,Q08211,P57678,Q00403,P24928,O14893,P14678,P08579,P63162,P20226;11218,1660,50628,2959,5430,8487,6628,6629,6638,6908;MI:0019- coimmunoprecipitation;11149922;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"Physical association between the Survival Motor Neuron (SMN) complex,  RNA polymerase II (pol II), snRNPs and RNA helicase A (RHA) suggest a role  for the SMN complex in the assembly of the pol II transcription/processing machinery.  SMN localizes both in the cytoplasm and in gems, nuclear bodies similar in size and  number to coiled bodies (Cajal bodies) and often associated with them. ";"Spinal muscular atrophy (SMA)";""
1750;PPP4C-PPP4R2-Gemin3-Gemin4 complex;;Human;Q9UHI6,P57678,P60510,Q9NY27;11218,50628,5531,151987;MI:0007- anti tag coimmunoprecipitation;12668731;14.07.03,70.10;"PPP4c is a member of the PPP family of protein phosphatases. PPP4 exists as high molecular mass complex of 450-600 kDa, and two putative regulatory subunits have been identified, R1 and R2. Protein phosphatase 4 interacts also with the Survival of Motor Neurons (SMN) complex and enhances the temporal localisation of snRNPs.";"";""
1751;SMN complex;;Human;Q9UHI6,P57678,Q8TEQ6,Q8WXD5,Q9H840,O14893,Q16637,P09012,P14678,Q9Y3F4;11218,50628,25929,79833,79760,8487,6606,6626,6628,11171;MI:0004- affinity chromatography technologies;15494309;11.04.03.01,11.04.05,14.10,16.03.03,20.01.01,20.01.21,20.09.01,70.03,70.10;"Survival of motor neurons (SMN) protein import depends on the presence of Sm snRNPs.  Conversely, import of labeled U1 snRNPs was SMN complex dependent.  Thus, import of SMN and U snRNPs are coupled in spinal muscular atrophy (SMA). ";"Spinal muscular atrophy (SMA)";""
1752;SMN complex;;Human;Q9UHI6,P57678,Q8TEQ6,Q8WXD5,Q9H840,O14893,Q16637;11218,50628,25929,79833,79760,8487,6606;MI:0007- anti tag coimmunoprecipitation;12065586;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"The survival of motor neurons (SMN) protein is the product of the gene mutated or deleted in the neurodegenerative disease,  spinal muscular atrophy.  SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6.  The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles.  The SMN complex is found both in the cytoplasm and in the nucleus where it is concentrated in gems, nuclear bodies similar in size and number to  Cajal bodies (coiled bodies (CBs) and often associated with them. ";"Spinal muscular atrophy (SMA)";""
1760;TOP1-PSF-P54 complex;;Human;Q15233,P23246,P11387;4841,6421,7150;MI:0004- affinity chromatography technologies;9756848;11.04.03.01,70.10;"";"";""
1767;CPSF6-ITCH-NUDT21-POLR2A-UBAP2L complex;;Human;Q16630,Q96J02,O43809,P24928,Q14157;11052,83737,11051,5430,9898;MI:0096- pull down;16055720;11.02.03.01,42.04.03,42.10.03;"";"";""
1768;CPSF6-EWSR1-ITCH-NUDT21-POLR2A-UBAP2L complex;;Human;Q16630,Q01844,Q96J02,O43809,P24928,Q14157;11052,2130,83737,11051,5430,9898;MI:0096- pull down;16055720;11.02.03.01,42.04.03,42.10.03;"";"";""
1769;CPSF6-ITCH-NUDT21-POLR2A complex;;Human;Q16630,Q96J02,O43809,P24928;11052,83737,11051,5430;MI:0096- pull down;16055720;11.02.03.01,42.04.03,42.10.03;"";"";""
1772;MICB-KLRK1-HCST complex;;Human;Q9UBK5,P26718,Q29980;10870,22914,4277;MI:0004- affinity chromatography technologies;11239445;36.25.16;"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.";"";""
1773;ULBP3-KLRK1-HCST complex;;Human;Q9UBK5,P26718,Q9BZM4;10870,22914,79465;MI:0004- affinity chromatography technologies;11239445;36.25.16;"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.";"";""
1774;MICA-KLRK1-HCST complex;;Human;Q9UBK5,P26718,Q29983;10870,22914,4276;MI:0004- affinity chromatography technologies;11239445;36.25.16;"";"";""
1775;ULBP2-KLRK1-HCST complex;;Human;Q9UBK5,P26718,Q9BZM5;10870,22914,80328;MI:0004- affinity chromatography technologies;11239445;36.25.16;"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.";"";""
1777;TGF-beta-receptor-SMAD7-SMURF2 complex;;Mammalia;O15105,Q9HAU4,P36897,P37173;4092,64750,7046,7048;MI:0007- anti tag coimmunoprecipitation;11163210;30.05.01.18.01,70.03;"SMAD7 mediates the interaction of SMURF2 with TGF-beta-receptor complex. ";"";""
1778;TGF-beta-receptor-Strap complex;;Mammalia;Q9Z1Z2,Q64729,Q62312;20901,21812,21813;MI:0007- anti tag coimmunoprecipitation;9856985;30.05.01.18.01,70.03;"";"";""
5852;p65-p50 Nf(kappa)B complex, Il-1-beta induced;;Rat;Q63369,Q7TQN4;81736,309165;MI:0412- electrophoretic mobility supershift assay;16556731;11.02.03.04.01,16.03.01,30.01.05.01.04;"The results suggest that 208F cells (fibroblast cell line) exposed to cytokine IL-1-beta have a different pattern of NF(kappa)B activation, with p65/p50 as the predominant NF-(kappa)B dimer. The results further show that cytokine induced NF(kappa)B activation in insulin-producing cells is more intense and sustained than in fibroblasts.";"";""
1779;TGF-beta-receptor-PAR6 complex;;Human;Q9NPB6,P36897,P37173;50855,7046,7048;MI:0007- anti tag coimmunoprecipitation | MI:0729- luminescence based mammalian interactome mapping;15761148;30.05.01.18.01,42.06,70.06;"PAR6 interacts directly with TGFBR1.";"";""
1782;TGF-beta receptor;;Mouse;Q64729,Q62312;21812,21813;MI:0007- anti tag coimmunoprecipitation;14612425;16.01,30.05.01.18.01,70.02;"Tgfbr1 and Tgfbr2 exist as homodimers on the cell surface and form a heterotetramer upon TGF-beta binding (PMID:7521335).";"";""
1783;TGF-beta receptor I-SMAD7-SMURF1 complex;;Mammalia;O15105,Q9HCE7,P36897;4092,57154,7046;MI:0007- anti tag coimmunoprecipitation;11278251;14.07.05,14.13.01.01,30.05.01.18.01,70.03;"SMAD7 associates with SMURF1 in the nucleus and is exported to the cytoplasm. Thus SMAD7 recruits SMURF1 to TGF-betaRI, resulting in the degradation of Tgf-betaRI. ";"";""
1784;RNF11-SMURF2-STAMBP complex;;Human;Q9Y3C5,Q9HAU4,O95630;26994,64750,10617;MI:0019- coimmunoprecipitation;14755250;14.13.01.01;"";"";""
1787;Nogo-potassium channel complex;;Human;P78357,Q09470,P16389,Q9NQC3;8506,3736,3737,57142;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;14592966;20.01.01.01,20.03.01.01,41.05.13,47.03.01.01,77.03.01.01;"Nogo-A is mainly localized at the gaps between Na+ and K+ channels along axons and its immunoreactivity is clearly located at sites where glial loops make contact with the axonal membrane surface in adult CNS. Nogo-A is a paranodal glial component.";"";""
1791;Nbr1-Sqstm1-Trim55 complex;;Rat;Q501R9,O08623,Q5PQN5;303554,113894,365751;MI:0096- pull down;15802564;45.03.12;"br1, p62, and MuRF2 proteins interacted in successive pairs in vitro and could be precipitated in a large complex from muscle tissue extracts, demonstrating their association in vivo.";"";""
1792;Lingo1-Rtn4r-Tnfrsf19 complex;;Mouse;Q9D1T0,Q99PI8,Q9JLL3;235402,65079,29820;MI:0019- coimmunoprecipitation;15694321;45.03.17;"TROY (also known as TAJ), a TNF receptor family member selectively expressed in the adult nervous system, can form a functional receptor complex with NgR and LINGO-1 to mediate cellular responses to myelin inhibitors.";"";""
1793;LINGO-1-Nogo-66-p75 signaling complex;;Human;Q96FE5,P08138,Q9BZR6;84894,4804,65078;MI:0019- coimmunoprecipitation | MI:0411- enzyme linked immunosorbent assay;14966521;18.01.07,18.02.05,41.05.13,73.03.13,75.03.17,77.03.01.01;"Triply transfected cells responded to OMgp by activating RhoA, but no activation occurred when binary pairs of NgR1/p75, LINGO-1/p75 or NgR1/LINGO-1 were tested.The binding of LINGO-1 to NgR1, p75 or to both together during CNS development or in response to injury, may modulate RhoA activation status in neurons, and thus control axon growth and extension.";"";""
1794;SORT1-NGFR complex;;Human;P08138,Q99523;4804,6272;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;14985763;16.01,70.03;"";"";""
1795;SORT1-NGFR-NGFB complex;;Human;P01138,P08138,Q99523;4803,4804,6272;MI:0030- cross-linking studies;14985763;40.10.02;"";"";""
5718;eNOS-HSP90-AKT complex, VEGF induced;;Human;P31749,P07900,P29474;207,3320,4846;MI:0006- anti bait coimmunoprecipitation;11425855;01.02.02.07,01.02.07.01,30.01.09.01,30.05.01.12,41.05.16,45.03.11;"VEGF stimulation promotes association of eNOS with HSP90 and AKT. ";"";""
1804;Smurf1-Par6 complex;;Mouse;Q9Z101,Q9CUN6;56513,75788;MI:0007- anti tag coimmunoprecipitation;15761148;14.07.05,42.06,45.03.09,70.03;"The amount of SMURF1-PAR6 complex increases after treatment of the cells with TGF-beta.  This complex is involved in epithelial-to-mesenchymal transition (EMT) process.";"";""
1810;ITGA4-PXN-GIT1 complex;;Human;Q9Y2X7,P13612,P49023;28964,3676,5829;MI:0004- affinity chromatography technologies;15793570;18.02,34.05.01;"";"";""
1812;AXIN-MEKK4-CCD1 complex;;Human;O15169,Q155Q3,Q9Y6R4;8312,85458,4216;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors analyzed that Ccd1 uses its coiled-coil domain to interact with MEKK4 and the DIX domain to interact with Axin, forming a ternary complex.";"";""
1813;MAD1L1 homodimer complex;;Human;Q9Y6D9;8379;MI:0018- two hybrid;9546394;10.03.01.03,70.05;"";"";""
1814;MAD1L1-MAD2L1 complex;;Human;Q9Y6D9,Q13257;8379,4085;MI:0071- molecular sieving;15694304;10.03.01.03;"The closed Mad2 bound to Mad1 represents a template for the conversion of open Mad2 into closed Mad2 bound to Cdc20. ";"";""
1816;JUN-TCF4-CTNNB1 complex;;Human;P35222,P05412,P15884;1499,3725,6925;MI:0096- pull down;16007074;30.05.02.20,30.07;"";"";""
1826;SMAD3-HEF1-APC10-CDH1 complex;;Human;Q9UM13,P12830,Q14511,P84022;10393,999,4739,4088;MI:0007- anti tag coimmunoprecipitation;15144564;14.13.01.01,30.05.01.18.01,70.03;"SMAD3 regulates the proteosomal degradation of its interacting proteins via recruiting the cell-cycle linked E3 ligase APC. SMAD3 interaction with APC10 is regulated by TGF-beta type I receptor activation.";"";""
1827;PML-SMAD2/3-SARA complex;;Human;P29590,Q15796,P84022,O95405;5371,4087,4088,9372;MI:0007- anti tag coimmunoprecipitation;15356634;30.05.01.18.01,70.03;"PML is essential for the formation of a stable and functional SARA-SMAD2/3complex. PML may function as a bridging factor between SARA and SMAD2/3. ";"Promyelocytic leukaemia";""
1828;TGF-beta receptor I-Axin-SMAD3 complex;;Human;O15169,P84022,P36897;8312,4088,7046;MI:0007- anti tag coimmunoprecipitation;11438668;30.05.01.18.01,70.03;"Phosphorylation of SMAD3 by TGF-betaRI is faciliated in the presence of Axin. In the absence of ligand stimulation, Axin was colocalized with Smad3 in the cytoplasm in vivo. Upon receptor activation, Smad3 was strongly phosphorylated by TGF-beta type I receptor (TGF-betaRI) in the presence of Axin, and dissociated from TGF-betaRI and Axin.";"";""
1829;SMAD3-VDR complex;;Mouse;Q8BUN5,P48281;17127,22337;MI:0007- anti tag coimmunoprecipitation;10224044;11.02.03.04,30.01.11,30.05.01.18.01,70.10;"SMAD3 acts as coactivator of VDR and positively regulates vitamin D signaling pathway. SMAD7 inhibits the formation of the SMAD3-VDR complex.";"";""
1830;Smad3-Hdac-Runx2 complex;;Rat;Q99P99,Q5RJZ2,Q9Z2J9,P84025;363287,84580,367218,25631;MI:0007- anti tag coimmunoprecipitation;15990875;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,30.05.01.18.01,42.10.03,43.03.17,70.10,73.03.17;"Activated SMAD3 recruits HDAC5 to Runx2 and stabilizes the HDAC/Runx2 complex.  TGF-beta inhibits osteoblast differentiation through inhibition of the function of Runx2 by Smad3.";"";""
1831;PIAS3-SMAD3-P300 complex;;Human;Q09472,Q9Y6X2,P84022;2033,10401,4088;MI:0007- anti tag coimmunoprecipitation;14691252;10.01.09.05,11.02.03.04.01,14.07.04,16.03.01,30.05.01.18.01,42.10.03,70.10;"TGF-beta treatment increases the complex formation.";"";""
1834;ITGAE-ITGB7-CDH1 complex; integrin complex;Human;P12830,P38570,P26010;999,3682,3695;MI:0019- coimmunoprecipitation;10837471;14.10;"";"";""
1839;SDCBP-CTNNB1-CTNNA1-CDH1 complex;;Dog;P12830,P35221,P35222,O00560;999,1495,1499,6386;MI:0019- coimmunoprecipitation;11179419;42.06;"";"";"Since  CDH1, CTNNA1, CTNNB1 and SDCBP from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from human were used."
1843;EB1-APC-mDia2 complex;;Mouse;Q61315,Q9Z207,Q61166;11789,56419,13589;MI:0096- pull down;15311282;34.05.01,42.04.05,70.04.05,73.03.17;"The authors showed that EB1 and APC interacted with mDia directly, through domains that were distinct from those that interact with each other.";"";""
1844;APC-IQGAP1 complex;;Mammalia;P25054,P46940;324,8826;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;15572129;34.05.01,42.04,70.04,73.03.17;"The authors demonstrate that the amount of IQGAP1 is about 20 times more than that of APC, and that the armadillo repeats of APC are responsible for the interaction with IQGAP1.";"";""
1845;APC-IQGAP1-CLIP-170 complex;;Mammalia;P25054,P30622,P46940;324,6249,8826;MI:0006- anti bait coimmunoprecipitation;15572129;34.05.01,42.04,70.04,73.03.17;"";"";""
1847;Axin-GSK-3-beta-beta-catenin complex;;Mammalia;O70239,Q9WU82,P18266;79257,84353,84027;MI:0096- pull down | MI:0007- anti tag coimmunoprecipitation;9482734;30.05.02.20;"The results show that GSK-3b, rAxin and b-catenin form a ternary complex in intact cells and that GSK-3b and b-catenin interact with separate sites on rAxin.";"";""
1851;BUB1-BUB3 complex;;Human;O43683,O43684;699,9184;MI:0019- coimmunoprecipitation;15525512;14.07.03;"Bub1-Bub3 phosphorylated Cdc20. Bub1 alone also efficiently phosphorylated Cdc20, indicating that Bub3 is not required for this process.";"";""
1856;CDCA5-PDS5A-RAD21-SMC1A-PDS5B-SMC3 complex;;Human;Q96FF9,Q29RF7,Q9NTI5,O60216,Q14683,Q9UQE7;113130,23244,23047,5885,8243,9126;MI:0004- affinity chromatography technologies;15837422;10.03.01.01;"";"";""
1863;TSG101-VPS37B-VPS28 complex;;Human;Q99816,Q9UK41,Q9H9H4;7251,51160,79720;MI:0019- coimmunoprecipitation;15218037;14.04;"";"";""
1867;ERC2-RIMS1-UNC13B complex;;Rat;Q8K3M6,Q9JIR4,Q62769;259269,84556,64830;MI:0019- coimmunoprecipitation;12163476;34.03.01,77.03.01.01.01;"";"";""
1873;SNARE complex (Snap25, Syt1, Unc13b, Vamp2, Stx1b2, Stx1a);;Rat;P60881,P32851,P61265,P21707,Q62769,P63045;25012,116470,24923,25716,64830,24803;MI:0019- coimmunoprecipitation | MI:0027- cosedimentation;8999968;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1874;SNARE complex (SNAP25, VAMP3, VAMP2, NAPB, STX13);;Human;Q9H115,P60880,Q86Y82,P63027,Q15836;63908,6616,23673,6844,9341;MI:0019- coimmunoprecipitation;9817754;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ";"";"Entrez Gene says that stx12 is synonym to stx13."
1875;STX12-SNAP25-HGS-VAMP2 complex;;Rat;Q9JJ50,P60881,O88385,P63045;56084,25012,65033,24803;MI:0004- affinity chromatography technologies;12847087;42.22;"";"";""
1876;SNARE complex (Stx4, Napa, Vamp3, Nsf, Vamp2);;Rat;P54921,Q9QUL6,Q08850,P63045,P63025;140673,60355,81803,24803,29528;MI:0019- coimmunoprecipitation;8973549;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1879;Nsf-Stx1a-NAPB complex;;Rat;P85969,Q9QUL6,P32851;499903,60355,116470;MI:0019- coimmunoprecipitation;1315316;20.09.07.27,20.09.16.09.05,77.03.11.07;"";"";""
1880;SNARE complex (Stx1a, Napa, Snap25, Vamp2, Nsf);;Rat;P54921,Q9QUL6,P60881,P32851,P63045;140673,60355,25012,116470,24803;MI:0019- coimmunoprecipitation;9267032;20.09.07.27,20.09.16.09.05,75.03.04;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
1883;Stx7-Vti1b-Vamp8-Stx8 complex;;Rat;O70257,Q9Z2Q7,Q9WUF4,P58200;60466,59074,83730,366673;MI:0114- x-ray crystallography;11786915;20.09.07.27;"";"";""
1890;ELK1-SRF-ELK4 complex;;Human;P19419,P28324,P11831;2002,2005,6722;MI:0413- electrophoretic mobility shift assay;7540136;11.02.03.04;"";"";""
1893;mTOR-RICTOR complex;;Human;P42345,Q9BVC4,Q6R327;2475,64223,253260;MI:0006- anti bait coimmunoprecipitation;15268862;30.01.05.01,40.01,42.04.03;"The authors found that the rictor-mTOR complex modulates the phosphorylation of Protein Kinase C alpha (PKCalpha) and the actin cytoskeleton. The rictor-mTOR complex is insensitive to rapamycin.  ";"";""
1895;RICTOR-mTOR complex;;Human;P42345,Q9BVC4,Q8N6M7;2475,64223,253260;MI:0019- coimmunoprecipitation;15718470;14.07.03;"Rictor-mTOR may serve as a drug target in tumors that have lost the expression of PTEN.";"";""
1897;RAPTOR-mTOR complex;;Human;P42345,Q9BVC4,Q8N122;2475,64223,57521;MI:0019- coimmunoprecipitation;15718470;14.07.03;"";"";""
1899;NTF4 homodimer complex;;Human;P34130;4909;MI:0114- x-ray crystallography;10631974;43.03.13;"The structures of the neurotrophin homodimers reveals common features that may be important in the binding between the neurotrophins and their receptors.";"";""
1900;PSD-95-TrkB complex;;Rat;P31016,P35439,Q63604,P10686,Q5M824;29495,24408,25054,25738,85385;MI:0019- coimmunoprecipitation;15665879;30.01.09.07,30.05.01.12,34.03.03,41.05.13.01,43.03.13,47.03.01.01,73.03.13,77.03.01.01;"The authors show that cAMP modulates TrkB signaling in two ways: cAMP gates BDNF-induced TrkB phosphorylation and cAMP facilitates the distribution of TrkB into the PSD in the spines of hippocampal neurons. They propose that cAMP gating occurs at the TrkB receptor level, rather than at intracellular signaling molecules.";"";""
1901;Drd1-Nmdar1 complex;;Rat;P18901,P35439;24316,24408;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down | MI:0012- bioluminescence resonance energy transfer;12646556;14.04,34.03,70.02,70.08,73.03.13,77.03.01.01.01;"The authors describe that this interaction is constitutive, occurs in the endoplasmic reticulum (ER), influences D1 receptor targeting to the cell membrane, and prevents agonist-induced D1 receptor internalization. The experiments suggest that D1 and NMDA receptors are assembled as oligomeric units in the ER and transported to the  cell surface as a preformed complex.";"";""
5719;eNos3-Calmodulin complex;;Rat;P62161,Q62600;24244,24600;MI:0006- anti bait coimmunoprecipitation;9856995;01.02.07.01,30.01.09.01,30.01.09.03;"";"";""
1907;NMDA receptor complex (NR2B, NR1, PSD-95, SynGAP, CaMK-II);;Rat;P11275,P31016,P35439,Q00960,Q9QUH6;25400,29495,24408,24410,192117;MI:0019- coimmunoprecipitation;15924861;14.04,20.03.01.01,30.01.05.05.01,30.05.02.24.05,30.07,34.03,70.02,73.03.13,77.03.01.01.01;"The authors analyse the links between NMDAR subtypes, Ras-ERK signaling, and AMPAR trafficking. They find that NR2A and NR2B have antagonistic actions on Ras-ERK activation and AMPAR distribution in mature neurons. NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expression of GluR1 - primarily by regulating GluR1 surface insertion. Coimmunoprecipitation done with NR2B antibody after depletion of NR2A.";"";""
1908;NMDA receptor complex (NR2A, NR2B, NR1, PSD-95, SynGAP, CaMK-II);;Rat;P11275,P31016,P35439,Q00959,Q00960,Q9QUH6;25400,29495,24408,24409,24410,192117;MI:0019- coimmunoprecipitation;15924861;14.04,20.03.01.01,30.01.05.05.01,30.05.02.24.05,30.07,34.03,70.02,73.03.13,77.03.01.01.01;"The authors analyse the links between NMDAR subtypes, Ras-ERK signaling, and AMPAR trafficking. They find that NR2A and NR2B have antagonistic actions on Ras-ERK activation and AMPAR distribution in mature neurons. NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expression of GluR1 - primarily by regulating GluR1 surface insertion.";"";""
1909;APC-DLG4 complex;;Human;P25054,P78352;324,1742;MI:0019- coimmunoprecipitation;9326658;34.05.01,40.01;"";"";""
1913;GluR delta-2 complex, postsynaptic (GluR delta-2, Shank1, Shank2, mGluR1 alpha, Homer, PSD-95);;Mouse;Q62108,Q61625,P97772,Q9Z2Y3,Q9WV48,Q80Z38;13385,14804,14816,26556,78957,210274;MI:0006- anti bait coimmunoprecipitation;15207857;20.03.01.01,34.03.01,41.05.13.01,73.03.13,77.03.01.01.01.02;"The immunoprecipitation experiments with SPM (synaptosomal plasma membrane) fractions of cerebella showed that GluR delta-2 formed the postsynaptic protein complex with Homer and mGluR1 alpha in vivo. The authors suppose that it is likely that GluR delta-2-Shank complex interacted with mGluR1 alpha via Homer.";"";"Since Shank1 from mouse was not available in the UniProt database at the time of annotation, the orthologous protein from rat was used. "
1914;KIF1B-alpha-PSD-95-SAP-97-S-SCAM complex;;Rat;Q62696,P31016,O88658,O88382;25252,29495,117548,113970;MI:0006- anti bait coimmunoprecipitation;12097473;14.04,20.09.14,34.05.02,73.03.13,77.03.01.01.01;"The results demonstrated that KIF1B-alpha , unlike the dendrite-specific KIF17, is widely distributed in both dendrites and axons along with SAP97 and S-SCAM, and biochemically associates with SAP97 and S-SCAM. The authors suggest that the PSD-95 family proteins and S-SCAM have a novel function as KIF1B-alpha  receptors, linking KIF1B-alpha  to its specific cargos, and are involved in peripheral neuropathies.";"KIF1B is involved in Charcot-Marie-Tooth disease type 2A (CMT2A). ";""
5707;Ternary complex (Abl1, Dok1, Nck1);;Mouse;P00520,P97465,Q8BMV0;11350,13448,17973;MI:0019- coimmunoprecipitation;15148308;42.04.03,43.03.17;"Mouse fibroblasts lacking c-Abl, Dok1, or Nck had fewer filopodia than cells reexpressing the product of the disrupted gene. Dok1 and c-Abl were both detected in filopodia of spreading cells, and therefore may act locally to modulate actin. The data suggest a novel pathway by which c-Abl transduces signals to the actin cytoskeleton through phosphorylating Dok1 Y361 and recruiting Nck.";"";""
1923;CaMKII-densin180-NR2B-(alpha)actinin-2 complex;;Rat;Q9JI91,P11275,Q00960,P70587;11472,25400,24410,117284;MI:0006- anti bait coimmunoprecipitation;16120608;30.01.09.03,77.03.01.01.01;"";"";"Since Actn2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
1926;Foxh1-Nkx2-5 complex;;Mouse;O88621,P42582;14106,18091;MI:0402- chromatin immunoprecipitation assays;15363409;45.03.12.03;"Foxh1 and Nkx2-5 functionally interact and are essential for development of the anterior heart field (AHF) and its derivatives, the right ventricle (RV) and outflow tract (OFT), in response to TGFbeta-like signals.";"";""
1927;PKD2-PACS1 complex;;Human;Q6VY07,Q13563;55690,5311;MI:0019- coimmunoprecipitation;15692563;20.03.01.01;"";"Mutations of PKD2, a member of the TRP family of cation channels, cause autosomal dominant polycystic kidney disease.";""
5721;CIN85-CBL-SH3GL2 complex;;Human;P22681,Q99962,Q96B97;867,6456,30011;MI:0019- coimmunoprecipitation;11894095;20.09.07.25,20.09.18.09.01;"Endogenous or overexpressed Cbl co-precipitated with endophilin A1 only in the presence of CIN85, indicating that CIN85 acts as a linker between Cbl and endophilins.";"";""
1932;NEK2-NEK11 complex;;Human;Q8NG66,P51955;79858,4751;MI:0019- coimmunoprecipitation;15161910;10.03.01.02;"";"";""
5713;SH3P2/OSTF1-CBL-SRC complex;;Human;P22681,Q92882,P12931;867,26578,6714;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;15135048;34.07,70.04.03;"";"";""
1937;Olfr992-Rtp1 complex;;Mouse;Q8VGC6,Q8C8C1;258865,239766;MI:0019- coimmunoprecipitation;15550249;18.02.07;"These protein are associated with OR proteins and enhance the OR responses to odorants.";"";""
1938;Olfr992-Reep1 complex;;Mouse;Q8VGC6,Q8BGH4;258865,52250;MI:0019- coimmunoprecipitation;15550249;18.02.07;"These protein are associated with OR proteins and enhance the OR responses to odorants.";"";""
1941;Sirpa-Pik3cg complex;;Mouse;Q9JHG7,P97797;30955,19261;MI:0004- affinity chromatography technologies;15797027;18.01.07;"Binding of p84 to p110(gamma) substantially increases the ability of G(beta)(gamma) to stimulate phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P(3)) production both in vitro and in vivo.";"";""
1944;IRAK1-IRAK2 complex;;Human;P51617,O43187;3654,3656;MI:0019- coimmunoprecipitation;10383454;36.25.16.01;"";"";""
1945;IRAK1-IRAK3 complex;;Human;P51617,Q9Y616;3654,11213;MI:0019- coimmunoprecipitation;10383454;36.25.16.01;"";"";""
1949;MAML2-RBP-Jkappa-Notch1 complex;;Mammalia;Q7TPU6,P46531,P31266;270118,4851,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
1957;DAP12 signaling homodimer complex;;Human;O43914;7305;MI:0019- coimmunoprecipitation;15845448;30.05.01.12;"";"";""
5716;eNOS-HSP90 complex, VEGF induced;;Human;P07900,P29474;3320,4846;MI:0006- anti bait coimmunoprecipitation;11425855;01.02.02.07,01.02.07.01,30.01.09.01,30.05.01.12,41.05.16,45.03.11;"VEGF stimulation promotes dissociation of eNOS and Caveolin and association of eNOS with HSP90. ";"";""
1970;BMP4-TWSG1 complex;;Human;P12644,Q9GZX9;652,57045;MI:0019- coimmunoprecipitation;15775969;30.05.01.18;"";"";""
1972;BMP4-BGN complex;;Human;P21810,P12644;633,652;MI:0019- coimmunoprecipitation;15775969;30.07;"";"";""
1975;GT198 homodimer complex;;Rat;Q91ZY6;140938;MI:0004- affinity chromatography technologies | MI:0018- two hybrid;11739747;30.01.09.08,70.10;"GT198 contains a leucine zipper required for its dimerization. As many nuclear receptors act as dimers on hormone response elements, the dimerization of GT198 might be important for the action on the DBD of nuclear receptors.";"";""
1976;MTNR1A homodimer complex;;Human;P48039;4543;MI:0019- coimmunoprecipitation;15266022;16.01.01;"";"";""
1977;MTNR1B homodimer complex;;Human;P49286;4544;MI:0012 bioluminescence resonance energy transfer | MI:0019- coimmunoprecipitation;15266022;16.01.01;"";"";""
1978;MTNR1A-MTNR1B complex;;Human;P48039,P49286;4543,4544;MI:0012 bioluminescence resonance energy transfer | MI:0019- coimmunoprecipitation;15266022;16.01.01;"This heterodimers contain two functional ligand binding sites that maintain their respective selectivity for MT(1) and MT(2) ligands. Occupation of either binding site is sufficient to induce a conformational change within the heterodimer. Taken together, these results show that the probability of GPCR heterodimer formation may be equal to or even higher than that of the corresponding homodimers and that specific properties of heterodimers can be revealed using a BRET-based ligand/receptor interaction assay.";"";""
1982;CACY homodimer  complex;;Human;P06703;6277;MI:0027- cosedimentation;9578461;16.17.01,16.17.09;"";"";""
1983;Retn homohexamer  complex;;Mouse;Q99P87;57264;MI:0071- molecular sieving;15155948;01.05.25,01.08.02;"";"";""
1984;PEX14 homodimer complex;;Human;O75381;5195;MI:0030- cross-linking studies | MI:0018- two hybrid;12096124;14.10,42.19,70.19;"";"";""
1985;AIRE homodimer complex;;Human;O43918;326;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;10748110;11.02.03.04.01;"";"Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy is caused by mutations in the autoimmune regulator (AIRE) gene.";""
1986;Endoglin homodimer complex;;Human;P17813;2022;MI:0019- coimmunoprecipitation;15806144;30.07;"";"";""
1987;MYOM1 homodimer complex;;Human;P52179;8736;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0096- pull down;15571722;45.03.12,75.03.12;"";"";""
1988;Bcl2 homodimer complex;;Mouse;P10417;12043;MI:0019- coimmunoprecipitation;7609638;40.10.02.04;"";"";""
1989;BANF1 homodimer protein;;Human;O75531;8815;MI:0077- nuclear magnetic resonance;9783751;16.03.01,34.11.10;"";"";""
1990;PGRMC1-SCAP complex;;Human;O00264,Q12770;10857,22937;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;15782218;34.01.07,70.07;"";"";""
1991;PRMT2 homodimer complex;;Human;P55345;3275;MI:0096- pull down;12039952;18.02.07;"";"";""
1992;LEPR homodimer complex;;Human;P48357;3953;MI:0019- coimmunoprecipitation;9038364;40.02.03.01;"";"";""
1993;SLC1A2 homotrimer complex;;Human;P43004;6506;MI:0030- cross-linking studies;15483603;20.01.07;"";"";""
1995;Sgk3 homodimer complex;;Mouse;Q9ERE3;170755;MI:0114- x-ray crystallography | MI:0030- cross-linking studies;15126499;40.01;"";"";""
1997;Adiponectin homotrimer complex;;Mouse;Q60994;11450;MI:0071- molecular sieving;15558058;30.01.05.01.06;"";"";""
1998;Adiponectin homohexamer complex;;Mouse;Q60994;11450;MI:0071- molecular sieving;15558058;30.01.05.01.06;"";"";""
2000;BAX homo-oligomer complex;;Human;Q07812;581;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;15735709;40.10.02.03.01;"Arsenic trioxide  As(2)O(3) treatment triggered Bax conformational change and subsequent translocation from cytosol to mitochondria to form various multimeric homo-oligomers in IM-9 cells.";"";"Oligomer"
2001;NOD1 homodimer complex;;Human;Q9Y239;10392;MI:0114- x-ray crystallography;18186648;30.01.05.01.04,36.25.16.07;"";"";""
2003;COX1 homodimer complex;;Human;P23219;5742;MI:0114- x-ray crystallography;11318639;01.06.02,70.03;"";"";""
2004;C1D homodimer protein;;Human;Q13901;10438;MI:0019- coimmunoprecipitation;11801738;14.10;"Only the dimeric but not the monomeric form of C1D can interact with TRAX protein. The finding that the SDS-resistant homodimers of C1D and TRAX interact only after gamma-irradiation may indicate that a post-translational modification is required for the interaction. ";"";""
2005;PTPRA homodimer complex;;Human;P18433;5786;MI:0030- cross-linking studies | MI:0055- fluorescent resonance energy transfer;11401727;16.01.01,30.05.01;"RPTPalpha dimerized constitutively in living cells, which may be mediated by the transmembrane domain, providing strong support for the model that dimerization is involved in regulation of RPTPs.";"";""
2006;Ptpra homodimer complex;;Mouse;P18052;19262;MI:0030- cross-linking studies;10913175;18.02.01.02,70.03;"Based on surface cross-linking studies, the authors provide the first evidence that RPTPalpha homodimerizes efficiently on the cell surface via multiple domains, suggesting that dimerization-mediated negative regulation of RPTPalpha biological activity is likely to be physiologically relevant.";"";""
2007;PRNP homo-oligomer complex;;Human;P04156;5621;MI:0276- blue native page;16148934;43.03.13,73.03.13;"The non-fibrillar particles, with masses equivalent to 14-28 PrP molecules, are the most efficient initiators of TSE disease.";"";"Oligomer"
2008;Prnp homodimer complex;;Mouse;P04925;19122;MI:0019- coimmunoprecipitation;7609638;43.03.13;"";"";""
2009;Birc6 homodimer complex;;Mouse;Q69ZM5;12211;MI:0019- coimmunoprecipitation;15200957;;"It seems possible that only homodimerized full-length BRUCE possesses IAP activity and that the conformation of the 70 kDa dimer renders it inactive. ";"";""
2010;AXL homodimer complex;;Human;P30530;558;MI:0018- two hybrid;12470648;16.01.01,30.05.01.12,70.02;"";"";""
2013;STAT5B homodimer complex;;Human;P51692;6777;MI:0413- electrophoretic mobility shift assay;10594041;11.02.03.04.01;"";"";""
2014;Whrn homodimer complex;;Mouse;Q80VW5;73750;MI:0019- coimmunoprecipitation;15590698;43.03.23,47.03.02.01;"";"";""
2016;IL12A homodimer complex;;Human;P29459;3592;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;7527811;43.03.07.02.01.02;"";"";""
2018;IL12A-IL12B complex;;Human;P29459,P29460;3592,3593;MI:0114- x-ray crystallography;10899108;30.05.01.05;"";"";""
2019;IL12A-IL12B-IL12RB1 complex;;Human;P29459,P29460,P42701;3592,3593,3594;MI:0027- cosedimentation | MI:0099-  scintillation proximity assay;9498755;30.05.01.05;"";"";""
2020;IL12B-IL12RB1-IL12RB2 complex;;Human;P29460,P42701,Q99665;3593,3594,3595;MI:0019- coimmunoprecipitation;7527811;43.03.07.02.01.02;"IL12B (p40) homodimer  was capable of competing with IL-12 heterodimer in binding to the IL12R on T cells but was unable to cause cellular proliferation. Furthermore, p40 homodimer inhibited IL-12-induced T cell proliferation.";"";""
2021;IL12A-IL12B-IL12RB2 complex;;Human;P29459,P29460,Q99665;3592,3593,3595;MI:0027- cosedimentation | MI:0099- scintillation proximity assay;9498755;30.05.01.05;"";"";""
2022;Stat5a-Jak2 complex;;Mouse;Q62120,P42230;16452,20850;MI:0019- coimmunoprecipitation;9834069;43.03.07.02.01.02;"The phosphorylation of STAT5 associated with JAK2 was found to be induced in the absence of JAK3 activation. ";"";""
2023;STAT5A homodimer complex;;Human;P42229;6776;MI:0413- electrophoretic mobility shift assay;10594041;11.02.03.04.01;"";"";""
2024;Agtr1a-Jak2 complex;;Mouse;P29754,Q62120;11607,16452;MI:0019- coimmunoprecipitation;15146194;18.02.01;"Mechanical stretch induces association of the AT1 receptor with Janus kinase 2, and translocation of G proteins into the cytosol.";"";""
2026;IL12RB1-IL12RB2 complex;;Human;P42701,Q99665;3594,3595;MI:0019- coimmunoprecipitation;8943050;30.05.01.05,70.02;"";"";""
2028;JAK2-IL12RB2 complex;;Human;Q99665,O60674;3595,3717;MI:0019- coimmunoprecipitation;9038232;30.05.01.05;"";"";""
2029;BNIP2-ARHGAP8 complex;;Human;P85298,Q12982;23779,663;MI:0019- coimmunoprecipitation | MI:0096- pull down;12944407;18.02.01.01.01;"";"";""
2034;Apaf1 homo-oligomer complex;;Mouse;O88879;11783;MI:0071- molecular sieving;15907471;40.10.02.04;"";"";"Oligomer"
2051;MALT1 oligomer complex;;Human;Q9UDY8;10892;MI:0019- coimmunoprecipitation;15125833;18.02.01.01,73.03.07.02.01;"TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by MALT1 and BCL10 in lymphocytes. Only oligomers of MALT1 and BCL10 can activate IKK in vitro. MALT1 oligomers bind to TRAF6, induce TRAF6 oligomerization, and activate the ligase activity of TRAF6 to polyubiquinate NEMO. These results reveal an oligomerization-ubiquination-phosphorylation cascade that culminates in NF-kappaB activation in T lymphocytes.";"";""
2052;BCL10 oligomer complex;;Human;O95999;8915;MI:0019- coimmunoprecipitation;15125833;18.02.01.01,73.03.07.02.01;"TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by MALT1 and BCL10 in lymphocytes. Only oligomers of MALT1 and BCL10 can activate IKK in vitro.";"";""
2053;BCL10-MALT1 complex;;Human;O95999,Q9UDY8;8915,10892;MI:0019- coimmunoprecipitation;15125833;18.02.01.01,73.03.07.02.01;"BCL10 binds to the Ig domains of MALT1 and promotes MALT1 oligomerization.";"";""
2054;CASP8-FADD-MALT1-BCL10 complex;;Human;O95999,Q14790,Q13158,Q9UDY8;8915,841,8772,10892;MI:0019- coimmunoprecipitation;15746428;11.02.03.04.01;"";"";""
2055;CASP8-CHUK-IKBKB-MALT1-BCL10 complex;;Human;O95999,Q14790,O15111,O14920,Q9UDY8;8915,841,1147,3551,10892;MI:0019- coimmunoprecipitation;15746428;11.02.03.04.01;"";"";""
2056;BCL10-CHUK-BCL10-IKBKB complex;;Human;O95999,Q14790,O15111,O14920;8915,841,1147,3551;MI:0019- coimmunoprecipitation;15746428;11.02.03.04.01;"";"";""
2073;TNFRSF11A-TRAF6-SRC complex;;Human;P12931,Q9Y6Q6,Q9Y4K3;6714,8792,7189;MI:0007- anti tag coimmunoprecipitation;10635328;30.01.05.01.05;"";"";""
2074;TRAF6 oligomer complex;;Human;Q9Y4K3;7189;MI:0019- coimmunoprecipitation;15125833;18.02.01.01,73.03.07.02.01;"MALT1 oligomers bind to TRAF6, induce TRAF6 oligomerization, and activate the ligase activity of TRAF6 to polyubiquinate NEMO. These results reveal an oligomerization-ubiquination-phosphorylation cascade that culminates in NF-kappaB activation in T lymphocytes.";"";""
2077;B-raf-MAP3K11 complex;;Human;Q9NY11,Q16584;6635,4296;MI:0019- coimmunoprecipitation;15258589;30.01.05;"MLK3 and B-Raf form a complex in vivo.";"";""
2084;NFKB1-NFKB2-REL-RELA-RELB complex;;Human;P19838,Q00653,Q04864,Q04206,Q01201;4790,4791,5966,5970,5971;MI:0413- electrophoretic mobility shift assay;15782119;11.02.03.04;"";"";""
2086;NFKB1-NFKB2-RELA-RELB complex;;Human;P19838,Q00653,Q04206,Q01201;4790,4791,5970,5971;MI:0413- electrophoretic mobility shift assay;15782119;11.02.03.04;"";"";""
5723;Cbl-Cd2ap-Flt1 complex;;Mouse;P22682,Q9JLQ0,P35969;12402,12488,14254;MI:0006- anti bait coimmunoprecipitation;15001553;14.07.05,20.09.18.09.01,30.05.01.12,41.05.16,70.09;"After VEGF stimulation the Cbl-Cda2p complex binds to activated Flt-1 and plays a crucial role in endocytosis and subsequent ubiquitination of Flt-1.";"";""
2100;CHUK-IKBKB-MAP3K14 complex;;Human;O15111,O14920,Q99558;1147,3551,9020;MI:0019- coimmunoprecipitation;9346485;18.02.01;"";"";""
2101;IKKA-IKKB complex;;Human;O15111,O14920;1147,3551;MI:0019- coimmunoprecipitation;9346485;18.02.01;"";"";""
2104;IKKB-NIK complex;;Human;O14920,Q99558;3551,9020;MI:0019- coimmunoprecipitation;9346485;18.02.01;"";"";""
2105;IkappaB kinase complex (IKBKB, CHUK, IKBKAP, NFKBIA, RELA, MAP3K14);;Human;O15111,O95163,O14920,Q99558,P25963,Q04206;1147,8518,3551,9020,4792,5970;MI:0019- coimmunoprecipitation;9751059;30.01.05.01.04,30.07;"";"";""
2112;CDC37-HSP90AA1-HSP90AB1-MAP3K11 complex;;Human;Q16543,P07900,P08238,Q16584;11140,3320,3326,4296;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;15001580;18.02.01;"MLK3 associates with Hsp90/p50(cdc37) through its catalytic domain in an activity-independent manner.";"";""
2118;CHUK-ERC1-IKBKB-IKBKG;;Human;O15111,Q8IUD2,O14920,Q9Y6K9;1147,23085,3551,8517;MI:0019- coimmunoprecipitation;15218148;30.01.05.01.04;"ELKS may contribute an important oligomerization interface to members of the IKK complex as well as to other upstream or downstream regulators of NF-kappaB transcriptional activity, such as I(kappa)B(alpha).  ";"";""
2120;Chuk-Ikbkb-Ikbkg complex;;Mouse;Q60680,O88351,O88522;12675,16150,16151;MI:0019- coimmunoprecipitation;15479644;45.03.12;"";"";""
2121;CHUK-IKBKB-IKBKG complex;;Human;O15111,O14920,Q9Y6K9;1147,3551,8517;MI:0019- coimmunoprecipitation;9751060;18.02;"";"";""
2123;IKBKG homodimer complex;;Human;Q9Y6K9;8517;MI:0018- two hybrid | MI:0030- cross-linking studies;12435599;18.02.01;"KK-gamma forms homodimer and homotrimer both in vitro and in yeast or mammalian cells through a C-terminal domain comprising amino acids 251-419.";"";""
2124;IKK-alpha--ER-alpha-AIB1 complex;;Human;O15111,P03372,Q9Y6Q9;1147,2099,8202;MI:0006- anti bait coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;15808510;11.02.03.04,14.07.03,16.03.01,30.01.11;"The authors showed that in estradiol-stimulated MCF7 cells, the association of both ER-alpha and AIB1/SRC-3 with IKK-alpha bound to the cyclin D1 promoter was markedly increased in an estrogen-dependent manner. Further siRNA experiments showed that IKK-alpha contributes to the estrogen-mediated phosphorylation of both ER-alpha and AIB1/SRC-3.";"";""
2129;DNAJB2-HSPA8-PSMA3 complex;;Human;P25686,P11142,P25788;3300,3312,5684;MI:0019- coimmunoprecipitation;15936278;14.04,14.13.01.01;"";"";""
2142;Map2k5-Map3k3 complex;;Mouse;Q9WVS7,Q61084;23938,26406;MI:0019- coimmunoprecipitation;12912994;30.01.05.01,30.07;"";"";""
2143;MAP2K5-PRKCI-SQSTM1 complex;;Human;Q13163,P41743,Q13501;5607,5584,8878;MI:0019- coimmunoprecipitation;12813044;30.01.05.01,30.07;"";"";""
2145;HSF1-YWHAE complex;;Human;Q00613,P62258;3297,7531;MI:0004- affinity chromatography technologies | MI:0096- pull down;15364926;32.01.05;"";"";""
2147;Aip-Hsp90-Ahr complex;;Mouse;P30561,O08915,P11499;11622,11632,15516;MI:0018- two hybrid | MI:0019- coimmunoprecipitation;9083006;11.02.03.04,14.04,70.03;"The authors suggest that AIP influences ligand receptivity and/or nuclear targeting of AhR.";"";""
2149;Arnt-Sim2 complex;;Mouse;P53762,Q61079;11863,20465;MI:0019- coimmunoprecipitation;11782478;11.02.03.04;"The murine SIM factors, in combination with ARNT, attenuate transcription from the hypoxia-inducible erythropoietin (EPO) enhancer during hypoxia.";"";""
2151;Arnt-Sim1 complex;;Mouse;P53762,Q61045;11863,20464;MI:0019- coimmunoprecipitation;11782478;01.02.03.04;"The murine SIM factors, in combination with ARNT, attenuate transcription from the hypoxia-inducible erythropoietin (EPO) enhancer during hypoxia.";"";""
2152;ARNT-HLF complex;;Human;P27540,Q16534;405,3131;MI:0019- coimmunoprecipitation;9113979;11.02.03.04.01;"";"";""
2153;ITGAM-ITGB2-CD11 complex; integrin complex;Human;P08962,P11215,P05107;967,3684,3689;MI:0019- coimmunoprecipitation;8871662;30.07,34.07,73.03.07;"";"";""
2156;YBX1-AKT1 complex;;Human;P31749,P67809;207,4904;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;15806160;40.01.05,70.10;"";"Akt and YB-1 work together to promote the growth and possibly the development of breast tumors.";""
2159;AR-AKT-APPL complex;;Human;P31749,Q9UKG1,P10275;207,26060,367;MI:0007- anti tag coimmunoprecipitation;12621049;30.01.11;"The authors  suggest that APPL, Akt, and AR may exist in a complex and Akt may serve as an important bridge factor for the association of APPL with AR. They demonstrated that the APPL·AR complex was not clearly seen, and that the addition of Akt markedly enhanced APPL·AR complex formation.";"";""
2160;AOF2-AR complex;;Human;O60341,P10275;23028,367;MI:0019- coimmunoprecipitation;16079795;11.02.03.04.01;"The androgen receptor and LSD1 form chromatin-associated complexes in a ligand-dependent manner. LSD1 co-localizes with the androgen receptor in normal human prostate and prostate tumour. ";"";""
2162;APPBP1-UBA3 complex;;Human;Q13564,Q8TBC4;8883,9039;MI:0114- x-ray crystallography;12646924;14.07.05;"The APPBP1-UBA3 complex initiates NEDD8 conjugation by first catalyzing adenylation of the C terminus of NEDD8 and ultimately catalyzing transfer of NEDD8 to the downstream enzyme in the pathway, Ubc12 (PMID:16275315).";"";""
2169;Ubiquitin E3 ligase (Neurl2, Tceb1, Tceb2, Cul5, Rbx1);Ozz-E3;Mouse;Q9D5V5,Q9D0S4,P62878,P83940,P62869;75717,415115,56438,67923,67673;MI:0019- coimmunoprecipitation;14960280;14.07.05,14.13.01.01,45.03.12.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. In the differentiating myofibers, the RING-type ubiquitin E3 ligase (containing Neurl2, Tceb1, Tceb2, Cul5 and Rbx1) regulates the levels of sarcolemma-associated beta-catenin by mediating its degradation via the proteasome. Expression of beta-catenin mutants that reduce the binding of Ozz to endogenous beta-catenin leads to Mb-beta-catenin accumulation and myofibrillogenesis defects similar to those observed in Ozz null myocytes.";"";""
2170;Ubiquitin E3 ligase (CDC34, CUL1, RBX1);;Human;P49427,Q13616,P62877;997,8454,9978;MI:0007- anti tag coimmunoprecipitation;11675391;14.07.05,14.13.01.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The conjugation of Nedd8 to the ROC1-CUL1 complex selectively stimulates Cdc34-catalyzed Lys48-linked multiubiquitin chain assembly.";"";""
2171;Ubiquitin E3 ligase (CHEK1, CUL4A);;Human;O14757,Q13619;1111,8451;MI:0019- coimmunoprecipitation;16137618;14.07.05,14.13.01.01,32.01.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The Chk1 kinase is a major effector of S phase checkpoint signaling during the cellular response to genotoxic stress. Replicative stress induces the polyubiquitination and degradation of Chk1 in human cells.";"";""
2172;Ubiquitin E3 ligase (CDT1, DDB1, CUL4A, RBX1);;Human;Q9H211,Q13619,Q16531,P62877;81620,8451,1642,9978;MI:0019- coimmunoprecipitation;15448697;14.07.05,14.13.01.01,32.01.09;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The CDT1-DDB1-CUL4A complex was observed in an investigation of targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage.";"";""
2173;COP9 signalosome complex (CSN);;Mammalia;P61202,O35864,Q8VBV7,P56213,Q99LD4;12848,26754,108679,11692,209318;MI:0019- coimmunoprecipitation | MI:0276- blue native page;15304329;47.03.11.07,70.10,77.03.11.07;"CSN is a key player in the functional regulation of hepatopoietin (HPO). It also functions at the interface between signal transduction, ubiquitin-dependent proteolysis, and developmental control. ";"";"At the time of annotation, the members of the protein complex (green monkey) were not found in the UniProt database. The orthologous proteins from mouse were used."
2174;COP9 signalosome complex; JAB1-containing signalosome (GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7) | COP9 complex homolog;Human;P61201,Q9UNS2,Q9BT78,Q92905,Q7L5N1,Q99627,Q13098,(Q9UBW8,Q9H9Q2);9318,8533,51138,10987,10980,10920,2873,(50813,64708);MI:0047- far western blotting;9535219;11.02.03.04,30,34.11.01;"The purified complex is very similar, if not identical,  to the plant COP9 complex involved in light-mediated signal transduction. A regulating transcriptional activity is discussed.";"";""
2179;CNS-P53 complex;;Human;P61201,Q9UNS2,Q9BT78,Q92905,Q7L5N1,Q9UBW8,Q99627,Q13098,P04637;9318,8533,51138,10987,10980,50813,10920,2873,7157;MI:0096- pull down | MI:0047- far western blotting | MI:0040- electron microscopy;11285227;14.04;"";"";""
2183;Kaiso-NCOR complex;;Human;Q92828,Q13227,O15379,O75164,P52732,O75376,O60907,Q9BZK7,Q9UPN9,Q86T24;7464,2874,8841,9682,3832,9611,6907,79718,51592,10009;MI:0047- far western blotting;14527417;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"Kaiso targets the N-CoR complex to the MTA2 gene promoter in a methylation-dependent manner. The authors postulate that deacetylation of chromatin stabilizes the association of Kaiso-N-CoR with chromatin.";"";""
2184;Gata1-Gfi1b complex;;Mouse;P17679,O70237;14460,14582;MI:0019- coimmunoprecipitation;15920471;11.02.03.04.03,43.03.07.01,70.10;"Experiments suggest a role for the Gata1-Gfi1b complex in the repression of genes associated with cell proliferation.";"";""
2185;Gata1-Ldb1-Tal1 complex;;Mouse;P17679,P70662,P22091;14460,16825,21349;MI:0019- coimmunoprecipitation;15920471;11.02.03.04.01,43.03.07.01,70.10;"Strong GATA-1 binding and a clear enrichment for TAL-1 binding were detected at the EKLF enhancer, providing evidence for a role as transcriptional activator for the Gata1-Ldb1-Tal1 complex.";"";""
2186;Gata1-Snf2h complex;;Mouse;P17679,Q91ZW3;14460,93762;MI:0019- coimmunoprecipitation;15920471;70.10;"The interaction between SNF2h and GATA-1 may help explain the observation that knocking down SNF2h expression in primary hematopoietic progenitor cells blocked erythroid differentiation (PMID:14617767).";"";""
2187;Ubiquitin E3 ligase (NFKBIA, FBXW11, BTRC, CUL1, SKP1A);;Human;Q9Y297,Q13616,Q9UKB1,P25963,P63208;8945,8454,23291,4792,6500;MI:0007- anti tag coimmunoprecipitation;10644755;14.07.05,14.13.01.01,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitination-dependent destruction of NF-kappa-B inhibitor alpha is mediated by ubiquitin E3 ligases containing heterdimers and homodimers of beta-TrCP1 (BTRC) and beta-TrCP2 (FBXW11).";"";""
2188;Ubiquitin E3 ligase (CDC34, NEDD8, BTRC, CUL1, SKP1A, RBX1);;Human;Q9Y297,Q13616,Q15843,P62877,P63208;8945,8454,4738,9978,6500;MI:0007- anti tag coimmunoprecipitation;10713156;14.07.05,14.13.01.01,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Regulation of NF-kappaB occurs through phosphorylation-dependent ubiquitination of IkappaBalpha, which is degraded by the 26S proteasome. Recent studies have shown that ubiquitination of IkappaBalpha is carried out by ubiquitin E3 ligase complexes. Nedd8 modification of the Cul-1 component of ubiquitin E3 ligases is important for ubiquitination of IkappaBalpha.";"";""
2189;Ubiquitin E3 ligase (SMAD3, BTRC, CUL1, SKP1A, RBX1);ROC1-SCFFbw1a;Human;Q9Y297,Q13616,P62877,P63208,P84022;8945,8454,9978,6500,4088;MI:0019- coimmunoprecipitation;11359933;14.07.05,14.13.01.01,30.07,70.03,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitin E3 ligase complex ROC1-SCFFbw1a interacts with activated Smad3 through its MH2 domain and induces the ubiquitination and proteasomal degradation of the transcriptional modulator Smad3.";"";""
2190;Ubiquitin E3 ligase (Fbxo15, Cul1, Skp1a);;Mouse;Q9WTX6,Q9QZN0,Q9WTX5;26965,50764,21402;MI:0007- anti tag coimmunoprecipitation;12665572;14.07.05;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The F-box-containing protein Fbx15 is a novel target of the POU transcription factor Oct3/4 but is dispensable for embryonic stem cell self-renewal and mouse development.";"";""
2191;Ubiquitin E3 ligase (FBXO18, SKP1A, CUL1, RBX1);SCFhFBH1 complex;Human;Q13616,Q8NFZ0,P62877,P63208;8454,84893,9978,6500;MI:0007- anti tag coimmunoprecipitation;11956208;14.07.05,14.13.01.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. hFBH1 is the first F-box protein implicated in nucleic acid metabolism.";"";""
2192;Ubiquitin E3 ligase (NIPA, SKP1A, CUL1, RBX1);SCF(NIPA);Human;Q13616,P62877,P63208,Q86WB0;8454,9978,6500,51530;MI:0007- anti tag coimmunoprecipitation;16009132;10.03.01.01,14.07.05,14.13.01.01,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Activity of ubiquitin E3 ligase (containing NIPA, SKP1A, CUL1 and RBX1) oscillates throughout the cell cycle, and cell-cycle-regulated phosphorylation of NIPA constitutes the responsible timing circuit. Nuclear cyclin B1 was identified to be a critical substrate of the complex in interphase. According to the oscillating activity of ubiquitin E3 ligase (containing NIPA, SKP1A, CUL1 and RBX1), this targeting process is terminated at G2/M to allow for nuclear cyclin B1 accumulation, which is necessary for mitotic entry.";"";""
2193;Ubiquitin E3 ligase (Fbxo32, Skp1a, Cul1, Rbx1);;Mouse;Q9WTX6,Q9CPU7,P62878,Q9WTX5;26965,67731,56438,21402;MI:0007- anti tag coimmunoprecipitation;11717410;14.07.05,14.13.01.01,75.03.12.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Atrogin-1 (Fbxo32) is one of the few examples of an F-box protein or Ub-protein ligase (E3) expressed in a tissue-specific manner (striated muscles) and appears to be a critical component in the enhanced proteolysis leading to muscle atrophy in diverse diseases.";"";""
2194;Ubiquitin E3 ligase (Fbxo2, Skp1a, Cul1, Rbx1);SCF(Fbx2);Mouse;Q9WTX6,Q80UW2,P62878,Q9WTX5;26965,230904,56438,21402;MI:0007- anti tag coimmunoprecipitation;12140560;14.07.05,14.13.01.01,32.01.07,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Results indicate that SCF(Fbx2) ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism.";"";""
2196;LIG1-9-1-1 complex;;Human;O60921,P18858,O60671,Q99638;3364,3978,5810,5883;MI:0007- anti tag coimmunoprecipitation;15871698;10.01.05.01,10.03.01.03,32.01.09,70.10;"The 9-1-1 complex can stimulate DNA ligase I.";"";""
2197;FEN1-9-1-1 complex;;Human;P39748,O60921,O60671,Q99638;2237,3364,5810,5883;MI:0006- anti bait coimmunoprecipitation;15556996;01.03.16,10.01.05.01,10.03.01.03,32.01.09,70.10;"The 9-1-1 complex stimulates FEN1 activity.";"";""
2198;RAD9-RAD1-HUS1-POLB complex; 9-1-1-POLB complex;Human;O60921,P06746,O60671,Q99638;3364,5423,5810,5883;MI:0007- anti tag coimmunoprecipitation;15314187;10.01.05.01,10.03.01.03,32.01.09,70.10;"The 9-1-1 complex directly interacts with and stimulates POLB activity thus recruiting POLB to DNA damage sites.";"";""
2199;CTF18-RFC subcomplex;;Human;Q8WVB6,P35250,P40938,P35249,P40937;63922,5982,5983,5984,5985;MI:0007- anti tag coimmunoprecipitation;12930902;01.04,10.01.03,10.03.04.05,16.01,16.03.01,42.10.03,70.10;"CTF18 interacts with RFC5.";"";""
2200;RFC2-5 subcomplex;;Human;P35250,P40938,P35249,P40937;5982,5983,5984,5985;MI:0029- cosedimentation through density gradients;9488738;01.04,10.01.03,16.03.01,70.10;"Reconstitution experiments have revealed that a minimum of three subunits (the 40-, 37-, and 36-kDa subunits) are required for DNA-dependent ATPase activity in vitro.";"";""
2201;PCNA-RFC2-5 complex;;Human;P12004,P35250,P40938,P35249,P40937;5111,5982,5983,5984,5985;MI:0007- anti tag coimmunoprecipitation;12171929;10.01.03,70.10;"";"";""
2202;CHL12-RFC2-5 complex;;Human;Q8WVB6,P35250,P40938,P35249,P40937;63922,5982,5983,5984,5985;MI:0007- anti tag coimmunoprecipitation;12171929;10.01.03,70.10;"";"";""
2203;BRD4-RFC complex;;Human;O60885,P35251,P35250,P40938,P35249,P40937;23476,5981,5982,5983,5984,5985;MI:0007- anti tag coimmunoprecipitation;12192049;10.03.01,10.03.01.01.03,70.10;"BRD4 regulates cell cycle progression from G1 to S phase by interacting with RFC1.";"";""
2204;MCM8-ORC2-CDC6 complex;;Human;Q99741,Q9UJA3,Q13416;990,84515,4999;MI:0019- coimmunoprecipitation;15684404;10.01.03,10.03.01.01.03,70.10;"Down-regulation of MCM8 impairs the G1-to-S transition.";"";""
2205;ORC5-ORC1 complex;;Human;Q13415,O43913;4998,5001;MI:0006- anti bait coimmunoprecipitation;15448696;10.01.03.03,70.10;"";"";""
2210;BRCA1-IRIS-pre-replication complex;;Human;Q5YLB2,Q99741,O75496,Q13415;672,990,51053,4998;MI:0006- anti bait coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;15448696;10.01.03,70.10;"BRCA1-IRIS is a BRCA1 gene product encoded by an uninterrupted open reading frame that extends from codon 1 of the known BRCA1 open reading frame to a termination point 34 triplets into intron 11. BRCA1-IRIS localizes to the nucleus and fails to interact with BARD1.";"";""
2211;BARD1-BRCA1-CSTF complex;;Human;Q99728,P38398,Q05048,P33240,Q12996;580,672,1477,1478,1479;MI:0006- anti bait coimmunoprecipitation;10477523;11.04.03.05,16.03.03,70.10;"Interaction of BARD1 with CstF inhibits RNA polyadenylation and ensures that at DNA damage sites nascent RNAs are not erroneously polyadenylated. ";"BRCA1 is involved in breast cancer.";""
2213;BRCA1-BARD1-POLR2A complex;;Human;Q99728,P38398,P24928;580,672,5430;MI:0019- coimmunoprecipitation;15886201;11.02.03.04,14.07.05,70.10;"BRCA1 and BARD1 heterodimer ubiquitinates a hyperphosphorylated form of POLR2A. ";"BRCA1 is involved in breast cancer.";""
2214;LMO4-BRCA1-CTIP-LDB1 complex;;Human;P38398,Q86U70,P61968,Q99708;672,8861,8543,5932;MI:0006- anti bait coimmunoprecipitation;11751867;11.02.03.04,16.03.01,70.10;"";"BRCA1 is involved in breast cancer.";""
2215;BRCA1-LMO4-CTIP complex;;Human;P38398,P61968,Q99708;672,8543,5932;MI:0007- anti tag coimmunoprecipitation;11751867;11.02.03.04,16.03.01,70.10;"LMO4 functions as a repressor of BRCA1 activity in breast tissue. ";"BRCA1 is involved in breast cancer.";""
2217;MDC1-MRN-ATM-FANCD2 complex;;Human;Q13315,Q9BXW9,Q14676,P49959,O60934,Q92878;472,2177,9656,4361,4683,10111;MI:0006- anti bait coimmunoprecipitation;12607005;10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"Prior exposure of cells to irradiation appears to reduce the interaction of MDC1 with ATM and FANCD2.";"";""
2218;MDC1-MRE11-RAD50-NBS1 complex;;Human;Q14676,P49959,O60934,Q92878;9656,4361,4683,10111;MI:0019- coimmunoprecipitation | MI:0096- pull down;12607003;10.01.05.01,10.03.01.03,32.01.09,70.10;"In response to ionizing radiation, MDC1 is hyperphosphorylated and rapidly relocalizes to nuclear foci that also contain the MRE11 complex. MDC1-mediated focus formation by the MRE11 complex at sites of DNA damage is crucial for the efficient activation of the intra-S-phase checkpoint.";"";""
2219;TERF1 homodimer complex;;Human;P54274;7013;MI:0413- electrophoretic mobility shift assay;9391075;10.03.01,16.03.01,42.10.03;"TERF1 is shown to be important in regulating telomere length. It may connect mitotic control to the telomere regulatory machinery.";"";""
2220;RAD52-ERCC4-ERCC1 complex;;Human;P07992,Q92889,P43351;2067,2072,5893;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;14734547;01.03.16.03,10.01.05,70.10;"Rad52-XPF-ERCC1 complex processes recombination intermediates generated during the repair of DNA double strand breaks.";"ERCC4 is involved in xeroderma pigmentosum group F.";""
2221;RPA-MSH4-BLM complex;;Mouse;O88700,Q99MT2,Q8VEE4,Q62193,Q9CQ71;12144,55993,68275,19891,68240;MI:0416- fluorescence microscopy | MI:0040- electron microscopy;11950880;10.03.01.01.11,42.10.03,70.10;"RPA stimulates helicase activity of BLM.";"";""
2222;BLM complex II;;Human;P54132,Q9H9A7,P27694,P15927,P35244,Q13472;641,80010,6117,6118,6119,7156;MI:0006- anti bait coimmunoprecipitation;15775963;10.01.02,10.01.05.01,32.01.09,70.10;"BLAP75 is an integral component of BLM complexes and is essential for their stability.";"";""
2223;BLM-TOP3A complex;;Human;P54132,Q13472;641,7156;MI:0006- anti bait coimmunoprecipitation;10734115;10.01.02,70.10;"";"BLM is involved in Bloom syndrome (BS).";""
2224;MSH2/6-BLM-p53-RAD51 complex;;Human;P54132,P43246,P52701,Q06609,P04637;641,4436,2956,5888,7157;MI:0006- anti bait coimmunoprecipitation;15064730;32.01.09,10.01.05.01,70.10;"MSH2/6 protein complex stimulates the ability of the Bloom's syndrome gene product, BLM, to process Holliday junctions in vitro, an activity that could also be regulated by p53. MSH6 colocalizes with BLM and p53 in hydroxyurea-induced RAD51 nuclear foci.";"BLM is involved in Bloom's syndrome.";""
2225;MutS-alpha-histone H4 complex;;Mouse;P62806,P43247,P54276;97122,17685,17688;MI:0402- chromatin immunoprecipitation assays;15753043;10.01.05.03.03,43.03.07.02.01.01,73.03.07.02.01.01;"MSH2 associates with transcribed S regions in primary murine B cells activated for switch recombination. Electron microscopic imaging reveals that MutSalpha binds in vitro to DNA structures formed within transcribed S regions and mediates their synapsis.";"";""
2226;MutS-alpha-PK-zeta complex;;Human;P43246,P52701,Q05513;4436,2956,5590;MI:0006- anti bait coimmunoprecipitation;15808853;10.01.05.01,14.13.01.01;"PKC zeta protects MutS-alpha protein complex from degradation. PKC zeta interacts with hMSH2 and hMSH6 proteins and phosphorylates both.";"";""
2228;BLM-RAD51L3-XRCC2 complex;;Human;P54132,O75771,O43543;641,5892,7516;MI:0006- anti bait coimmunoprecipitation;12975363;10.01.05.01,70.10;"Interaction between BLM and RAD51L3 is mediated through the N-terminal domain of BLM. RAD51L3-XRCC2 complex stimulates ability of BLM to disrupt Holliday junction structures. ";"BLM is involved in Bloom's syndrome (BS).";""
2230;PCNA complex;;Rabbit;P11802,Q00535,P38936,Q08211,P12004,P27694,P11387;1019,1020,1026,1660,5111,6117,7150;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;11254741;10.01.03,10.03,70.10,77.03.05.01;"";"";"Since none of the proteins from rabbit were available in the UniProt database at the time of annotation, the orthologous human proteins were used."
2231;PCNA homotrimer complex;;Human;P12004;5111;MI:0071- molecular sieving | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;7522248;10.01.03,70.10;"PCNA exists mainly as homotrimer whose expression increases in the late G1- to S-phase of cell cycle. ";"PCNA is a target for autoimmunity in systemic lupus erythematosus.";""
2233;Replication-coupled CAF-1-MBD1-ETDB1 complex;;Human;Q13111,Q9UIS9,Q15047;10036,4152,9869;MI:0006- anti bait coimmunoprecipitation | MI:0018- two hybrid;15327775;10.01.03,10.01.09.05,10.01.09.07,10.03.01.01.05,14.07.09,42.10.03,70.10;"Formation of CAF-1-MBD1-SETDB1 complex occurs during S phase of cell cycle. This complex facilitates methylation of H3-K9 during replication-coupled chromatin assembly.";"";""
2234;Chromatin assembly complex (CAF-1 complex);;Human;Q13111,Q13112,Q09028;10036,8208,5928;MI:0029- cosedimentation through density gradients;8858152;10.01.03,10.01.09.05,10.03.01.01.05,42.10.03,70.10;"Caf-1 complex assembles nucleosomes in a replication-dependent manner.";"";""
2235;ASF1-interacting protein complex;;Human;Q9Y294,Q9NVP2,Q13111,Q13112,P54198,P68431;25842,55723,10036,8208,7290,8350;MI:0019- coimmunoprecipitation;15664198;10.01.03,10.01.09.05,42.10.03;"Asf1 provides the cells with a buffering system for histone excess generated in response to stalled replication and explains how mammalian cells maintain a critical "active" histone pool available for deposition during recovery from replication stresses.";"";""
2236;ASF1-histone containing complex;;Human;Q9Y294,Q9NVP2,Q13112,O96017,P68431,P49321,P50502;25842,55723,8208,11200,8350,4678,6767;MI:0071- molecular sieving;15664198;10.01.03,10.01.09.05,42.10.03;"Asf1 provides the cells with a buffering system for histone excess generated in response to stalled replication and explains how mammalian cells maintain a critical "active" histone pool available for deposition during recovery from replication stresses.";"";""
2237;SP1-MCAF2 complex;;Human;Q5U623,P08047;80063,6667;MI:0019- coimmunoprecipitation;15691849;10.01.09.05,10.01.09.07,11.02.03.04.03,11.02.03.04.07,42.10.03,70.10;"MCAF2 also binds to SETDB1, but more efficiently to SP1.";"";""
2238;MBD1-MCAF1-SETDB1 complex;;Human;Q6VMQ6,Q9UIS9,Q15047;55729,4152,9869;MI:0019- coimmunoprecipitation;15691849;10.01.09.05,10.01.09.07,11.02.03.04.03,11.02.03.04.07,14.07.09,42.10.03,70.10;"MCAF1 enhances transcriptional repression by MBD1 together with SETDB1.";"";""
2240;Hd-Hap1-Dctn1 complex;;Rat;P28023,P54256,P51111;29167,29430,29424;MI:0019- coimmunoprecipitation;9454836;20.09.14,70.03,77.03.01.01.01;"This protein complex may take part in dynein-dynactin-associated intracellular transport.";"";""
2241;HD-RAB8A-OPTN complex;;Human;P42858,Q96CV9,P61006;3064,10133,4218;MI:0004- affinity chromatography technologies | MI:0018- two hybrid;11137014;20.09.07;"This complex probably involved in membrane trafficking and cellular morphogenesis.";"";""
2242;TGM2-HD-CALM1 complex;;Human;P62158,P42858,P21980;805,3064,7052;MI:0019- coimmunoprecipitation;14985437;14.10;"Inhibiting the interaction of calmodulin with transglutaminase and huntingtin protein could decrease cross-linking and diminish huntingtin aggregate formation in the HD brain.";"";""
2243;TGM2-HD complex;;Human;P42858,P21980;3064,7052;MI:0019- coimmunoprecipitation;11442349;14.10;"";"";""
2247;Dynactin complex (DCTN1, DCTN2, DCTN3, DCTN4, DCTN6, CAPZA1, CAPZB, ACTR1A);;Bovine;P61163,P52907,P47756,Q14203,Q13561,O75935,Q9UJW0,O00399;10121,829,832,1639,10540,11258,51164,10671;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;10074429;20.09.14,77.03.01.01.01;"";"";""
2254;CTGF/Hcs24-actin complex;;Human;P29279,(P60709,P63261);1490,(60,71);MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;12470643;10.03.05,42.04.03,45.03.05.05,70.03,75.03.06;"The authors suggest that binding of CTGF/Hcs24 to actin in chondrocytes may play some important roles in the regulation of cytoskeletal organization and of the cell cycle.";"";""
2255;Cofilin-actin-CAP1 complex;;Human;P60709,Q01518,P23528;60,10487,1072;MI:0096- pull down;11950878;34.05,42.04.03,70.04.03;"As well as full-length CAP1, both CAP1-NT and CAP1-CT enhanced cofilin-induced acceleration of F-actin turnover, whereas their effect was only marginally visible in the absence of cofilin. Localization experiments in fibroblasts demonstrated that CAP1-NT is primarily responsible for accumulating CAP1 with cofilin and actin in dynamic peripheral regions of spreading cells.";"";""
2256;RIAM-Rap1-GTP complex;;Human;Q7Z5R6,P62834;54518,5906;MI:0019- coimmunoprecipitation | MI:0096- pull down;15469846;34.07,42.04.03,70.02;"RIAM preferentially interacted with Rap1-GTP compared to Ras-GTP. The results indicate that RIAM is required for localization of Rap1-GTP at the plasma membrane.";"";""
2258;VILIP-1-AChR-alpha-4-AChR-beta-2 complex;;Human;P43681,P17787,P62760;1137,1141,7447;MI:0096- pull down;12202488;16.17.01,18.02.10,20.03.01.01,34.03.01;"The results suggest a rule for VILIP-1 as an AChR-associated protein that modulates the surface expression levels and functional properties of alpha 4beta 2 AChRs in response to changes in the intracellular levels of calcium.";"";""
2261;GluR6a-GluR6b heterodimer complex;;Mammalia;P39087;14806;MI:0019- coimmunoprecipitation;16102538;20.01.01.01,20.03.01.01,34.03.01,70.02;"";"";"The authors show that the two splice variants of the GluR6 subunit, GluR6a and GluR6b, which differ in their C-terminal domains, do not show distinct functional properties, but coassemble as heteromers in vitro and in vivo."
2266;PPP3CA-PPP3CA-RCAN1 complex;;Human;Q08209,P16298,P53805;5530,5532,1827;MI:0019- coimmunoprecipitation;12809556;30.01.09.03;"";"";""
2267;Pick1 homodimer complex;;Rat;Q9EP80;84591;MI:0096- pull down;11466413;14.10;"The authors conclude that PICK1 dimerizes or multimerizes via the coiled coil region or the C-terminal neighboring sequences.";"";""
2268;Pick1-Glur2-Pkca complex, TPA (tissue plasminogen activator) treated;;Rat;P19491,Q9EP80,P05696;29627,84591,24680;MI:0096- pull down;11466413;14.04,34.03.01,70.02;"The experiment demonstrates that a heterocomplex, in which a PICK1 dimer or higher multimer is linked simultaneously to the C termini of PKC-alpha  and GluR2, forms by a phorbol ester and PDZ-dependent mechanism. Such a complex could target the activated form of PKC-alpha  to GluR2. Ser880 of GluR2 is a substrate for PKC. To determine whether PICK1 clusters contain GluR2 that has been phosphorylated by PKC, the authors assayed the clusters for GluR2Ser880-PO4 by using an affinity-purified phosphopeptide antiserum. Western blot analysis revealed that TPA (tissue plasminogen activator)  induced a strong increase of GluR2Ser880-PO4 present in protein extracts from neurons, confirming the PKC phosphorylation of GluR2 in vivo.";"";""
2270;Hippocalcin-beta2-adaptin-Glur2 complex, Ca(2+) dependent;;Rat;P62944,P19491,P84076;140670,29627,29177;MI:0019- coimmunoprecipitation;16102532;16.17.01,20.09.18.09.01,34.03.01,70.02,73.03.13,77.03.01.01;"The authors describe that in neurons the hippocalcin-AP2 complex binds TfR in a Ca(2+)-independent manner, whereas the complex only binds to AMPARs, like Glur2 in the presence of Ca(2+). Since there is no direct interaction between hippocalcin and GluR2/3, the data indicate that hippocalcin complexes with AMPARs via its interaction with AP2. Hippocalcin binds the beta-2-adaptin subunit of the AP2 adaptor complex.  ";"";"The authors state that beta2-adaptin is part of AP2 complex, described in PMID:12086608."
2271;Grip-Glur2/3-liprin-alpha-Lar complex;;Rat;P19491,P19492,Q91Z80,Q64604,(P97879,Q9WTW1);29627,29628,140592,360406,(84016,171571);MI:0006- anti bait coimmunoprecipitation | MI:0030- cross-linking studies;11931740;14.04,41.05.13.01,70.02,77.03.01.01.01;"The authors showed that Liprin-alpha and LAR-RPTPs are enriched at synaptic sites, and interfering with the GRIP-liprin-alpha interaction disrupts the synaptic targeting of AMPA receptors.";"";""
2272;PICK1-GRIP1-GLUR2 complex;;Human;P42262,Q9Y3R0,Q9NRD5;2891,23426,9463;MI:0096- pull down;16055064;14.04,20.09.18.09.01,70.02;"Complex analysed both in vitro and in vivo. This triple complex may function in the presentation of PKC-PICK1 complexes to the ABP/GRIP-GluR2 complex.";"";""
2273;Nsg1-Glur2-Grip1 complex;;Rat;P19491,P97879,P02683;29627,84016,25247;MI:0019- coimmunoprecipitation | MI:0096- pull down;16037816;14.04,20.09.18.09.01,70.02,77.03.01.01.01;"The results indicate that NEEP21-RIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane.";"";""
2274;Beta-catenin-Cadherin-Grip-liprin-alpha-GluR2/3 complex;;Rat;Q9Z1Y3,Q9WU82,(P19491,P19492),(P97879,Q9WTW1),(Q91Z79,Q91Z80);83501,84353,(29627,29628),(84016,171571),(140591,140592);MI:0006- anti bait coimmunoprecipitation;15750591;14.04,41.05.13.01,73.03.13,77.03.01.01.01;"The authors suggest that LAR-RPTPs (Leukocyte common antigen-related (LAR) family receptor protein tyrosine phosphatases) contribute to synapse morphogenesis by regulating the synaptic delivery of a protein complex that is scaffolded by GRIP and liprin-alpha and that includes AMPA receptors and cadherin-beta-catenin.";"";""
2275;GluR receptor complex;;Rat;P19490,P19491,P19492,P19493;50592,29627,29628,29629;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;1309749;20.01.01.01,20.03.01.01,30.05.02.24.05,34.03.01,70.02,77.03.01.01.01;"Immunolabeling done from detergent solubilized rat brain membranes.";"";""
2276;GluR1 homomer complex;;Rat;P19490;50592;MI:0019- coimmunoprecipitation;15924137;20.01.01.01,20.03.01.01,34.03.01,36.25.03.04.01,73.03.13,77.03.01.01.01;"Ser831 phosphorylation of GluR1 by CaMKII enhances the single-channel conductance of GluR1 homomers, and this tightly correlates with the increased channel conductance of synaptic AMPARs during LTP (long-term potentiation).";"";""
2277;D2 receptor-GluR2-GluR1 complex;;Rat;P61169,P19490,P19491;24318,50592,29627;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;15858065;14.04,20.01.01.01,20.03.01.01,30.05.02.24.03,34.03.01,77.03.01.01.01;"The authors show that D2 receptors interact with the GluR1 subunit only in the presence of the GluR2 subunit, indicating that GluR2 subunit is responsible for D2-AMPA receptor complex formation. In further experiments they show that D2 receptors interact with GluR2 subunit through NSF.";"";""
2281;Protein kinase A II alpha homodimer complex;;Mouse;P12367;19087;MI:0077- nuclear magnetic resonance;11985580;30.01.05.01,30.01.09.07;"";"";""
2294;ABI1-WASF2 complex;;Human;Q8IZP0,Q9Y6W5;10006,10163;MI:0019- coimmunoprecipitation;16155590;42.04.03;"";"";""
2296;Abi1-Wasl complex;;Mouse;Q8CBW3,Q91YD9;11308,73178;MI:0019- coimmunoprecipitation;16155590;42.04.03;"";"";""
2297;ABI1-WASL complex;;Human;Q8IZP0,O00401;10006,8976;MI:0004- affinity chromatography technologies;16155590;42.04.03;"";"Neural Wiskott-Aldrich syndrome";""
2300;Profilin 2 complex;;Human;P60709,Q7L576,Q05193,P11142,Q9Y2A7,P35080,O75116,P17600,Q92777;60,23191,1759,3312,10787,5217,9475,6853,6854;MI:0019- coimmunoprecipitation;9463375;14.10,20.09.18.09.01,42.04.03;"";"";""
2307;AP3D1-AP3S2 complex;;Human;O14617,P59780;8943,10239;MI:0004- affinity chromatography technologies;15469849;14.04;"";"";""
2308;AP3D1-AP3S1 complex;;Human;O14617,Q92572;8943,1176;MI:0018- two hybrid | MI:0004- affinity chromatography technologies;15469849;14.04;"";"";""
2318;ITGA6-ITGB4-Laminin10/12 complex; integrin complex;Human;P23229,P16144,O15230,P07942,P11047;3655,3691,3911,3912,3915;MI:0004- affinity chromatography technologies;10671376;34.07;"";"";""
2319;ITGA6-ITGB4-Laminin10/12 complex; integrin complex;Human;P23229,P16144,O15230,P55268,P11047;3655,3691,3911,3913,3915;MI:0004- affinity chromatography technologies;10671376;34.07;"";"";""
2320;ITGA6-ITGB4-CD151 complex; integrin complex;Human;P48509,P23229,P16144;977,3655,3691;MI:0019- coimmunoprecipitation;10811835;16.01,34.07.02,77.03.02.05;"The recruitment of Cd151 into hemidesmosomes is regulated by the integrin alpha6beta4.";"";""
2321;ITGA6-ITGB4-FYN complex; integrin complex;Human;P06241,P23229,P16144;2534,3655,3691;MI:0019- coimmunoprecipitation;11684709;16.01,40.10.02.02.03,77.03.02.05;"EGF-R with  ITGA6-ITGB4 and, through the tyrosine kinase Fyn, induces phosphorylation of the beta4 tail (ITGB4) and disruption of hemidesmosomes.";"";""
2322;ITGA6-ITGB4-LAMA5 complex; integrin complex;Human;P23229,P16144,O15230;3655,3691,3911;MI:0019- coimmunoprecipitation;7556090;34.07,75.03.09,77.03.02.05;"";"";""
2323;ITGA6-ITGB4 complex; integrin complex;Human;P23229,P16144;3655,3691;MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;2649503;30.05.02,34.05,77.03.02.05;"";"";""
2342;ITGAV-ITGB8-MMP14-TGFB1 complex;;Human;P06756,P26012,P50281,P01137;3685,3696,4323,7040;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;11970960;18.01.07,18.02,70.02,75.03.09,75.03.17;"SLC binds to alphav-beta8, an integrin expressed by normal epithelial and neuronal cells in vivo. This binding results in the membrane type 1 (MT1)-MMP-dependent release of active TGF-beta, which leads to autocrine and paracrine effects on cell growth and matrix production.";"";""
2343;ITGAV-ITGB5-PLAUR complex; integrin complex;Human;P06756,P18084,Q03405;3685,3693,5329;MI:0019- coimmunoprecipitation;10537314;34.05.01;"uPAR association with alpha(v)beta5 leads to a functional interaction of these receptors and suggests that uPAR directs cytoskeletal rearrangements and cell migration by altering alpha(v)beta5 signaling specificity.";"";""
2345;ITGAV-ITGB5-ICAM4 complex; integrin complex;Human;Q14773,P06756,P18084;3386,3685,3693;MI:0401- biochemical;11435317;16.01,34.07;"";"";""
2346;ITGAV-ITGB5-ADAM9 complex; integrin complex;Human;Q13443,P06756,P18084;8754,3685,3693;MI:0054- fluorescence-activated cell sorting;11162558;16.01,34.07;"MDC-9 interacts with alpha(v)beta(5) in an RGD-independent manner.";"";""
2347;ITGAV-ITGB5-SPP1 complex; integrin complex;Human;P06756,P18084,P10451;3685,3693,6696;MI:0110- text mining;16005200;16.01,34.07;"";"";""
2348;ITGAV-ITGB5-CYR61 complex; integrin complex;Human;O00622,P06756,P18084;3491,3685,3693;MI:0004- affinity chromatography technologies;11287419;16.01,18.01.07,34.05.01,34.07,75.03.05;"CYR61-dependent chemotaxis is mediated through integrin alpha(v)beta5.";"";""
2350;ITGAV-ITGB5 complex;;Human;P06756,P18084;3685,3693;MI:0004- affinity chromatography technologies;1694173;16.01,34.07;"";"";""
2351;ITGB6-FYN-FN1 complex;;Human;P02751,P06241,P18564;2335,2534,3694;MI:0019- coimmunoprecipitation;12917446;18.01.07,30.01.05.01,30.07;"Integrin beta6 signaling activates Fyn and thus promotes oral cancer progression.";"";""
2352;ITGAV-ITGB6-SPP1 complex; integrin complex;Human;P06756,P18564,P10451;3685,3694,6696;MI:0004- affinity chromatography technologies;16005200;16.01,34.07;"";"";""
2353;ITGAV-ITGB6-TGFB3 complex; integrin complex;Human;P06756,P18564,P10600;3685,3694,7043;MI:0004- affinity chromatography technologies;11821050;16.01,18.01.07;"";"";""
2354;ITGAV-ITGB6 complex;;Human;P06756,P18564;3685,3694;MI:0019- coimmunoprecipitation;8798654;16.01;"Cells expressing alpha(v)beta6 attach, but less avidly, do not spread, and completely fail to proliferate.";"";""
2355;ITGAV-ITGB3-CD47-FCER2 complex;;Human;Q08722,P06734,P06756,P05106;961,2208,3685,3690;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;10037797;16.01,36.25.16.07,73.03.07;"Alpha(v)beta3-CD47 mediates proinflammatory cytokine synthesis via interaction with CD23.";"";""
2356;ITGB3-ITGAV-CD47 complex; integrin complex;Human;Q08722,P06756,P05106;961,3685,3690;MI:0019- coimmunoprecipitation;7691831;16.01,34.07,70.02;"CD47 interactions with alpha(v)beta3 were found to promote both integrin activation induced by RGD peptide, and alpha(v)beta3 avidity in binding immobilized substrates by enhancing integrin clustering (PMID:14966135).";"";""
2358;ITGAV-ITGB3-SPP1 complex; integrin complex;Human;P06756,P05106,P10451;3685,3690,6696;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation | MI:0030- cross-linking studies;9256478;34.05.01,40.01;"The interaction of OPN with alpha(v)beta3 integrin, expressed on CASMCs (coronary artery smooth muscle cells), causes migration, extracellular matrix invasion, and proliferation.";"";""
2359;ITGAV-ITGB3-ADAM15 complex; integrin complex;Human;Q13444,P06756,P05106;8751,3685,3690;MI:0004- affinity chromatography technologies;11882657;16.01,34.07,70.02,70.27.01;"ADAM15/alpha(v)beta3 interactions may be important in the adhesion of tumour cells to endothelium (PMID:9914169).";"";""
2360;Itgav-Itgb3-Gsn complex; integrin complex;Mouse;P13020,P43406,O54890;227753,16410,16416;MI:0004- affinity chromatography technologies;11577104;16.01,73.03.01;"";"";""
2362;ITAGV-ITGB3-F11R complex; integrin complex;Human;Q9Y624,P06756,P05106;50848,3685,3690;MI:0019- coimmunoprecipitation;12750158;18.01.07,47.03.03.02;"JAM-1/A and alpha(v)beta3 form a complex in the absence of bFGF.";"";""
2363;ITGAV-ITGB3-PXN-PTK2b complex; integrin complex;Human;P06756,P05106,Q14289,P49023;3685,3690,2185,5829;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;11683411;16.01,34.07;"This complex could play key role in the regulation of cell adhesion-triggered cytoskeletal organization and signal transduction in podosome-containing cells derived from monocytic lineage.";"";""
2364;ITGAV-ITGB3-ADAM23 complex; integrin complex;Human;O75077,P06756,P05106;8745,3685,3690;MI:0004- affinity chromatography technologies;10749942;16.01,34.07;"ADAM 23, through its disintegrin-like domain, may function as an adhesion molecule involved in alpha(v)beta3-mediated cell interactions occurring in normal and pathological processes, including progression of malignant tumors from neural origin.";"";""
2365;ITGAV-ITGB3-COL4A3 complex; integrin complex;Human;Q01955,P06756,P05106;1285,3685,3690;MI:0004- affinity chromatography technologies;12682293;12.07;"Tumstatin binding to alpha(v)beta3 integrin leads to the inhibition of Cap-dependent translation (protein synthesis) mediated by focal adhesion kinase/phosphatidylinositol 3-kinase/Akt/mTOR/4E-BP1 pathway.";"";""
2366;ITGAV-ITGB3-PPAP2b complex; integrin complex;Human;P06756,P05106,O14495;3685,3690,8613;MI:0004- affinity chromatography technologies;16099422;34.07,47.03.03.02,70.02;"";"";""
2369;ITGAV-ITGB3-EGFR complex; integrin complex;Human;P00533,P06756,P05106;1956,3685,3690;MI:0019- coimmunoprecipitation;15834425;16.01,30.05.01.12.01,30.05.02.26;"The coordination between EGFR and alpha(v)beta3 is essential for the early events of HCMV infection, including viral entry.";"";""
2370;ITGA2b-ITGB3-CD9 complex; integrin complex;Human;P21926,P08514,P05106;928,3674,3690;MI:0019- coimmunoprecipitation;10429193;18.01.07,34.07,70.02,73.03.07;"CD9 is part of a protein complex that co-precipitates with aIIb3 under native conditions and provides evidence of CD9 and aIIbb3 associating in resting, inactive platelets (PMID:9355765).";"";""
2373;ITGAV-ITGB3-SPP1 complex; integrin complex;Human;P06756,P05106,P10451;3685,3690,6696;MI:0019- coimmunoprecipitation;7532190;34.05.01,75.03.12.02;"";"";""
2374;ITGAV-ITGB3-LAMA4 complex; integrin complex;Human;P06756,P05106,Q16363;3685,3690,3910;MI:0004- affinity chromatography technologies;16824487;16.01,34.07,70.27.01,77.03.03.02;"The alpha4 laminin subunit mediates endothelial cell-adhesion through alpha(v)beta3 integrin and that the key site is G1121-1139. ";"The G1121-1139 peptide promotes angiogenesis in vivo.";""
2375;FN1-TGM2 complex;;Human;P02751,P21980;2335,7052;MI:0030- cross-linking studies;10684262;16.01,34.07;"Overexpression of tTG increases the amount of Fn on the cell surface, enhances adhesion and spreading of fibronectin.";"";""
2376;ITGA2B-ITGB3-FN1-TGM2 complex;;Human;P02751,P08514,P05106,P21980;2335,3674,3690,7052;MI:0019- coimmunoprecipitation;10684262;16.01,34.07,70.02;"The tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.";"";""
2377;ITGA2b-ITGB3-CD47-SRC complex; integrin complex;Human;Q08722,P08514,P05106,P12931;961,3674,3690,6714;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;9169439;16.01,70.02;"At least five members of the Src-type kinase family are expressed in megakaryocytes and platelets (PMID:7545532) but only c-Src could be detected in the alpha IIb-beta 3-IAP complex.";"";""
2378;ITGA2b-ITGB3-TLN1 complex; integrin complex;Human;P08514,P05106,Q9Y490;3674,3690,7094;MI:0004- affinity chromatography technologies;8663236;16.01,73.03.07;"The purified talin binds to the cytoplasmic sequences of both alpha  and beta  subunits of this integrin. The regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation (PMID:14526080). ";"Disrupting the beta3 integrin-talin interaction blocks {alpha}IIb-beta3 activation and has a dramatic antithrombotic effect (PMID:17627302).";""
2379;ITGA2B-ITGB3-CIB1 complex; integrin complex;Human;Q99828,P08514,P05106;10519,3674,3690;MI:0411, enzyme-linked immunosorbent assay | MI:0018- two hybrid;9030514;16.17.01,34.07,77.03.11.07;"CIB does not regulate alpha-IIb-beta3 inside-out signaling, but rather is involved in an alpha-IIb-beta3 post-receptor occupancy event.";"";""
2381;ITGA2B-ITGB3 complex;;Human;P08514,P05106;3674,3690;MI:0004- affinity chromatography technologies;8132607;34.07;"";"";""
2382;ITGA2B-ITGB3-F11R complex; integrin complex;Human;Q9Y624,P08514,P05106;50848,3674,3690;MI:0004- affinity chromatography technologies;11171323;34.07;"";"";""
2383;ITGA5-ITGB1-FN1-TGM2 complex;;Human;P02751,P08648,P05556,P21980;2335,3678,3688,7052;MI:0019- coimmunoprecipitation;10684262;16.01,34.07,70.02;"The tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.";"";""
2384;ITGA5-ITGB1-ADAM15 complex; integrin complex;Human;Q13444,P08648,P05556;8751,3678,3688;MI:0004- affinity chromatography technologies;9914169;16.01,34.07;"";"";""
2385;ITGA5-ITGB4 complex;;Human;P08648,P05556;3678,3688;MI:0019- coimmunoprecipitation;3546305;34.07;"";"";""
2386;Itga-Itgb1-Ppap2b complex; integrin complex;Mouse;P11688,P09055,Q99JY8;16402,16412,67916;MI:0004- affinity chromatography technologies;16099422;34.07,47.03.03.02,70.02;"";"";""
2388;Itga5-Itgb1-Fn1-Sfrp2 complex;;Dog;Q28275,P08648,P05556,Q863H1;403845,3678,3688,475471;MI:0019- coimmunoprecipitation;14709558;40.10.02.04;"";"";"Since ITGA5 and ITGB1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from human were used."
2390;CD98-LAT2-ITGB1 complex;;Human;P05556,Q9UHI5,(P08195,Q01650);3688,23428,(6520,8140);MI:0019- coimmunoprecipitation;11507094;34.07.01,75.03.09;"The specific molecular ratio between the heterodimer CD98/LAT-2 and beta 1 integrin may be required for the polarity of epithelial cells.";"";""
2395;ITGA7-ITGB1-CD151 complex; integrin complex;Human;P48509,Q13683,P05556;977,3679,3688;MI:0019- coimmunoprecipitation;11884516;16.01,34.07,75.03.12;"The expression of alpha7-beta1 in K562 cells results in increased levels of CD151 at its surface.";"";""
2396;ITGA7-ITGB1-CD9 complex; integrin complex;Human;P21926,Q13683,P05556;928,3679,3688;MI:0019- coimmunoprecipitation;10459022;41.05.15;"";"";""
2397;ITGA7-ITGB1-ITGB1BP3 complex; integrin complex;Human;Q13683,P05556,Q9NPI5;3679,3688,27231;MI:0019- coimmunoprecipitation;12941630;34.07;"";"";""
2398;ITGA3-ITGB1-BSG complex; integrin complex;Human;P35613,P26006,P05556;682,3675,3688;MI:0019- coimmunoprecipitation;9360995;18.02,34.07.02;"The physical association between EMMPRIN and alpha3-beta1 may play a role in adhesion-induced matrix metalloproteinase production.";"";""
2399;ITGA3-ITGB1-CD63 complex; integrin complex;Human;P08962,P26006,P05556;967,3675,3688;MI:0019- coimmunoprecipitation;9360995;34.05,34.07;"";"";""
2400;ITGA3-ITGB1-CD151 complex; integrin complex;Human;P48509,P26006,P05556;977,3675,3688;MI:0019- coimmunoprecipitation;10811835;16.02,34.07.02,70.02,77.03.02.05;"CD151 is colocalized with alpha3-beta1 in pre-hemidesmosomal structures together with laminin-5.";"";""
2401;ITGA3-ITGB1-THBS1 complex; integrin complex;Human;P26006,P05556,P07996;3675,3688,7057;MI:0004- affinity chromatography technologies;11358957;34.07;"";"";""
2402;Itga3-Itgb1-Tgm2 complex; integrin complex;Rat;Q62470,P49134,Q9WVJ6;16400,24511,56083;MI:0019- coimmunoprecipitation;10684262;16.01,34.07,70.02;"Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions. ";"";"Since Itga3 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
2406;ITGA3-ITGB1 complex;;Human;P26006,P05556;3675,3688;MI:0019- coimmunoprecipitation;3546305;34.07;"";"";""
2411;ITGA6-ITGB1-CD151 complex; integrin complex;Human;P48509,P23229,P05556;977,3655,3688;MI:0019- coimmunoprecipitation;11884516;34.05.01;"The YXXphi motif-mediated internalization of CD151 promotes integrin-dependent cell migration by modulating the endocytosis and/or vesicular trafficking of its associated integrins (PMID:17716972).";"";""
2413;ITGA6-ITGB1 complex; Integrin complex;Human;P23229,P05556;3655,3688;MI:0004- affinity chromatography technologies;2649503;34.07;"";"";""
2415;Itgb1-Rap1a-Prkd1 complex;;Mouse;P09055,Q62101,P62835;16412,18760,109905;MI:0019- coimmunoprecipitation;16111639;18.02;"";"";""
2416;ITGB1-RAP1A-PKD1 complex;;Human;P05556,P98161,P62834;3688,5310,5906;MI:0019- coimmunoprecipitation;16111639;18.02;"";"";""
2417;ITGA4-ITGB1-EMILIN1 complex; integrin complex;Human;Q9Y6C2,P13612,P05556;11117,3676,3688;MI:0004- affinity chromatography technologies;12456677;34.05,34.07;"";"";""
2418;ITGA4-ITGB1 complex;;Human;P13612,P05556;3676,3688;MI:0019- coimmunoprecipitation;3546305;34.07;"";"";""
2419;ITGA4-ITGB1-CD81 complex; integrin complex;Human;P60033,P13612,P05556;975,3676,3688;MI:0019- coimmunoprecipitation;10229664;34.07;"";"";""
2420;ITGA4-ITGB1-CD53 complex;;Human;P19397,P13612,P05556;963,3676,3688;MI:0019- coimmunoprecipitation;8757325;16.01;"";"";""
2421;ITGA4-ITGB1-VCAM1 complex; integrin complex;Human;P13612,P05556,P19320;3676,3688,7412;MI:0004- affinMI:0030- cross-linking studies;10623819;34.07;"";"";""
2422;ITGA4-ITGB1-JAM2 complex; integrin complex;Human;P13612,P05556,P57087;3676,3688,58494;MI:0004- affinity chromatography technologies;12070135;34.07;"";"";""
2423;ITGA4-ITGB1-CD47 complex; integrin complex;Human;Q08722,P13612,P05556;961,3676,3688;MI:0019- coimmunoprecipitation;15292185;34.07;"";"";""
2424;ITGA4-ITGB1-CD63 complex; integrin complex;Human;P08962,P13612,P05556;967,3676,3688;MI:0019- coimmunoprecipitation;8757325;16.01;"";"";""
2425;ITGA4-ITGB1-PXN complex; integrin complex;Hamster;P13612,P05556,P49023;3676,3688,5829;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;12221126;34.05.01;"";"";"Since ITGA4, ITGB1 and PXN from hamster were not available in the UniProt databaseat the time of annotation, the orthologous human proteins were used."
2426;ITGA4-ITGB1-THBS1 complex; integrin complex;Human;P13612,P05556,P07996;3676,3688,7057;MI:0004- affinity chromatography technologies;11980922;34.07;"";"";""
2427;Itga4-Itgb1-Adam2 complex; integrin complex;Mouse;Q60718,Q00651,P09055;11495,16401,16412;MI:0019- coimmunoprecipitation | MI:0031- protein cross-linking with a bifunctional reagent;9889149;34.07.01;"This complex mediates sperm-egg fusion.";"";""
2428;ITGA4-ITGB1-THBS2 complex; integrin complex;Human;P13612,P05556,P35442;3676,3688,7058;MI:0004- affinity chromatography technologies;11980922;34.07;"";"";""
2429;ITGA2-ITGB1-CD47 complex; integrin complex;Human;Q08722,P17301,P05556;961,3673,3688;MI:0019- coimmunoprecipitation;10397731;34.11.03.03;"Integrin-associated protein (IAP/CD47) augments the function of alpha2-beta1 integrin in smooth muscle cells (SMC), resulting in enhanced chemotaxis toward soluble collagen.";"";""
2430;ITGA2-ITGB1-CHAD complex; integrin complex;Human;O15335,P17301,P05556;1101,3673,3688;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;9281592;34.07;"";"";""
2431;ITGA2-ITGB1-COL6A3 complex; integrin complex;Human;P12111,P17301,P05556;1293,3673,3688;MI:0004- affinity chromatography technologies;8387021;16.01,34.07,70.02,70.27.01;"";"";""
2432;ITGA2-ITGB1 complex;;Human;P17301,P05556;3673,3688;MI:0019- coimmunoprecipitation;3546305;34.07;"";"";""
2433;Itga5-Itgb1-Tgm2 complex; integrin complex;Rat;Q7M074,P49134,Q9WVJ6;315346,24511,56083;MI:0019- coimmunoprecipitation;10684262;16.01,34.07,70.02;"Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions.";"";""
2434;ITGA1-ITGB1-COL6A3 complex; integrin complex;Human;P12111,P56199,P05556;1293,3672,3688;MI:0004- affinity chromatography technologies;8387021;16.01,34.07,70.02,70.27.01;"";"";""
2435;ITGA1-ITGB1-PTPN2 complex; integrin complex;Human;P56199,P05556,P17706;3672,3688,5771;MI:0019- coimmunoprecipitation;15592458;30.05.01.12;"The cytoplasmic tail of alpha(1) integrin selectively interacts with a ubiquitously expressed TCPTP and activates it after cell adhesion to collagen.";"";""
2436;ITGAV-ITGB1 complex; integrin complex;Human;P06756,P05556;3685,3688;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;2138612;16.01,34.07;"The cell surface expression level of alphaV-beta1 is dependent on the number of alphaV subunits available after the formation of other alphaV-containing heterodimers (PMID:11997396).";"";""
2437;ITGA6-ITGB1-CYR61 complex; integrin complex;Human;O00622,P23229,P05556;3491,3655,3688;MI:0004- affinity chromatography technologies;12826661;34.07,47.03.03.02;"The T1 sequence in CCN1 is a novel binding motif for integrin alpha6-beta1.";"";""
2439;ITGA8-ITGB1 complex; integrin;Human;P53708,P05556;8516,3688;MI:0004- affinity chromatography technologies;7559467;16.01,34.07;"This integrin is receptor for tenascin, fibronectin, and vitronectin.";"";""
2440;ITGA9-ITGB1-ADAM9 complex; integrin complex;Human;Q13443,Q13797,P05556;8754,3680,3688;MI:0004- affinity chromatography technologies;11882657;16.01;"Alpha9-eta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.";"";""
2441;Itga9-Itgb1-Adam2 complex; integrin complex;Mammalia;Q60718,Q13797,P05556;11495,3680,3688;MI:0004- affinity chromatography technologies;11882657;16.01;"Alpha9-beta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.";"";""
2442;ITGA9-ITGB1-VCAM1 complex; integrin complex;Human;Q13797,P05556,P19320;3680,3688,7412;MI:0004- affinity chromatography technologies;10209034;34.05.01,34.07,45.03.11;"";"";""
2443;ITGA9-ITGB1-TNC complex; integrin complex;Human;Q13797,P05556,P24821;3680,3688,3371;MI:0004- affinity chromatography technologies;9565552;16.01;"";"";""
2444;ITGB1-ITGA9 complex;;Human;Q13797,P05556;3680,3688;MI:0019- coimmunoprecipitation;8798654;16.01,34.07,40.01.03.01;"Cells expressing alpha9-beta1 attach and spread equally well, and also proliferate, but significantly less than do cells expressing alpha(v)beta3.";"";""
2445;ITGA9-ITGB1-ADAM15 complex; integrin complex;Human;Q13444,Q13797,P05556;8751,3680,3688;MI:0004- affinity chromatography technologies;11882657;16.01,34.07.01;"Alpha9-beta 1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.";"";""
2446;ITGA9-ITGB1-FIGF complex; integrin complex;Human;O43915,Q13797,P05556;2277,3680,3688;MI:0004- affinity chromatography technologies;15590642;34.05.01,34.07,43.03.07.02.01;"Alpha9-beta1 directly binds to VEGF-C and -D and contributes to lymphangiogenesis.";"";""
2447;ITGA9-ITGB1-ADAM12 complex; integrin complex;Human;O43184,Q13797,P05556;8038,3680,3688;MI:0004- affinity chromatography technologies;10944520;34.07.01,70.02;"";"";""
2453;Multiprotein complex (monoubiquitination);;Human;Q13191,P00533,Q96B97,Q5U5U6;868,1956,30011,7314;MI:0019- coimmunoprecipitation;12218189;14.07.05;"The authors show that the adaptor protein CIN85 and its homologue CMS are monoubiquitinated by Cbl/Cbl-b after epidermal growth factor (EGF) stimulation. CIN85  has a dual role in controlling EGFR down-regulation, because it both promotes receptor internalization and participates in endosomal sorting and subsequent degradation of activated receptors.";"";""
2454;CIN85-CBL-SH3GL2-EGFR complex, EGF stimulated;;Human;P22681,P00533,Q3V639,Q96B97;867,1956,6456,30011;MI:0019- coimmunoprecipitation;11894095;20.09.07.25,20.09.18.09.01,30.05.01.12.01;"Cbl rapidly recruits CIN85 and endophilins to form a complex with activated EGF receptors, thus controlling receptor internalization.";"";""
2455;CIN85-SH3GL2 complex;;Human;Q99962,Q96B97;6456,30011;MI:0096- pull down;11894095;20.09.07.25,20.09.18.09.01;"";"";""
2456;MET-CIN85-SH3GL3-CBL complex, HGF stimulated;;Human;P22681,P08581,Q99963,Q96B97;867,4233,6457,30011;MI:0006- anti bait coimmunoprecipitation;11894096;20.09.07.25,20.09.18.09.01,30.05.01.12;"The authors propose the following model: upon ligand activation, HGF receptor becomes tyrosine phosphorylated, binds and phosphorylates Cbl, which in turn targets the receptor to clathrin-coated pits by recruiting the CIN85–endophilin complex.";"";""
2457;CIN85-SH3GL3 complex;;Human;Q99963,Q96B97;6457,30011;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;11894096;20.09.07.25,20.09.18.09.01;"";"";""
5722;Cbl-Cd2ap complex;;Mouse;P22682,Q9JLQ0;12402,12488;MI:0006- anti bait coimmunoprecipitation;15001553;16.01,20.09.18.09.01,70.09;"";"";""
5714;eNOS-CAV1 complex;;Human;Q03135,P29474;857,4846;MI:0006- anti bait coimmunoprecipitation;11425855;01.02.07.01,30.01.09.01,45.03.11;"";"";""
2462;Caveolin-1 homodimer complex;;Human;Q03135;857;MI:0030- cross-linking studies;15782218;34.01.07,70.07;"";"";""
2470;p130Cas-ER-alpha-cSrc-kinase- PI3-kinase p85-subunit complex;;Human;P56945,P03372,P27986,P12931;9564,2099,5295,6714;MI:0006- anti bait coimmunoprecipitation;15020686;10.03,14.07.03,30.01.05,30.01.09.08;"The authors suggest that estradiol triggers association of ER-alpha, c-Src, the p85 subunit of PI 3-kinase (PI3K) and p130Cas in a macromolecular complex and activates the c-Src kinase leading to p130Cas-dependent Erk1/2 phosphorylation.";"";""
2471;SRC-PRKCD-CDCP1 complex;;Human;Q9H5V8,Q05655,P12931;64866,5580,6714;MI:0019- coimmunoprecipitation;15851033;14.07.03,16.01;"";"";""
2475;Cbl-Crkl-Rapgef1 complex;;Mouse;P22682,P47941,Q91ZZ2;12402,12929,107746;MI:0006- anti bait coimmunoprecipitation;10608804;30.05.02.26,34.05.01;"The complex may be involved in migration signaling. ";"Crkl is one of the major tyrosine phosphoproteins detected in cells from patients with chronic myelogenous leukemia.";""
2476;CRKL-PDGFRA-CRK-RAPGEF1 complex;;Human;P46108,P46109,P16234,Q13905;1398,1399,5156,2889;MI:0019- coimmunoprecipitation;9546424;30.01;"";"";"CrkI and CrkII are splice variants of the Crk gene, only variant CrkII has been identified as component of the complex."
2480;CIN85 complex (CIN85, CRK, BCAR1, CBL, PIK3R1, GRB2, SOS1);;Human;P56945,P22681,P46108,P62993,P27986,Q96B97,Q07889;9564,867,1398,2885,5295,30011,6654;MI:0019- coimmunoprecipitation;11071869;30.05.01.12;"The authors propose that CIN85 acts as a mediator to couple the c-Cbl signaling pathway with other pathways through its multiple protein complexes, thereby leading to their interplay.";"";""
2486;GIPC1-LHCGR complex;;Human;O14908,P22888;10755,3973;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;14507927;14.04,20.09.18.09.01;"This protein is involved in the post-endocytotic trafficking of the internalized hCG and in maintaining the levels of cell surface hLHR during endocytosis of the bound hormone.";"";""
2487;GIPC1-NTRK1-RGS19 complex;;Human;O14908,P04629,P49795;10755,4914,10287;MI:0019- coimmunoprecipitation;11251075;20.09.07.07;"GIPC forms a complex with GAIP and the TrkA receptor and colocalizes with phosphoryated TrkA in retrograde transport vesicles.";"";""
2489;NCR3-CD247 complex;;Human;P20963,O14931;919,259197;MI:0019- coimmunoprecipitation;15821739;40.10.02.03;"NKp30, similar to other NK triggering receptors including CD16 (34) (35) and NKp46 (23), can transduce activating signals via association with the ITAM-containing CD3{zeta} polypeptides (PMID: 10562324).";"";""
5709;ArgBP2a-CBL-PTK2B complex;;Human;O94875,P22681,Q14289;8470,867,2185;MI:0019- coimmunoprecipitation;15128873;14.04,42.04.03,43.03.13;"";"";""
2510;ZAP70-CRKL-WIPF1-WAS complex; ZAP-70-CrkL-WIP-WASP complex;Human;P46109,P42768,O43516,P43403;1399,7454,7456,7535;MI:0019- coimmunoprecipitation;12504004;30.01;"";"";""
2511;CRKL-WIPF1-WAS complex; CrkL-WIP-WASP complex;Human;P46109,P42768,O43516;1399,7454,7456;MI:0019- coimmunoprecipitation;12504004;30.01;"";"";""
2513;N-WASp homomer;;Human;O00401;8976;MI:0031- protein cross-linking with a bifunctional reagent;10781580;42.04.03;"N-WASp undergoes self-association upon increasing concentration and the monomeric form activates actin polymerization and is favored by Grb2 binding.";"";""
5720;CIN85-CBL complex;;Human;P22681,Q96B97;867,30011;MI:0007- anti tag coimmunoprecipitation;11894095;20.09.07.25,20.09.18.09.01;"";"";""
2528;ERBB2-MEMO-SHC complex;;Human;P04626,Q9Y316,P29353;2064,51072,6464;MI:0019- coimmunoprecipitation;15156151;34.05,42.04.05;"The results suggest that the Shc adaptor protein mediates binding of Memo to the phospho-YD (Tyr 1227) residue of ErbB2.";"";""
2529;LAT-PLC-gamma-1-p85-GRB2-CBL-VAV-SLP-76 signaling complex, C305 activated;;Human;P22681,P62993,O43561,Q13094,P27986,P19174,P15498;867,2885,27040,3937,5295,5335,7409;MI:0019- coimmunoprecipitation;9489702;30.01.09.11,30.05.01.12,36.25.16.03.03;"The authors show that upon tyrosine phosphorylation, LAT binds Grb2, PLC-gamma1, the p85 subunit of PI3K, and other critical signaling molecules. They provide evidence that LAT plays an important role in linking the TCR to cellular activation.";"";""
2534;Cbl-SLP-76-Grb2 complex, Fc receptor gamma-R1 stimulated;;Human;P22681,P62993,Q13094;867,2885,3937;MI:0019- coimmunoprecipitation;9716598;30.05.01.12,36.25.16;"The authors demonstrate that the kinetics of SLP-76 phosphorylation parallels the kinetics of Cbl phosphorylation, suggesting a link between these two adapter proteins in the Fc gamma RI-signaling cascade.";"";""
2535;SLP-76-Cbl-Grb2-Shc complex, Fc receptor gamma-R1 stimulated;;Human;P22681,P62993,Q13094,P29353;867,2885,3937,6464;MI:0019- coimmunoprecipitation;9716598;30.05.01.12,36.25.16;"The authors propose that the association of Grb2 and Shc with SLP-76 and Cbl may serve as a repository for Grb2 and Shc, regulating their association with Sos and subsequent activation of Ras.";"";""
2536;PLC-gamma-2-SLP-76-Lyn-Grb2 complex;;Human;P62993,Q13094,P07948,P16885;2885,3937,4067,5336;MI:0096- pull down;10469124;30.01.09.11,30.05.01.12,36.25.16.09,73.03.07.03;"Analyses done with different GST-PLC-gamma-2 fusion proteins from resting and CRP (collagen-related peptide) stimulated platelets.";"";""
2537;PKC-alpha-PLD1-PLC-gamma-2 signaling complex, lacritin stimulated;;Human;P16885,Q13393,P17252;5336,5337,5578;MI:0006- anti bait coimmunoprecipitation;16923831;30.01.09.03,30.01.09.11,45.03.09,70.08,75.03.09;"Lacritin is described as mitogenic for a small subset of epithelial cell lines derived mainly from the nongermative epithelia that normally contact lacritin during its outward glandular flow. The authors propose that lacritin signaling  stimulates the formation of a transient perinuclear Golgi complex of PKC-alpha, PLD1, and PLC-gamma-2. This activates PLD1 of the mTOR pathway. Some PLC-gamma-2 activation and considerable IP3 generation were detected. Ca(2+) mobilization may then be a consequence.";"";""
2539;Lab-Grb2 complex, BCR stimulated;;Mouse;Q60631,Q9JHL0;14784,56743;MI:0006- anti bait coimmunoprecipitation;12514734;30.01.05,36.25.16.03.01,43.03.07.02.01.01,70.02,73.03.07.02.01.01;"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. The authors describe that LAB subsequently associates with Grb2, thereby recruiting Grb2 and Grb2-associated proteins to lipid rafts at the membrane.";"";""
2540;BCR-ABL (p210 fusion protein)-GRB2 complex;;Human;A1Z199,P62993;0,2885;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;8112292;30.01.05.01.05,30.01.05.05;"It was shown that Grb2 binds to the Tyr177 autophosphorylation site on Bcr-Abl.";"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL). ";""
2541;HGF-Met complex;;Human;P14210,P08581;3082,4233;MI:0411- enzyme linked immunosorbent assay;15161915;30.05.01.12;"HGF interacts with the extracellular domain of Met, resulting in the activation of Met and subsequent downstream functions. The authors demonstrate that that copper(II) inhibits HGF/Met interaction.";"";""
2542;EGFR-CBL-GRB2 complex;;Human;P22681,P00533,P62993;867,1956,2885;MI:0055- fluorescent resonance energy transfer;15782196;30.01,70.22;"The energy transfer analysis results prompted the authors to support the previously proposed model that although Cbl is capable of direct binding to EGFR, it preferentially binds receptors indirectly through Grb2.";"";""
2545;Grb2-mSos1 complex;;Mouse;Q60631,Q62245;14784,20662;MI:0071- molecular sieving | MI:0027- cosedimentation;8940013;30.01;"The stoichiometry of the Grb2-mSos1 complex was 1:1. Grb2-mSos1 is a stable complex and both proteins can exist in a constitutive complex in unstimulated cells.";"";""
2547;PLC-gamma-1-SLP-76-SOS1-LAT complex;;Human;O43561,Q13094,P19174,Q07889;27040,3937,5335,6654;MI:0019- coimmunoprecipitation;15696170;30.01.09.11,30.05.01.12,36.25.16.03.03;"In a supplementary figure the authors show that PLC-gamma-1, SLP-76 and Sos1 are effectively recruited to LAT in the absence of Dyn2. The results show further that when Dyn2 was present, several tyrosine-phosphorylated proteins coimmunoprecipitated with Lat, including SLP76, PLC-gamma1 and several other unidentified proteins. PLC-gamma-1 total tyrosine phosphorylation was diminished in the absence of Dyn2.";"";""
2548;Egfr-Grb2-mSos1 complex, EGF stimulated;;Mouse;Q01279,Q60631,Q2M4G6;13649,14784,20662;MI:0107- surface plasmon resonance;8940013;30.01.05.05,30.05.01.12.01;"The authors analysed the binding of Grb2-mSos1 to different phosphopeptides Shc pYVNV, EGFR1068, IR-PEP. Shc pYVNV showed the highest affinity.";"";""
2550;Frs2-Grb2-Shp2 complex, FGF stimulated;;Mouse;Q8C180,Q60631,P35235;327826,14784,19247;MI:0007- anti tag coimmunoprecipitation;9632781;30.05.01.12.03;"On the basis of further experiments the authors conclude that FGF stimulation leads to tyrosine phosphorylation of Shp2 and association with the Grb2-Sos complex.";"";""
2551;PDGFRA-PLC-gamma-1-PI3K-SHP-2 complex, PDGF stimulated;;Human;P16234,P27986,P19174,Q06124;5156,5295,5335,5781;MI:0019- coimmunoprecipitation;8943348;30.05.01.12;"Mutational analysis shows that Y720 of PDGFRA is required for binding of SHP-2 to the PDGFRA but not for the association of PLCg, the p85 subunit of PI3K, or Src. The data strongly suggest that SHP-2 must bind to the PDGFRA to be efficiently tyrosine phosphorylated.";"";""
2552;Il3rb1-Shc complex, IL-3 stimulated;;Mouse;P26955,P98083;12983,20416;MI:0019- coimmunoprecipitation;10891441;30.05.01.05;"The authors describe that Shc-Ship and Shc-Il3rb1 exist as separate complexes. They further propose that the interaction between Shc and the Il3rb1 subunit seems to be transient and of a lower affinity than the association of Shc with Ship.";"";""
2553;Shc-Grb2-mSos1 complex, EGF stimulated;;Mouse;Q60631,P98083,Q2M4G6;14784,20416,20662;MI:0107- surface plasmon resonance;8940013;30.01.05.05,30.05.01.12;"The authors analysed the binding of Grb2-mSos1 to different phosphopeptides Shc pYVNV, EGFR1068, IR-PEP. Shc pYVNV showed the highest affinity.";"";""
2558;p56(Lck)-CAML complex;;Mouse;P49070,P06240;12328,16818;MI:0006- anti bait coimmunoprecipitation;16111633;30.05.01.12,43.03.07.02.01.02,73.03.07.02.01.02;"The results of the authors suggest that CAML interacts with p56Lck to regulate its subcellular localization and timely activation of the kinase in response to TCR induction. They propose that CAML functions to maintain the proper storage of p56Lck to prevent excessive activation and to ensure carefully measured release of the kinase in response to TCR stimulation, thereby facilitating productive T cell activation with less cell death.";"";""
2559;p56(LCK)-CAML complex;;Human;P49069,P06239;819,3932;MI:0019- coimmunoprecipitation;16111633;30.05.01.12,43.03.07.02.01.02,73.03.07.02.01.02;"The results of the authors suggest that CAML interacts with p56Lck to regulate its subcellular localization and timely activation of the kinase in response to TCR induction. They propose that CAML functions to maintain the proper storage of p56Lck to prevent excessive activation and to ensure carefully measured release of the kinase in response to TCR stimulation, thereby facilitating productive T cell activation with less cell death.";"";""
2560;Nephrin-cadherin complex (Nphs1, Ctnnd1, ZO-1, Cd2ap);;Dog;Q9JLQ0,P30999,Q9QZS7,O97758;12488,12388,54631,403752;MI:0096- pull down;15331416;34.07.01,70.06.04,75.03.09;"";"";"Since Cd2ap, Ctnnd1 and Nphs1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
2561;Nephrin-cadherin complex (Nphs1, Cask, Cd2ap);;Rat;Q62915,Q80ZE7,Q9R044;29647,316258,64563;MI:0096- pull down;15331416;34.07.01,42.06.04,70.06.04,75.03.09,77.03.07.01;"The authors discuss eight bands stained with GelCode Blue, but describe only the 110kd band analysed by MS as CASK. Immunofluorescence labeling of cryosections from rat kidney lead to the conclusion that CASK is expressed in podocytes and MDCK-nephrin cells in the appropriate location to interact with nephrin.";"";""
2562;Nephrin-cadherin complex (Nphs1, Ctnnd1, Cdh3, Cd2ap);;Dog;Q9JLQ0,P10287,P30999,Q9QZS7;12488,12560,12388,54631;MI:0019- coimmunoprecipitation;15331416;34.07.01,70.06.04,75.03.09;"";"";"Since Cd2ap, Cdh3, Ctnnd1 and Nphs1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
2563;FGFR2-c-Cbl-Lyn-Fyn complex;;Human;P22681,P21802,P06241,P07948;867,2263,2534,4067;MI:0019- coimmunoprecipitation;15190072;14.13.01.01,30.01.05.01.05,30.05.01.12.03,43.03.17,73.03.17;"The results indicate that FGFR2 interacts with Lyn and Fyn and with c-Cbl, which can then mediate proteasome degradation of these three molecules in osteoblasts. The authors propose a mechanism by which constitutive FGFR2 activation in osteoblasts induces c-Cbl-dependent recruitment of FGFR2, Lyn, and Fyn, leading to their proteasome degradation, decreased kinase activity, and hence increased osteoblast differentiation.";"";""
2564;p21(ras)GAP-Fyn-Lyn-Yes complex, thrombin stimulated;;Human;P06241,P07948,P20936,P07947;2534,4067,5921,7525;MI:0019- coimmunoprecipitation;1544885;30.01.05,36.25.16.09,73.03.07.03;"The authors showed that Fyn, Lyn, and Yes are associated with GAP in thrombin-stimulated platelets. They could not distinguish whether this complex is preformed in resting platelets or whether the kinases associate with GAP following activation with thrombin.";"";""
2565;CD20-LCK-LYN-FYN-p75/80 complex, (Raji human B cell line);;Human;P06241,P06239,P07948,P11836;2534,3932,4067,931;MI:0019- coimmunoprecipitation;7545683;30.01.05.01.05,73.03.07.02.01.01;"Lyn accounted for most of the PTK activity in the CD20 complex.";"";"At the time of annotation, the identity of the additional member p75/80 of the protein complex was not known. "
2567;NCAM140-p59(fyn)-p125(fak) signaling complex;;Mammalia;Q62844,P13596,O35346;25150,24586,25614;MI:0019- coimmunoprecipitation;9079653;30.01.05.01.05,34.07,40.01.03.03;"p59 (fyn) appeared to be constitutively bound to NCAM140, either directly or indirectly, whereas p125fak was recruited to the NCAM complex. The authors showed that antibody-mediated ligation of cell surface NCAM140 or stimulation with soluble NCAM fusion protein led to a transient increase in tyrosine phosphorylation of both p125 (fak) and p59 (fyn), suggesting that activation of these nonreceptor tyrosine kinases is a proximal event in the NCAM signal transduction pathway.";"";""
2568;Slam-SAP-FynT complex;;Mouse;P39688,O88890,Q9QUM4;14360,20400,27218;MI:0007- anti tag coimmunoprecipitation;11477403;30.01.05.01.05,36.25.16.03,40.02.03.01,73.03.07.02.01.02;"FynT was clearly associated with Tac-SLAM in cells that were coexpressing SAP. The analysis of the role of FynT in SLAM-SAP signaling showed that Fyn was absolutely required for antibody-mediated tyrosine phosphorylation of SLAM in thymocytes. SLAM tyrosine phosphorylation is not required for SAP binding, the association between SLAM and SAP was Fyn-independent.";"";""
2569;Slam-SAP-SHIP complex;;Mouse;Q9ES52,O88890,Q9QUM4;16331,20400,27218;MI:0006- anti bait coimmunoprecipitation;11477403;30.07,36.25.16.03,40.02.03.01,73.03.07.02.01;"The authors showed that SHIP appeared to be the intermediate molecule that linked SLAM-SAP to Dok-related adaptors and RasGAP.";"";""
2570;Slam-SAP complex;;Mouse;O88890,Q9QUM4;20400,27218;MI:0006- anti bait coimmunoprecipitation;11477403;30.01.05,36.25.16.03,40.02.03.01,73.03.07.02.01.02;"The authors showed that SLAM was constitutively associated with SAP in thymocytes. The authors deduced that SLAM engagement is capable of triggering a protein tyrosine phosphorylation signal in T cells, and that this signal is strictly dependent on the presence of SAP. SLAM-SAP signaling was able to selectively inhibit IFN-gamma production by activated BI-141 T cells.";"Sh2d1a is involved in X-linked lymphoproliferative syndrome (XLP).";""
2572;RAB5-EEA1 complex;;Human;Q15075,P20339;8411,5868;MI:0055- fluorescent resonance energy transfer;15782196;20.09.18.09.01,70.22;"";"";""
2573;Class C VPS/HOPS complex;;Human;Q15075,P20339,Q9H270,Q9H269,Q9P253,Q96JC1;8411,5868,55823,64601,57617,23339;MI:0004- affinity chromatography technologies;16143105;20.09.18.09.01,42.22,70.22;"The class C VPS/HOPS complex, an established GEF for Rab7, interacts with Rab5 and is required for Rab5-to-Rab7 conversion.";"";""
2574;CD19-Vav-PI 3-kinase (p85 subunit) complex;;Human;P15391,P27986,P15498;930,5295,7409;MI:0019- coimmunoprecipitation;7528218;14.07.03,30.01.05,36.25.16.03.01,43.03.07.02.01.01,73.03.07.02.01.01;"The authors show that cross-linking of CD19 on surface Ig-negative B cell precursors and surface Ig-positive immature B cells results in the rapid tyrosine phosphorylation of Vav and a concomitant physical association of Vav with CD19 and PI 3-kinase.";"";""
2575;PI3-kinase p85-subunit alpha- PI3-kinase p110 complex;;Bovine;P32871,P23727;282306,282307;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;8313896;14.07.03,30.01.09.11;"The results demonstrate that p110 is able to form a stable, active PI 3-kinase complex with either of the p85 isoforms.";"";""
2577;Sam68-p85 P13K-IRS-1-IR signaling complex;;Human;P06213,P35568,Q07666,P27986;3643,3667,10657,5295;MI:0019- coimmunoprecipitation;11604231;30.05.01.12.05,70.03;"The authors found that Sam68 is tyrosine phosphorylated and associates with p85 PI3K after insulin stimulation in a complex that also contains IRS-1 and the IR itself. Further they demonstrated that Sam68 relocalizes after insulin stimulation from the nucleus to the cytoplasm. Regarding the association of Sam68 with p120GAP it is concluded that Sam68 is linking p120GAP to P13K signaling pathway.";"";""
2578;Sam68-p120GAP complex;;Human;Q07666,P20936;10657,5921;MI:0019- coimmunoprecipitation;11604231;30.05.01.12.05,70.03;"The authors suggest that Sam68 is associated with p120GAP after insulin stimulation and in this way it links GAP to the PI3K pathway. Further they demonstrated that Sam68 relocalizes after insulin stimulation from the nucleus to the cytoplasm.";"";""
2579;Chromosomal passenger complex CPC (INCENP, BIRC5, AURKB);;Human;Q96GD4,O15392,Q9NQS7;9212,332,3619;MI:0096- pull down | MI:0416- fluorescence microscopy;12925766;10.03.01.01,10.03.05.01,14.07.03,70.10.04;"All three proteins showed very similar changes in cell cycle progression, low in G1/S, increased during G2 and M. The studies revealed an evolutionarily conserved mechanism for Aurora B activation by INCENP binding and phosphorylation.";"";""
2580;Survivin homodimer complex;;Human;O15392;332;MI:0114- x-ray crystallography;10876248;10.03.01.01.11,10.03.05.01,40.10.02.01,42.04.05,70.04.05;"Survivin temporally and spatially localizes to microtubule organizing centers (MTOC) during mitosis (PMID:9859993).";"";""
2581;RasGAP-AURKA/AURKB-survivin complex;;Human;O15392,P20936,(O14965,Q96GD4);332,5921,(6790,9212);MI:0019- coimmunoprecipitation | MI:0096- pull down;11976319;10.03.01,30.01.05.05;"The authors define this ternary complex by several protein-protein interactions. RasGAP binds to the kinase domain of Aurora and this interaction inhibits the kinase activity of AURKA and AURKB.";"";""
2582;Chromosomal passenger complex CPC (CDCA8, AURKB, BIRC5);;Human;Q96GD4,O15392,Q53HL2;9212,332,55143;MI:0006- anti bait coimmunoprecipitation;15260989;10.03.01.01,10.03.05.01,70.10.04;"The authors propose that Dasra B may act to regulate the stability of Survivin, which, together with Incenp, serves to target Aurora B to chromosomal arms and centromeres.";"";""
2583;CSK-GAP-A.p62 complex;;Mouse;P41241,Q60749;12988,20218;MI:0019- coimmunoprecipitation | MI:0096- pull down;7544435;30.07,70.02,70.04;"The interaction requires the SH2 domain of CSK.";"";"The authors differentiate between GAP-A.p62 and Sam68, but there is no other corresponding entry than Swiss:Q60749 in SWISS-DB. "
2584;c-Src-Muc1 complex;;Mouse;P41241,Q02496;12988,17829;MI:0019- coimmunoprecipitation | MI:0663- confocal microscopy;15897873;30.07,70.02;"The authors use MMTV-PyV MT (MMTV-driven polyoma middle T-antigen transgenic mice)  as model to characterize the effect of Muc1 expression on c-Src signaling. Muc1 and c-Src colocalize in the MT tumors mainly at the apical membrane.";"";""
2585;KLC1-nKHC-uKHC kinesin complex;;Mouse;P33175,Q61768,O88447;16572,16573,16593;MI:0019- coimmunoprecipitation;9624122;20.09.14.01,34.05.02,70.04.05,77.03.01.01.01;"The authors demonstrate that neither KLC nor KHC form heterodimers in the native complex in brain and that there is no specificity in the interaction of the kinesin light chains with the kinesin heavy chains. Immunprecipitation done from brain lysate with KLC1 antibodies shows nKHC, uKHC and KLC1, but not KLC2.";"";""
2586;KLC2-nKHC-uKHC kinesin complex;;Mouse;P33175,Q61768,O88448;16572,16573,16594;MI:0019- coimmunoprecipitation;9624122;20.09.14.01,34.05.02,70.04.05,77.03.01.01.01;"The authors demonstrate that neither KLC nor KHC form heterodimers in the native complex in brain and that there is no specificity in the interaction of the kinesin light chains with the kinesin heavy chains. Immunprecipitation done from brain lysate with KLC2 antibodies shows nKHC, uKHC and KLC2, but not KLC1.";"";""
2587;nKHC-KLC1-KLC2 kinesin complex;;Mouse;P33175,O88447,O88448;16572,16593,16594;MI:0019- coimmunoprecipitation;9624122;20.09.14.01,34.05.02,70.04.05,77.03.01.01.01;"Immunoprecipitation done from brain lysate with nKHC antibodies brings down both kinesin light chains.";"";""
2589;PGC-1-SRp40-SRp55-SRp75 complex;;Human;Q9UBK2,Q08170,Q13243,Q13247;10891,6429,6430,6431;MI:0007- anti tag coimmunoprecipitation;10983978;11.02.03.04,11.04.03,16.03,70.10;"PGC-1 is part of both the preinitiation and elongation Pol II complexes, and association with the elongation form of Pol II depends on the C-terminal domain of PGC-1.";"";""
2590;FOXO1-FHL2-SIRT1 complex;;Human;Q14192,Q12778,Q96EB6;2274,2308,23411;MI:0019- coimmunoprecipitation;15692560;11.02.03.04.03,14.07.04,70.10;"The authors came to the following results: 1. FHL2 colocalizes and interacts with FOXO1 in prostate cancer cells. 2. FHL2 inhibits the activation of an IRS-driven reporter gene by FOXO1 in the presence but not in the absence of SIRT1 activity. 3. SIRT1 binds FOXO1, decreases its acetylation, and inhibits its transcriptional activity. 4. FHL2 interacts with SIRT1 and promotes its interaction with FOXO1. They suggest a model  that FHL2 negates the transcriptional activity of FOXO1 by promoting its deacetylation by SIRT1.";"";""
2591;SIRT1-HNF4-alpha-PGC-1-alpha complex, in response to fasting;;Mouse;P49698,O70343,Q923E4;15378,19017,93759;MI:0006- anti bait coimmunoprecipitation;15744310;02.01.03,11.02.03.04,32.01.11,34.01.04,70.10,77.03.11.07;"Acetylation of PGC-1 alpha by SIRT1 decreases its ability to efficiently coactivate HNF4alpha. In general the results show that PGC-1 alpha and SIRT1 can function together to promote adaptation to nutrient deprivation by regulating the genetic programmes of gluconeogenesis and glycolysis. SIRT1 can act both positively and negatively to control gene expression as a cofactor for PGC-1 alpha.";"";""
2592;SIRT1 homotrimer complex;;Human;Q96EB6;23411;MI:0071- molecular sieving;15469825;14.07.04,70.10;"SirT1 exists as a trimer and interacts with histone H1.";"";""
2593;FOXO3-SIRT1 complex, oxidative stress stimulated;;Human;O43524,Q96EB6;2309,23411;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;14976264;11.02.03.04,32.01.01,40.10.02.01,70.10;"SIRT1 and  transcription factor FOXO3 formed a complex in cells in response to oxidative stress, and SIRT1 deacetylated FOXO3 in vitro and within cells. SIRT1 increased FOXO3's ability to induce cell cycle arrest and resistance to oxidative stress but inhibited FOXO3's ability to induce cell death.";"";""
2598;NELF complex (Negative elongation factor complex);;Human;Q8WX92,P18615,Q8IXH7,Q9H3P2;25920,7936,51497,7469;MI:0007- anti tag coimmunoprecipitation;12612062;11.02.03.01.04,11.02.03.04.03,16.01,16.03.03,18.01.07,18.02.09,70.10;"NELF cooperates with DSIF and represses DRB-sensitive RNA-Polymerase II.";"";""
2599;POLR2A-CCNT1-CDK9-NCL-LEM6-CPSF2 complex;;Human;O60563,P50750,Q9P2I0,P19338,P24928,Q9UBK2;904,1025,53981,4691,5430,10891;MI:0007- anti tag coimmunoprecipitation;10983978;11.02.03.04,11.04.03,14.07.03,16.03,18.01.01,18.02,70.10;"The authors demonstrate that PGC-1 is part of both the preinitiation and elongation Pol II complexes, and association with the elongation form of Pol II depends on the C-terminal domain of PGC-1.";"";""
2600;BRD4 complex;;Human;O60885,O60563,P50750,Q15648,Q93074,O60244,Q9NVC6,O75448;23476,904,1025,5469,9968,9282,9440,9862;MI:0676- tandem affinity purification;16109376;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"";"";""
2601;P-TEFb-BRD4-TRAP220 complex;;Human;O60885,O60563,P50750,Q15648;23476,904,1025,5469;MI:0007- anti tag coimmunoprecipitation;16109377;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"Brd4 is necessary to mediate the interaction between P-TEFb and Mediator complex.";"";""
2602;P-TEFb-7SKRNA-HEXIM1 complex;;Human;O60563,P50750,O94992;904,1025,10614;MI:0007- anti tag coimmunoprecipitation;14580347;01.04,11.02.03.01.04,11.02.03.04,18.01.01,18.02.01,70.10;"7SK RNA is required for HEXIM1 to associate with P-TEFb complex. This allowes HEXIM1 to inhibit transcription. P-TEFb dissociates from HEXIM1 and 7SK in cells undergoing stress response, increasing the level of active P-TEFb for stress-induced transcription.";"";""
2603;Transcription elongation factor complex (SUPT5H, CDK9, CCNT1);;Human;O60563,P50750,O00267;904,1025,6829;MI:0047- far western blotting;11145967;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"";"";""
2604;P-TEFb-SKP2 complex;;Human;O60563,P50750,Q13309;904,1025,6502;MI:0019- coimmunoprecipitation;11689688;11.02.03.01.04,11.02.03.04,14.13.01.01,18.01.01,18.02.01.01,70.10;"Binding of SKP2 to P-TEFb requires PEST domain of cyclin T1. CDK9 is ubiquitinated and degraded by the proteasome whereas cyclin T1 is stable.";"";""
2605;Heterotrimeric complex (CCNT1, CDK9, GRN);;Human;O60563,P50750,P28799;904,1025,2896;MI:0019- coimmunoprecipitation;12588988;11.02.03.04.03;"Granulin is a cellular protein that interacts with cyclin T1 to inhibit transcription.";"";""
2608;Brd4-P-TEFb complex;;Mouse;Q9ESU6,Q9QWV9,Q99J95;57261,12455,107951;MI:0809- bimolecular fluorescence complementation | MI:0006- anti bait coimmunoprecipitation;16109376;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"";"";""
2618;TUBA1A-TUBB2A complex;;Bovine;P02550,Q148E2;0,281555;MI:0040- electron microscopy;9428769;42.04.05;"";"";""
2625;CDK8-MED6-PARP1 complex;;Human;P49336,O75586,P09874;1024,10001,142;MI:0019- coimmunoprecipitation;15808511;11.02.03.04;"";"";""
2626;CCNC-CDK8-MED1-MED6-MED7 xcomplex;;Human;P24863,P49336,Q15648,O75586,O43513;892,1024,5469,10001,9443;MI:0019- coimmunoprecipitation;15808511;11.02.03.04;"";"";""
2628;CCNC-CDK3 complex;;Human;P24863,Q00526;892,1018;MI:0019- coimmunoprecipitation;15084261;10.03.01.01.02;"A non-cdk8-associated cellular pool of cyclin C combines with cdk3 to stimulate pRb phosphorylation at S807/811 during the G0/G1 transition, and that this phosphorylation is required for cells to exit G0 efficiently.";"";""
2635;BETA2-Cyclin D1 complex;;Human;P24385,Q13562;595,4760;MI:0019- coimmunoprecipitation;11788592;11.02.03.04;"";"";""
2638;HES1 promoter corepressor complex;;Human;P50613,Q92793,Q09472,P24928,Q06330,Q7KZ85;1022,1387,2033,5430,3516,6830;MI:0402- chromatin immunoprecipitation assays;15546612;11.02.03.04.03,16.03.01,70.10;"This complex has been studied on the HES1 promoter (a Notch target gene) in cells without Notch signaling.";"";""
2639;HES1 promoter-Notch enhancer complex;;Human;O60563,P50613,P49336,P50750,Q09472,Q92585,Q15648,P46531,P24928,Q06330,Q9BT40,Q9Y5B9,Q7KZ85;904,1022,1024,1025,2033,9794,5469,4851,5430,3516,51763,11198,6830;MI:0402- chromatin immunoprecipitation assays;15546612;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"After Notch signaling endogenous CDK8 is recruited to the HES1 promoter (a Notch target gene) together with Notch and MAM. Signaling also induces binding of SKIP, as well as two transcription elongation factors, P-TEFb and FACT.";"";""
2641;p300/CBP-PCAF-MyoD complex;;Human;P15172,Q92831,(Q92793,Q09472);4654,8850,(1387,2033);MI:0019- coimmunoprecipitation;9659901;11.02.03.04,41.05.15;"";"";"The transcriptional coactivators p300 and CBP are considered as functional homologs, the authors refer to them as p300/CBP."
2642;SMAD1-P300 complex;;Human;Q09472,Q15797;2033,4086;MI:0007- anti tag coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;10673036;10.01.09.05,11.02.03.04.01,14.07.04,30.05.01.18.01,42.10.03,70.10;"SMAD1 stimulates transcription cooperatively with P300.";"";""
2649;MYC-DNMT3A-ZBTB17 complex;;Human;Q9Y6K1,P01106,Q13105;1788,4609,7709;MI:0019- coimmunoprecipitation;15616584;11.02.03.04,16.03.01;"This complex is involved in a transcriptional silecing of  p21Cip1 promoter.";"";""
2650;DNMT3B-DNMT3L complex;;Human;Q9UBC3,Q9UJW3;1789,29947;MI:0071- molecular sieving;15105426;10.01.09.01;"";"";""
2651;DNMT3L-DNMT3A	complex;;Human;Q9Y6K1,Q9UJW3;1788,29947;MI:0071- molecular sieving;15105426;10.01.09.01;"";"";""
2653;MYC-MAX-BLOC1S1 complex;;Human;P78537,P61244,P01106;2647,4149,4609;MI:0019- coimmunoprecipitation;10611234;18.01.07;"";"";""
2655;MYC-MAX complex;;Human;P61244,P01106;4149,4609;MI:0019- coimmunoprecipitation;12584560;11.02.03.04,16.03.01;"";"";""
2657;ESR1-CDK7-CCNH-MNAT1-MTA1-HDAC2 complex;;Human;P51946,P50613,P03372,Q92769,P51948,Q13330;902,1022,2099,3066,4331,9112;MI:0019- coimmunoprecipitation;12527756;11.02.03.04,14.07.03,18.01.01,18.02,30.01.11,70.10;"The authors identified MAT1 as a target of corepressor MTA1 and provided new evidence to suggest that the transactivation functions of ER are influenced by the regulatory interactions between CAK and MTA1.";"MTA1 is involved in metastasis or cancer formation.";""
2660;ERCC2/CAK complex;;Human;P51946,P50613,P18074,P51948;902,1022,2068,4331;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;8692841;10.01.05.01;"TFIIH* and ERCC2/CAK interact to form the TFIIH holoenzyme capable of efficiently assembling the pol II transcription initiation complex and directly participating in excision repair reactions.";"";""
2670;Er-alpha-p53-hdm2 complex;;Human;P03372,Q00987,P04637;2099,4193,7157;MI:0096- pull down;10766163;18.02.01;"The authors demonstrated that ER-alpha protects p53 from being deactivated by hdm2 in a Luc reporter assay.";"";""
2678;FOXO3-TP53 complex, oxidative stress stimulated;;Human;O43524,P04637;2309,7157;MI:0019- coimmunoprecipitation;14976264;11.02.03.04,32.01.01,70.10;"";"";""
2679;p53-SP1 complex;;Human;P08047,P04637;6667,7157;MI:0006- anti bait coimmunoprecipitation;15674334;11.02.03.04,16.03.01,70.10;"The authors provide evidence that p53 repressed the RECQ4 promoter by forming a complex with the transcription factor, SP1, and by regulating promoter occupancy of both itself and SP1 in concert with histone deacetylase 1 (HDAC1). The formation of this complex is camptothecin-dependent.";"";""
2681;p53 homotetramer complex;;Human;P04637;7157;MI:0031- protein cross-linking with a bifunctional reagent | MI:0276- blue native page;15674341;11.02.03.04,16.03.01,70.10;"The results demonstrate that Ref-1 (redox factor 1) modulates p53 DNA binding not only as a redox regulator but also as a factor, which facilitates the formation of p53 tetramers from higher oligomeric forms as well as from dimers. Ref-1 mediates de-stacking of higher oligomeric forms into individual tetramers, as well as the assembly of dimers into tetramers. Redox-dependent and redox-independent activation of p53 seem to require different amounts of Ref-1.";"";""
2682;Bcl-xL-p53-PUMA complex, DNA damage induced;;Mouse;Q99ML1,Q64373,P02340;170770,12048,22059;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;16151013;40.10.02,70.03;"PUMA appeared to be the major regulator of the p53·Bcl-xL complex after UV treatment because no free cytoplasmic p53 was observed in Puma-/- cytosol. The authors support a model of p53-dependent, DNA damage-induced apoptosis that includes both nuclear and cytoplasmic functions of p53.";"";""
2683;PUMA-Bcl-xL complex, DNA-damage induced;;Mouse;Q99ML1,Q64373;170770,12048;MI:0004- affinity chromatography technologies;16151013;40.10.02,70.03;"The p53-Bcl-xL complex was disrupted by incubation with PUMA. The p53 released from Bcl-xL by PUMA still activated BAX and induced mitochondrial cytochrome c release.";"";""
2684;p53-Bcl-xL complex, DNA-damage induced;;Mouse;Q64373,P02340;12048,22059;MI:0019- coimmunoprecipitation;16151013;40.10.02,70.03;"In the presence of PUMA expression , the amount of p53 associated with Bcl-xL decreased after UV treatment, and this temporally correlated with the induction of apoptosis. PUMA may function to liberate p53 from Bcl-xL.";"";""
2685;RNA polymerase II (RNAPII);;Human;Q9Y5B0,Q00403,P35269,P13984,P24928,P30876,P19387,O15514,P19388,P61218,P62487,P52434,P36954,P52435,P53803,P62875,Q9BWH6;9150,2959,2962,2963,5430,5431,5432,5433,5434,5435,5436,5437,5438,5439,5440,5441,26015;MI:0004- affinity chromatography technologies | MI:0069- mass spectrometry studies of complexes;15282305;11.02.03.01,16.03.01,70.10;"The authors demonstrate the purification of a functionally active human RNAPII by the use of doubly tagged subunits expressed in mammalian cells.";"";""
2686;BRCA1-core RNA polymerase II complex;;Human;P38398,P24928,P30876,P19387,O15514,P19388,P61218,P62487,P52434,P36954,P52435,P53803,P62875;672,5430,5431,5432,5433,5434,5435,5436,5437,5438,5439,5440,5441;MI:0004- affinity chromatography technologies;10725406;11.02.03.01,16.03.01,70.10;"The transcriptional coactivator BRCA1 interacts directly with the core Pol II complex in vitro.";"";""
2688;MT1-MMP-claudin-1 complex;;Human;O95832,P50281;9076,4323;MI:0006- anti bait coimmunoprecipitation;11382769;18.01.07,18.02.01.01.03;"";"";""
2689;Fra1-JunB DNA-protein complex;;Rat;P10158,P24898;25445,24517;MI:0413- electrophoretic mobility shift assay;12371906;11.02.03.04,16.03.01,70.10,75.03.12.03;"Examination of the -1410 to -1362 bp promoter sequence of matrix metalloproteinase 2 (MMP-2) revealed a potential AP-1 complex binding site at -1394 to -1384bp. EMSA studies, combined with single and double antibody studies, indicate the specific binding of Fra1-JunB heterodimers to the AP-1 site using nuclear extracts from fibroblasts cultured under normoxic conditions. The studies demonstrate that a functional AP-1 site mediates MMP-2 transcription in cardiac cells through the binding of distinctive Fra1-JunB and FosB-JunB heterodimers.";"";""
2690;Atf2-c-Jun-c-Myc complex;;Rat;Q00969,P17325,P09416;81647,24516,24577;MI:0019- coimmunoprecipitation;15990869;10.03,11.02.03.04,16.03.01,32.01,70.10;"c-Myc forms a ternary complex with ATF2/c-Jun through its direct binding to ATF2. ATF2/c-Jun complex binds the ATF/CRE DNA motif and c-Myc is recruited to the proximal region of the ATF3 promoter. The authors describe a functional link between the stress response gene ATF3 and the proto-oncogene c-myc.";"";""
2692;SMAD3-SMAD4-cJun-cFos complex;;Human;P01100,P05412,P84022,Q13485;2353,3725,4088,4089;MI:0412- electrophoretic mobility supershift assay;9732876;11.02.03.04.01,16.03.01,30.05.01.18.01,70.10;"";"";""
2693;NFAT-JUN-FOS DNA-protein complex;;Human;P01100,P05412,Q13469;2353,3725,4773;MI:0114- x-ray crystallography;9510247;11.02.03.04.01,16.03.01,36.25.16;"NFAT and heterodimer Fos-Jun cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes.";"";""
2694;ERG-JUN-FOS DNA-protein complex;;Human;P11308,P01100,P05412;2078,2353,3725;MI:0096- pull down | MI:0413- electrophoretic mobility shift assay | MI:0114- x-ray crystallography;11278640;11.02.03.04,16.03.01,70.10;"The authors demonstrated that amino acids Arg(367) and Tyr(371) of the ETS domain, but not Asp374, play an important role in the recruitment of the Jun/Fos heterodimer by Erg. The authors propose that interdependent protein-protein and protein-DNA contacts regulate Erg-Jun/Fos-DNA complex assembly.";"";""
2695;ETS2-FOS-JUN complex;;Human;P15036,P01100,P05412;2114,2353,3725;MI:0096- pull down;9334186;11.02.03.04,16.03.01,70.10;"The results suggest that stromelysin-1 promoter DNA can enhance the ETS2/Fos/Jun interaction, perhaps by stabilizing protein contacts.";"";""
2699;ER-alpha-GRIP1-c-Jun complex;;Human;P03372,Q9Y3R0,P05412;2099,23426,3725;MI:0096- pull down;11477071;11.02.03.04,30.01.11;"The authors showed that ERalpha , c-Jun, and the p160 coactivator GRIP1 can form a multiprotein complex in vitro and in intact cells and that the ERalpha - c-Jun interaction could be crucial for the stability of this complex.";"";""
2700;ER-alpha-c-Jun complex;;Human;P03372,P05412;2099,3725;MI:0096- pull down | MI:0019- coimmunoprecipitation;11477071;11.02.03.04,16.03.01,30.01.11;"All experiments demonstrated that ER-alpha and c-Jun could interact in mammalian cells in a ligand-dependent manner.";"";""
2704;Ectodermin-SMAD4 complex;;Human;Q13485,Q9UPN9;4089,51592;MI:0007- anti tag coimmunoprecipitation;15820681;14.07.05,30.05.01.18.01,70.10;"";"";""
2705;SMAD3-SMAD4-CTCF protein-DNA complex;;Human;P49711,P84022,Q13485;10664,4088,4089;MI:0413- electrophoretic mobility shift assay;12099698;11.02.03.04,16.03.01,30.05.01.18.01,70.10;"The authors demonstrated that TGF-beta increases APP gene transcription in NHAs (normal human astrocytes) through activation of the proximal APP promoter domain, (-488) base pairs (bp) relative to the transcription start site (+1). In the presence of TGF-beta stimulation, Smads 3 and 4 specifically associated with the CTCF-APBbeta complex, likely enhancing APP gene transcription.";"";""
2706;SMAD3-SMAD4-SP1 complex;;Human;P84022,Q13485,P08047;4088,4089,6667;MI:0413- electrophoretic mobility shift assay | MI:0019- coimmunoprecipitation;11432852;11.02.03.04,16.03.01,30.05.01.18.01,70.10;"The authors demonstrated that Sp1 and Smad3/Smad4 are able to bind the endoglin promoter at positions -50/-29 forming a multiprotein complex, and suggest their cooperation in the transcriptional activity of endoglin.";"";""
2707;SMAD3-SMAD4-FOXO3-FOXG1 complex;;Human;P55316,O43524,P84022,Q13485;2290,2309,4088,4089;MI:0007- anti tag coimmunoprecipitation;15084259;11.02.03.04,16.03.01,30.05.01.18.01,70.10,75.03.09;"The results suggest that FoxG1 is a direct inhibitor of the FoxO-Smad transcriptional complex and a blocker of p21Cip1 induction by TGF-beta signals in neuroepithelial cells.";"";""
2708;SMAD3-SMAD4-cJUN complex;;Human;P05412,P84022,Q13485;3725,4088,4089;MI:0096- pull down;10220381;11.02.03.04,30.05.01.18.01,70.10;"On TGF-beta  treatment, Smad3 and Smad4 heteromerize and enter the nucleus, where they can associate with TGF-beta-responsive promoters by binding a discreet DNA sequence and/or AP-1 members bound to AP-1 sites on the same promoter.";"";""
2709;MMP-9-TIMP-1-LRP complex;;Human;Q07954,P14780,P01033;4035,4318,7076;MI:0047- far western blotting | MI:0411- enzyme linked immunosorbent assay;11279011;18.02.01,20.09.18.09.01.01,42.27.01;"The binding to LRP was blocked when excess RAP (39-kDa receptor-associated protein) was incubated along with MMP-9. Further results indicated that MMP-9 directly binds to LRP even in the absence of TIMP-1 and that reduction of MMP-9 abolishes its ability to bind LRP. The authors summarize that LRP is a functional receptor for MMP-9 and confirm that LRP is capable of mediating the cellular uptake of at least three MMPs (MMP-2, MMP-13, and MMP-9).";"";""
2710;LRP-1-Alpha-2-M-annexin VI complex;;Human;P01023,P08133,Q07954;2,309,4035;MI:0019- coimmunoprecipitation;15226301;20.09.18.09.01.01;"Cell surface annexin VI is involved in the binding of 125I-alpha-2M(activated) to LRP-1 at neutral pH and forms ternary complexes with 125I-alpha-2M(activated) and LRP-1 at neutral pH.";"";""
2711;Amyloid beta protein oligomer;;Human;P05067;351;MI:0019- coimmunoprecipitation;15834427;36.25.03.04;"Size fractionation showed that Abeta oligomers, not monomers or fibrils, were responsible for inhibiting long-term potentiation (LTP), and an Abeta antibody again prevented such inhibition.";"";""
2712;Aph1a-Psen1-Ncstn complex;;Mouse;Q8BVF7,P57716,P49769;226548,59287,19164;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0069- mass spectrometry studies of complexes;15146195;14.13.01.01,30.05.02.14,70.02,77.03.01.01.01;"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch.";"";""
2714;Ubiquitin E3 ligase (CHEK1, CUL1);;Human;O14757,Q13616;1111,8454;MI:0019- coimmunoprecipitation;16137618;14.07.05,14.13.01.01,32.01.09,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The Chk1 kinase is a major effector of S phase checkpoint signaling during the cellular response to genotoxic stress. Replicative stress induces the polyubiquitination and degradation of Chk1 in human cells.";"";""
2715;Ubiquitin E3 ligase (CSN1, CSN8, HRT1, SKP1, SKP2, CUL1, CUL2, CUL3);;Human;Q99627,Q13616,Q13617,Q13618,Q13098,P62877,P63208,Q13309;10920,8454,8453,8452,2873,9978,6500,6502;MI:0047- far western blotting;11337588;14.07.05,14.13.01.01,18.01.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. SCF ubiquitin ligases consist of at least four subunits: CUL1 and HRT1 (=ROC1, RBX1), which  harbor a core ubiquitin ligase activity- a variable F-box protein that serves as a substrate receptor- and SKP1, which links the two modules together. Because CSN binds all cullins, it might be a global signal integrator that radiates its output onto various associated ubiquitin ligases to modulate their activity.";"";""
2716;Elongator core complex;;Human;Q6IA86,Q9H9T3,O95163;55250,55140,8518;MI:0029- cosedimentation through density gradients;11714725;11.02.03.01.04,70.10;"The core-Elongator complex does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit.";"";""
2717;Ubiquitin E3 ligase (TRIM25, DDX58);TRIM25 E3 ubiquitin ligase;Human;O95786,Q14258;23586,7706;MI:0096- pull down;17392790;14.07.05,30.01,32.05.05,70.03;"TRIM25 E3 ubiquitin ligase induces the Lys 63-linked ubiquitination of RIG-I, which is crucial for the cytosolic RIG-I signalling pathway to elicit host antiviral innate immunity.";"";""
2718;MAD2-CDC20 complex;;Human;Q12834,Q13257;991,4085;MI:0114- x-ray crystallography;10700282;10.03.01.02,18.01.07,70.10;"The checkpoint protein Mad2 inhibits the activity of the anaphase promoting complex by sequestering Cdc20 until all chromosomes are aligned at the metaphase plate.";"";""
2719;Casein kinase II-HMG1 complex; FCP1-specific kinase complex;Human;P68400,P19784,P67870,P09429;1457,1459,1460,3146;MI:0029- cosedimentation through density gradients;12591939;01.04,14.07.03,18.01.01,18.02.01;"CK2 is comprised of the subunits CK2alpha , CK2alpha ', and CK2beta , and the differences in FCP1 kinase activity among the elution fractions reflect a dose-dependent effect related to the amount of CK2 present but do not depend on the presence of HMG1.";"";""
2720;Casein kinase II complex; CK2 complex | FCP1-specific kinase complex;Human;P68400,P19784,P67870;1457,1459,1460;MI:0029- cosedimentation through density gradients;12591939;01.04,14.07.03,18.01.01,18.02.01;"CK2 phosphorylates FCP1 and RAP74.";"";""
2721;HCF-1 complex; HCF-1-associated protein complex;Human;Q9UBL3,P51610,Q13547,Q92769,P34932,P11021,P11142,O15294,Q09028,Q16576,O75446,O15047,Q96ST3,O75182,P08047,Q9H7L9,P61964,(P07900,P08238);9070,3054,3065,3066,3308,3309,3312,8473,5928,5931,8819,9739,25942,23309,6667,64426,11091,(3320,3326);MI:0007- anti tag coimmunoprecipitation;12670868;10.01.09.05,10.03.03,11.02.03.04,14.07.09,40.01,42.10.03,70.10;"HCF-1 can regulate transcription, both positively and negatively, through selective modulation of chromatin structure.";"";""
2722;Ubiquitin E3 ligase (DDB1, CUL4A, RBX1);;Human;Q13619,Q16531,P62877;8451,1642,9978;MI:0019- coimmunoprecipitation;15448697;14.07.05,14.13.01.01,32.01.09;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The ubiquitin E3 ligase (DDB1, CUL4A and RBX1) perfoms targeted ubiquitination of CDT1 in response to DNA damage.";"";""
2723;ATM-NBS1 complex;;Human;Q13315,O60934;472,4683;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down;10839544;10.03.01.03,14.07.03,30.01.05.01.06,32.01.09,32.01.13,70.10;"NBS1 was co-immunoprecipitated by the ATM antibody from untreated cells and in increased quantities from cells treated with ionizing radiation. The results indicate that phosphorylation of Ser 278 and Ser 343 in NBS1 contributes to both cellular resistance to ionizing radiation and formation of foci that contain NBS1 in response to ionizing radiation.";"";""
2724;Ubiquitin E3 ligase (NFKBIA, BTRC, CUL1, SKP1A);;Human;Q9Y297,Q13616,P25963,P63208;8945,8454,4792,6500;MI:0007- anti tag coimmunoprecipitation;10644755;14.07.05,14.13.01.01,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitination-dependent destruction of NF-kappa-B inhibitor alpha is mediated by ubiquitin E3 ligases containing heterdimers and homodimers of beta-TrCP1 (BTRC) and beta-TrCP2 (FBXW11).";"";""
2725;Ubiquitin E3 ligase (NFKBIA, FBXW11, CUL1, SKP1A);;Human;Q13616,Q9UKB1,P25963,P63208;8454,23291,4792,6500;MI:0007- anti tag coimmunoprecipitation;10644755;14.07.05,14.13.01.01,70.03;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitination-dependent destruction of NF-kappa-B inhibitor alpha is mediated by ubiquitin E3 ligases containing heterdimers and homodimers of beta-TrCP1 (BTRC) and beta-TrCP2 (FBXW11).";"";""
2726;PXN-ITGB5-PTK2 complex;;Human;P18084,Q05397,P49023;3693,5747,5829;MI:0019- coimmunoprecipitation;11278329;30.05.02.26;"The changes in the expression of PAR1 in a cell affect its invasive capabilities. These changes come about through the specific recruitment of the alpha(v)-beta 5 integrin, through cytoskeletal reorganization, and through distinct signaling at FACs.";"";""
2727;SRC-3 complex;;Human;O15111,Q92793,O14920,Q9Y6K9,Q15596,Q9Y6Q9,P10155;1147,1387,3551,8517,10499,8202,6738;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving | MI:0226- ion exchange chromatography;11971985;11.02.03.04.01,14.07.04,30.01.05.01.04,30.01.11,36.25.16.07,70.10;"SRC-3 enhances NF-kappaB-mediated gene expression in concert with IKK.";"";""
2728;SRC-1 complex;;Human;Q92793,Q15788,Q15596,P10155;1387,8648,10499,6738;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving | MI:0226- ion exchange chromatography;11971985;30.01.05.01.04,30.01.11,70.10;"";"";""
2729;PIP complex;;Mouse;O55222,Q99JW4,Q9EPC1;16202,110829,57342;MI:0019- coimmunoprecipitation;15872073;34.07,40.10.02.04,77.03.07.01;"Disruption of the PINCH-1-ILK-alpha-parvin complex significantly reduced the podocyte-matrix adhesion and foot process formation. The PIP complex promotes glomerular mesangial matrix deposition and protects podocytes from apoptosis.";"";""
2730;Set1B complex;;Human;Q9UBL3,Q8ND76,Q15291,Q9UPS6,P61964,Q6UXN9;9070,219771,5929,23067,11091,80335;MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;17355966;10.01.09.05,10.01.09.07,14.07.09,16.03.01,42.10.03,70.10,77.03.07.01;"The SET1B complex is a methyltransferase that produces trimethylated histone H3 at Lysine 4.";"";""
2731;Set1A complex; SET1-CFP1 complex;Human;Q9UBL3,Q8ND76,Q15291,O15047,P61964,Q6UXN9;9070,219771,5929,9739,11091,80335;MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;17355966;10.01.09.05,10.01.09.07,14.07.09,16.03.01,42.10.03,70.10,77.03.07.01;"The SET1A complex is a methyltransferase that produces mono-di- and trimethylated histone H3 at Lysine 4.";"";""
2732;Translocon-associated protein complex (TRAP complex);;Dog;P16967,P23438,Q9UNL2,P51571;403951,403950,6747,6748;MI:0004- affinity chromatography technologies;7916687;14.04,16.17.01,70.07;"TRAP complex regulates the retention of ER resident proteins.";"";"Since SSR4 and SSR3 from dog were not available in the UniProt database at the time of annotation, the orthologous human protein was used. "
2733;Aph1a-pPsen1-nNcstn complex;;Rat;Q5PQQ3,Q8CGU6,P97887;365872,289231,29192;MI:0007- anti tag coimmunoprecipitation;12297508;14.13.01.01,30.05.02.14,70.02,77.03.01.01.01;"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. The authors use the splice variant mAPH-1a-L for the coimmunoprecipitation experiment. The authors show that endogenous mAPH-1, nicastrin, and the presenilin NTF:CTF heterodimers physically interact with each other in vivo and under the conditions that are compatible with gamma-secretase activity.";"";""
2734;APH1A-PSEN1-NCSTN complex;;Human;Q96BI3,Q92542,P49768;51107,23385,5663;MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down;12297508;14.13.01.01,30.05.02.14,70.02,77.03.01.01.01;"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. The authors use the splice variant mAPH-1a-L for  experiments.";"";""
2735;APH1A-PSEN2-NCSTN complex;;Human;Q96BI3,Q92542,P49810;51107,23385,5664;MI:0007- anti tag coimmunoprecipitation;12297508;14.13.01.01,30.05.02.14;"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. The authors use the splice variant mAPH-1a-L for  experiments. In an additional pull down experiment the authors show the interaction of APH1B with presenilin 2.";"";""
2736;TAJ-NgR1-LINGO-1 signaling complex;;Human;Q96FE5,Q9BZR6,Q9NS68;84894,65078,55504;MI:0019- coimmunoprecipitation;15694322;18.01.07,18.02.05,41.05.13,73.03.13,75.03.17,77.03.01.01;"The authors additionally analyzed interactions between TAJ-NgR1 and TAJ-LINGO-1. The authors show that TAJ (an orphan receptor in the TNF family), broadly expressed in postnatal and adult neurons, binds to NgR1 and can replace p75 in the p75/NgR1/LINGO-1 complex to activate RhoA in the presence of myelin inhibitors.";"";""
2738;BLM complex II; BLM-CII complex;Human;P54132,Q9H9A7,P27694,P15927,P35244,Q13472;641,80010,6117,6118,6119,7156;MI:0006- anti bait coimmunoprecipitation;12724401;10.01.02,10.01.05.01,32.01.09,70.10;" ";"BLM complex II is involved in Bloom syndrome (BS).";"Another subunit of the complex was found in the analysis, which has not been further characterized: BLAPp100."
2739;FA complex (Fanconi anemia complex);;Human;P54132,O15360,Q8NB91,Q00597,Q9HB96,Q9NPI8,O15287,Q9NW38,Q9H9A7,P27694,Q13472;641,2175,2187,2176,2178,2188,2189,55120,80010,6117,7156;MI:0006- anti bait coimmunoprecipitation;12724401;14.07.05,32.01.09,70.10;"The FA complex contains several other proteins of unknown function, called FAAPs. ";"FA complex is involved in Fanconi anemia (FA) disease.";""
2740;MutS-alpha complex; MSH2-MSH6 complex;Human;P43246,P52701;4436,2956;MI:0019- coimmunoprecipitation;7604264;10.01.05.01,32.01.09,70.10;"The mismatch DNA repair complex hMSH2-MSH6, regulates BLM helicase activity.";"";""
2742;Gata2-Tal1-Tcf3-Lmo2 complex;;Mouse;O09100,P25801,P22091,P15806;14461,16909,21349,21423;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;7568177;11.02.03.04,43.03.07,70.10;"Complexes involving RBTN2, TAL1, and GATA1 (or -2), together with E47, the basic helix-loop-helix heterodimerization partner of TAL1, could be demonstrated. Thus, a molecular link exists between three proteins crucial for erythropoiesis, and the data suggest that variations in amounts of complexes involving RBTN2, TAL1, and GATA1 (or -2) could be important for erythroid differentiation.";"";""
2743;TRAF6-MALT1 complex;;Human;Q9UDY8,Q9Y4K3;10892,7189;MI:0019- coimmunoprecipitation;15125833;18.02.01.01,73.03.07.02.01;"The CARD domain protein BCL10 and paracaspase MALT1 are essential for the activation of IkappaB kinase (IKK) and NF-kappaB in response to T cell receptor (TCR) stimulation. TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by BCL10 and MALT1. MALT1 binds to TRAF6 through the C-terminal binding sites and induces the oligomerization of TRAF6 to activate IKK.";"";""
2744;TRAF2-MALT1 complex;;Human;Q9UDY8,Q12933;10892,7186;MI:0019- coimmunoprecipitation;15125833;18.02.01.01,73.03.07.02.01;"";"";""
2745;Ubiquitin ligase complex (TRAF6, TAB2, MALT1, UEV1A, BCL10);;Human;O95999,Q9UDY8,Q9NYJ8,Q9Y4K3,Q13404;8915,10892,23118,7189,387522;MI:0019- coimmunoprecipitation;15125833;14.07.05,18.02.01.01,73.03.07.02.01;"The TRAF6 ubiquitin ligase and TAK1 kinase mediate IkappaB kinase (IKK) activation by BCL10 and MALT1 in T lymphocytes. NF-kappaB is a ubiquitous transcription factor that plays a central role in many biological processes including innate and adaptive immunity. NF-kappaB is regulated primarily through its association with an inhibitory protein of the IkappaB family, which binds to and retains NF-kappaB in the cytoplasm.";"";""
2746;NMDA receptor complex;;Rat;P35439,Q00959,Q9R1M7;24408,24409,191573;MI:0019- coimmunoprecipitation;11160393;14.04,14.10,18.02.10,70.02,70.07;"Glutamate receptors of the NMDA subtype are involved in a number of physiological and pathological processes in the brain, including synaptic plasticity, refinement of synaptic connections during development, and excitotoxicity.  Heteromeric combinations of NR1 and NR2 subunits are characterized by a high relative Ca21 permeability.  NR3A associates independently with both NR1-1a and NR2A in the endoplasmic reticulum, but only heteromeric complexes containing the NR1-1a NMDA receptor subunit are targeted to the plasma membrane.";"";""
2747;Gata1-Fog1 complex;;Mouse;P17679,O35615;14460,22761;MI:0019- coimmunoprecipitation;15920471;11.02.03.04,18.01.07,18.02.09,70.10;"GATA-1 functions as both an activator and a repressor. The Gata-1-Fog-1 complex has been shown to repress some genes, such as GATA-2, and activate others, such as beta-globin or the EKLF gene. Fog-1 mediates Gata-1 interactions with the MeCP1 complex, thus providing an explanation for the overlapping functions of these two factors in erythropoiesis.";"";""
2748;Ubiquitin-protein ligase (UBE2N, UBE2V2/MMS2);TRIKA1;Human;P61088,Q13404;7334,387522;MI:0071- molecular sieving;11057907;14.07.05,18.01.01,18.02.01.01.05,30.07;"TRAF6 is a signal transducer that activates IkappaB kinase (IKK) and Jun  amino-terminal kinase (JNK) in response to pro-inflammatory mediators  such as interleukin-1 (IL-1) and lipopolysaccharides (LPS). IKK  activation by TRAF6 requires two intermediary factors, TRAF6-regulated  IKK activator 1 (TRIKA1) and TRIKA2. TRIKA1 is a dimeric  ubiquitin-conjugating enzyme complex composed of UBE2N and UBE2V1 or the  functionally equivalent UBE2V2 (complex 2756). This Ubiquitin-protein ligase complex,  together with TRAF6, catalyses the formation of a Lys 63 (K63)-linked  polyubiquitin chain that mediates IKK activation through a unique  proteasome-independent mechanism.";"";""
2749;SETDB1-containing HMTase complex; ESET-SETDB1 complex;Human;Q6VMQ6,Q15047;55729,9869;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving | MI:0226- ion exchange chromatography;14536086;10.01.09.05,11.02.03.04.03,11.02.03.04.07,14.07.09,42.10.03,70.10;"ATF7IP stimulates the HMTase activity of ESET (SETDB1) through facilitating the ESET-dependent conversion of dimethyl H3-K9 to the trimethyl state.";"";""
2750;Gata1-Fog1-MeCP1 complex;;Mouse;Q6PDQ2,P17679,Q8VHR5,O09106,P70288,Q9Z2E1,Q9Z2D8,Q8K4B0,Q9R190,Q924K8,Q60972,Q60973,O35615;107932,14460,229542,433759,15182,17191,17192,116870,23942,116871,19646,245688,22761;MI:0019- coimmunoprecipitation;15920471;10.01.09.05,11.02.03.04.03,42.10.03,70.10;"Experiments strongly suggest that GATA-1, FOG-1 and MeCP1 form the repressive complex responsible for GATA-2 silencing.";"";""
2752;CARMA1-BCL10-MALT1 complex;;Human;O95999,Q9BXL7,Q9UDY8;8915,84433,10892;MI:0019- coimmunoprecipitation;17478723;30.01.05.01.04,70.02;"The multiprotein complex consisting of the membrane-associated adapter protein CARMA1, the caspase-like protein MALT1, and the adapter protein BCL-10 is critical for TCR-dependent activation of the I{kappa}B kinase complex and subsequent NF-{kappa}B nuclear translocation.";"";""
2753;FYB-CARMA1-BCL-10-MALT1 complex;;Human;O95999,Q9BXL7,O15117,Q9UDY8;8915,84433,2533,10892;MI:0019- coimmunoprecipitation;17478723;30.01.05.01.04,70.02;"FYB (ADAP) was found to be an integral part of the multiprotein complex consisting of the membrane-associated adapter protein CARMA1, the caspase-like protein MALT1, and the adapter protein BCL-10, which is critical for TCR-dependent activation of the I{kappa}B kinase complex and subsequent NF-{kappa}B nuclear translocation.";"";""
2754;JUND-FOSB-SMAD3-SMAD4 complex; TRE binding complex;Human;P53539,P17535,P84022,Q13485;2354,3727,4088,4089;MI:0412- electrophoretic mobility supershift assay;10942775;11.02.03.04,30.05.01,40.10.02.03,70.10;"The authors found that only JunD and FosB, but not the other components of the AP-1 complex, are markedly induced during TGF-beta 1-dependent apoptosis. FosB enhanced Smad3·Smad4-dependent transcription, and its dominant-negative form blocked TGF-beta 1-dependent apoptosis but not growth inhibition. These results suggest that JunD·FosB activates transcription of a putative target gene for TGF-beta 1, which is responsible for apoptosis.";"";""
2755;17S U2 snRNP;;Human;Q8IWX8,Q7L014,O43143,O75937,Q9P0W2,P10809,Q7RTV0,Q9UHX1,Q96I25,Q15459,Q15428,Q12874,O75533,Q9Y3B4,Q13435,Q15393,Q15427,Q9BWJ5,Q07955,O75940,P09661,P14678,P08579,P62314,P62316,P62318,P62304,P62306,P62308,O15042,Q12931,Q01081,P26368;10523,9879,1665,22826,10362,3329,84844,22827,84991,10291,8175,10946,23451,51639,10992,23450,10262,83443,6426,10285,6627,6628,6629,6632,6633,6634,6635,6636,6637,23350,10131,7307,11338;MI:0019- coimmunoprecipitation;12234937;11.04.03.01,70.10;"Spliceosome assembly is initiated by the interaction of the U1 snRNP with the 5' splice site, forming the E complex. The latter also contains the 17S U2 snRNP, which at this stage associates via a non-base pairing interaction. In a subsequent ATP-dependent step, the U2 snRNA base pairs with the branch site of the pre-mRNA leading to stable association of the U2 snRNP and formation of the so-called A complex or prespliceosome.";"";""
2756;Ubiquitin-protein-ligase (UBE2N, UBE2V2/MMS2); TRIKA1;Human;P61088,Q15819;7334,7336;MI:0019- coimmunoprecipitation;11460167;14.07.05,18.01.01,18.02.01.01.05,30.07;"TRAF6 is a signal transducer that activates IkappaB kinase (IKK) and Jun  amino-terminal kinase (JNK) in response to pro-inflammatory mediators  such as interleukin-1 (IL-1) and lipopolysaccharides (LPS). IKK  activation by TRAF6 requires two intermediary factors, TRAF6-regulated  IKK activator 1 (TRIKA1) and TRIKA2. TRIKA1 is a dimeric  ubiquitin-conjugating enzyme complex composed of UBE2N and UBE2V1 or the  functionally equivalent UBE2V2. This Ubiquitin-protein ligase complex,  together with TRAF6, catalyses the formation of a Lys 63 (K63)-linked  polyubiquitin chain that mediates IKK activation through a unique  proteasome-independent mechanism.";"";""
2757;SMN complex, U7 snRNA specific;;Human;Q969L4,P83369,P14678,P62318,P62304,P62306,P62308;84967,134353,6628,6634,6635,6636,6637;MI:0019- coimmunoprecipitation;12975319;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"The Lsm11 protein of the U7 snRNA specific SMN complex plays an important role in histone RNA 3' end processing. ";"Spinal muscular atrophy (SMA)";""
2758;TRIKA2 protein kinase complex (TAK1, TAB1, TAB2);;Human;Q15750,Q9NYJ8,Q9NZ70;10454,23118,6885;MI:0091- chromatography technologies | MI:0019- coimmunoprecipitation;11460167;14.07.03,18.01.01,18.02.01.01.05,30.07;"TRAF6 is a signal transducer that activates IkappaB kinase (IKK) and Jun  amino-terminal kinase (JNK) in response to pro-inflammatory mediators  such as interleukin-1 (IL-1) and lipopolysaccharides (LPS). IKK  activation by TRAF6 requires two intermediary factors, TRAF6-regulated  IKK activator 1 (TRIKA1) and TRIKA2.";"";""
2759;MBD1-MCAF complex;;Human;Q6VMQ6,Q9UIS9;55729,4152;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;12665582;10.01.09.05,11.02.03.04.03,42.10.03,70.10;"MBD1 directly prevents transcription from methylated promoters in a histone deacetylation-independent manner, through interacting with MCAF. MBD1 competes with Sp1 for binding to MCAF. MBD1-MCAF complex blocks transcription through affecting Sp1 on methylated promoter regions.";"";""
2760;SMAD3-SMAD4-FOXO3 complex;;Human;O43524,P84022,Q13485;2309,4088,4089;MI:0007- anti tag coimmunoprecipitation;15084259;11.02.03.04,16.03.01,30.05.01.18.01,70.10,75.03.09;"Endogenous FoxO1, FoxO3, and FoxO4 bind to endogenous Smad2/3 and Smad4. Formation of these complexes was absolutely dependent on TGF-beta stimulation, as was the formation of a Smad2/3-Smad4 complex.";"";""
2761;SMAD3-SMAD4-FOXO1 complex;;Human;Q12778,P84022,Q13485;2308,4088,4089;MI:0007- anti tag coimmunoprecipitation;15084259;11.02.03.04,16.03.01,30.05.01.18.01,70.10,75.03.09;"Endogenous FoxO1, FoxO3, and FoxO4 bind to endogenous Smad2/3 and Smad4. Formation of these complexes was absolutely dependent on TGF-beta stimulation, as was the formation of a Smad2/3-Smad4 complex.";"";""
2762;SMAD3-SMAD4-FOXO4 complex;;Human;P98177,P84022,Q13485;4303,4088,4089;MI:0007- anti tag coimmunoprecipitation;15084259;11.02.03.04,16.03.01,30.05.01.18.01,70.10,75.03.09;"Endogenous FoxO1, FoxO3, and FoxO4 bind to endogenous Smad2/3 and Smad4. Formation of these complexes was absolutely dependent on TGF-beta stimulation, as was the formation of a Smad2/3-Smad4 complex.";"";""
2763;MBD1-Suv39h1-HP1 complex;;Human;P45973,Q9UIS9,O43463;23468,4152,6839;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;12711603;10.01.09.07,11.02.03.04.03,14.07.09,70.10;"MBD1 tethers the Suv39h1-HP1 complex to methylated DNA regions. MBD1 interacts with Suv39h1-HP1 complex via MBD domain.";"";""
2764;PRMT5 complex;;Human;O14744;10419;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;11152681;14.07.09,70.03;"PRMT5 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer. Recombinant PRMT5 protein methylates myelin basic protein, histone, and the amino terminus of fibrillarin.";"";""
2765;PRMT1 complex;;Human;Q99873;3276;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;11152681;14.07.09,70.10;"PRMT1 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer.";"";""
2766;TERF2-RAP1 complex;;Human;P49959,Q92878,Q15554,Q9NYB0,Q9BSI4,P13010,P12956;4361,10111,7014,54386,26277,7520,2547;MI:0007- anti tag coimmunoprecipitation;15383534;16.03.01,32.01.09,42.10.03,70.10;"This complex is responsible for proper maintenance of telomere length and structure.";"";""
2767;RAD50-MRE11-NBN-p200-p350 complex;;Human;P49959,O60934,Q92878;4361,4683,10111;MI:0006- anti bait coimmunoprecipitation;8756642;01.03.16.03,10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;" ";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: p350 and p200. "
2768;IKK complex (NEMO, IKKB);;Rat;Q9QY78,Q6TMG5;84351,309295;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;17419723;14.07.03,16.03.01,18.02.01.01.05;"NEMO molecules do not form a tripartite IKK complex with an IKKalpha-IKKbeta heterodimer.  NEMO is able to form a complex with the monomeric forms of IKKalpha and IKKbeta.";"";""
2769;IKK complex (NEMO);;Rat;Q6TMG5;309295;MI:0029- cosedimentation through density gradients;17419723;14.07.03,16.03.01,18.02.01.01.05;"";"";""
2770;ITGA6-ITGB4-CD9 complex; integrin complex;Human;P21926,P23229,P16144;928,3655,3691;MI:0024- confirmational text mining;10711425;34.05,77.03.02.05;"";"";""
2771;RAD51-DMC1 complex;;Mouse;Q61880,Q08297;13404,19361;MI:0416- fluorescence microscopy | MI:0040- electron microscopy;11950880;10.01.05.01,10.01.05.03.01,70.10;"";"";""
2772;Ubiquitin E3 ligase (CRY1, SKP1A, CUL1, FBXL3); SCF(FBXL3) ubiquitin ligase complex;Human;Q16526,Q13616,Q9UKT7,P63208;1407,8454,26224,6500;MI:0007- anti tag coimmunoprecipitation;17463251;14.07.05,14.13.01.01,34.11.11,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Cry1 and Cry2, encode inhibitors of the Clock-Bmal1 complex that establish a negative-feedback loop. Cry1 and Cry2 proteins are ubiquitinated and degraded via the SCF(Fbxl3) ubiquitin ligase complex. This regulation by SCF(Fbxl3) is a prerequisite for the efficient and timely reactivation of Clock-Bmal1 and the consequent expression of Per1 and Per2, two regulators of the circadian clock that display tumor suppressor activity.";"";""
2773;Ubiquitin E3 ligase (CRY2, SKP1A, CUL1, FBXL3); SCF(FBXL3) ubiquitin ligase complex;Human;Q49AN0,Q13616,Q9UKT7,P63208;1408,8454,26224,6500;MI:0007- anti tag coimmunoprecipitation;17463251;14.07.05,14.13.01.01,34.11.11,70.10;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Cry1 and Cry2, encode inhibitors of the Clock-Bmal1 complex that establish a negative-feedback loop. Cry1 and Cry2 proteins are ubiquitinated and degraded via the SCF(Fbxl3) ubiquitin ligase complex. This regulation by SCF(Fbxl3) is a prerequisite for the efficient and timely reactivation of Clock-Bmal1 and the consequent expression of Per1 and Per2, two regulators of the circadian clock that display tumor suppressor activity.";"";""
2774;MDC1-H2AFX-TP53BP1 complex;;Human;P16104,Q14676,Q12888;3014,9656,7158;MI:0006- anti bait coimmunoprecipitation;12607005;10.01.05.01,10.03.01.03,16.03.01,32.01.09,70.10;"MDC1 forms complexes with phosporylated H2AFX.";"";""
2775;MDC1-p53BP1-SMC1 complex;;Human;Q14676,Q14683,Q12888;9656,8243,7158;MI:0006- anti bait coimmunoprecipitation;12607005;10.01.05.01,10.03.01.03,16.03.01,70.10;"Interaction of MDC1 with 53BP1 and SMC1 is unaffected by DNA damage.";"";""
2776;RAD50-BRCA1 complex;;Human;P38398,Q92878;672,10111;MI:0007- anti tag coimmunoprecipitation | MI:0226- ion exchange chromatography;11504724;10.01.05.01,70.10;"";"BRCA1 is involved in breast cancer.";""
2777;Ecsit complex (Ecsit2-Smad4);;Mouse;Q9QZH6,P97471;26940,17128;MI:0006- anti bait coimmunoprecipitation;14633973;30.05.01.18.01,41.05.04;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. A mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated.The authors focused on Ecsit isoform 2 because it is the only Ecsit isoform expressed in P19 cells. Ecsit2 could be coprecipitated with Smad4 from both treated and untreated cells, while Smad1 coprecipitated with Ecsit2 only after Bmp4 treatment.";"";""
2778;Ecsit complex (Ecsit2-Smad1);;Mouse;Q9QZH6,P70340;26940,17125;MI:0006- anti bait coimmunoprecipitation;14633973;30.05.01.18.01,41.05.04;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. A mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. The authors focused on Ecsit2 because it is the only Ecsit isoform expressed in P19 cells. Ecsit2 could be coprecipitated with Smad4 from both treated and untreated cells, while Smad1 coprecipitated with Ecsit2 only after Bmp4 treatment. It seems that association of Ecsit2 with Smad1 is dependent on phosphorylation of Smad1 by ligand-activated Bmpr1a.";"";""
2779;Ecsit complex (Smad1-Smad4-Ecsit2);;Mouse;Q9QZH6,P70340,P97471;26940,17125,17128;MI:0006- anti bait coimmunoprecipitation;14633973;11.02.03.04,16.03.01,30.05.01.18.01,41.05.04,70.10;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. A mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. The authors focused on Ecsit2 because it is the only Ecsit isoform expressed in P19 cells. The authors describe that in resting cells, Ecsit binds constitutively to Smad4 and the Ecsit:Smad4 complex binds to promoters of certain target genes, without activating transcription. When the Bmp pathway is activated, phosphorylated Smad1 translocates to the nucleus and binds to the Ecsit:Smad4 complex to form a higher-order complex containing Ecsit, Smad1, and Smad4.";"";""
2780;Rab1-GTP-GM130 complex;;Rat;Q62839,Q6NYB7;64528,81754;MI:0096- pull down;11285137;20.09.07.03,20.09.07.25,20.09.07.27,70.08;"Interaction of GM130 was specific for the active GTP-bound conformation of Rab1. Since GM130 can directly interact with p115 the authors demonstrated that immunodepletion of p115 had no effect on Rab1-GM130 interaction.";"";""
2781;Rab1-GTP-p115 complex;;Rat;Q6NYB7,P41542;81754,56042;MI:0096- pull down;11285137;20.09.07.03,20.09.07.25,20.09.07.27,70.08;"The authors demonstrated that Rab1-GTP interacts with two different tethering factors - p115 and the GM130 complex.";"";""
2782;Rab1-GTP-GM130-GRASP65 complex;;Rat;Q62839,O35254,Q6NYB7;64528,56082,81754;MI:0096- pull down | MI:0019- coimmunoprecipitation;11285137;20.09.07.03,20.09.07.25,20.09.07.27,70.08;"The authors demonstrate that the cis-Golgi tethering protein GM130 forms a novel Rab1 effector complex that interacts with activated Rab1-GTP in a p115-independent manner and is required for coat protein II vesicle targeting/fusion with the cis-Golgi.";"";""
2783;BARD1-BRCA1-CSTF64 complex;;Human;Q99728,P38398,P33240;580,672,1478;MI:0006- anti bait coimmunoprecipitation;11257228;11.04.03.05,32.01.09,70.10;"DNA damage increases formation of a CstF-BARD1-BRCA1 inhibitory complex. Complex formation represses polyadenylation of mRNA. ";"BRCA1 is involved in breast cancer.";""
2784;Alpha-2-M enhanceosome DNA-protein complex;;Rat;P12841,P17325,P06536,P31503,P52631;314322,24516,24413,171068,25125;MI:0225- chromatin immunoprecipitation array;14522952;11.02.03.04.01,16.03.01,70.10;"Analysis done after IL-6 and Dex (Dexamethasone) treatment. The authors describe the association of severel proteins with the chromosomal (alpha)2-M enhanceosome and analyze the time course of assembly, disassembly, and stability of the enhanceosome.";"";""
2785;Alpha-2-M enhanceosome DNA-protein complex;;Rat;P17325,P06536,P31503,P52631;24516,24413,171068,25125;MI:0225- chromatin immunoprecipitation array;14522952;11.02.03.04.01,16.03.01,70.10;"Analysis done after IL-6 and Dex (Dexamethasone) treatment. The authors describe the association of severel proteins with the chromosomal (alpha)2-M enhanceosome and analyze the time course of assembly, disassembly, and stability of the enhanceosome. They suggest a model of the sequential formation of complexes leading to the activation of the (alpha)2-M gene. OCT-1 and c-Jun bind constitutively the (alpha)2-M promoter. Dex-activated GR is recruited to the complex, possibly by interacting with c-Jun. IL-6 treatment recruits STAT3 to the complex, and STAT3 alone is competent to recruit Pol II and stimulate low levels of transcription.";"";""
2786;BRCA1 A complex;;Human;Q99728,P38398,Q6UWZ7,Q96RL1;580,672,84142,51720;MI:0019- coimmunoprecipitation;17525340;10.01.05.01,10.03.01.03,32.01.13,70.10;"";"BRCA1 is involved in breast cancer.";""
2787;BRCA1 C complex;;Human;Q99728,P38398,Q99708,Q96RL1;580,672,5932,51720;MI:0019- coimmunoprecipitation;17525340;10.01.05.03,10.03.01.03,70.10;"";"BRCA1 is involved in breast cancer.";""
2788;BRCA1 B complex;;Human;O14867,Q99728,P38398;571,580,672;MI:0019- coimmunoprecipitation;17525340;10.01.05.03,70.10;"";"BRCA1 is involved in breast cancer.";""
2789;ETS2-ERG complex;;Human;P11308,P15036;2078,2114;MI:0096- pull down | MI:0018- two hybrid;9334186;11.02.03.04,16.03.01,70.10;"The authors found that different domains of ETS2 make contacts with the Fos/Jun complex and with other members of the Ets family to form stable heterotrimeric ETS2/Fos/Jun and heterodimeric ETS2/ERG and ETS2/ETS1 complexes.";"";""
2790;ETS2-ETS1 complex;;Human;P14921,P15036;2113,2114;MI:0096- pull down | MI:0018- two hybrid;9334186;11.02.03.04,16.03.01,70.10;"The authors found that different domains of ETS2 make contacts with the Fos/Jun complex and with other members of the Ets family to form stable heterotrimeric ETS2/Fos/Jun and heterodimeric ETS2/ERG and ETS2/ETS1 complexes.";"";""
2791;MCM4-MCM6-MCM7 complex;;Human;P33991,Q14566,P33993;4173,4175,4176;MI:0091- chromatography technologies;9305914;01.04,10.01.02,10.01.03,16.19.03,70.10;"This complex has DNA helicase activity.";"";""
2792;MCM2-MCM4-MCM6-MCM7 complex;;Human;P49736,P33991,Q14566,P33993;4171,4173,4175,4176;MI:0091- chromatography technologies | MI:0029- cosedimentation through density gradients;9305914;01.04,10.01.02,10.01.03,16.19.03,70.10;"This complex has DNA helicase activity.";"";""
2793;Brd4-Rfc complex;;Mouse;Q9ESU6,P35601,Q9WUK4,Q8R323,Q3UI84,Q9D0F6;57261,19687,19718,69263,106344,72151;MI:0007- anti tag coimmunoprecipitation;12192049;10.03.01,10.03.01.01.03,70.10;"BRD4 regulates cell cycle progression from G1 to S phase by interacting with RFC1.";"";""
2794;ATF2-c-Jun complex;;Rat;Q00969,P17325;81647,24516;MI:0019- coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;15990869;10.03,11.02.03.04,16.03.01,32.01,70.10;"The authors conclude that ATF2 and c-Jun are activated to bind to the ATF/CRE promoter motif in vivo, and c-Myc is also recruited to this region of ATF3 in response to serum.";"";""
2796;FosB-JunB DNA-protein complex;;Rat;P13346,P24898;14282,24517;MI:0413- electrophoretic mobility shift assay;12371906;11.02.03.04,16.03.01,70.10,75.03.12.03;"Examination of the -1410 to -1362 bp promoter sequence of matrix metalloproteinase 2 (MMP-2) revealed a potential AP-1 complex binding site at -1394 to -1384bp. EMSA studies, combined with single and double antibody studies, indicate the specific binding of FosB-JunB heterodimers to the AP-1 site using nuclear extracts from fibroblasts cultured under hypoxic conditions. The studies demonstrate that a functional AP-1 site mediates MMP-2 transcription in cardiac cells through the binding of distinctive Fra1-JunB and FosB-JunB heterodimers.";"";"Since FosB from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
2797;PCNA-CHL12-RFC2-5 complex;;Human;Q8WVB6,P12004,P35250,P40938,P35249,P40937;63922,5111,5982,5983,5984,5985;MI:0007- anti tag coimmunoprecipitation;12171929;10.01.03,70.10;"CHL12-RFC2-5 functions as a novel clamp loader protein.";"";""
2798;MMP-2-claudin-1 complex;;Human;O95832,P08253;9076,4313;MI:0006- anti bait coimmunoprecipitation;11382769;18.01.07,18.02.01.01.03;"";"";""
2799;RFC complex; Replication factor C complex;Human;P35251,P35250,P40938,P35249,P40937;5981,5982,5983,5984,5985;MI:0019- coimmunoprecipitation;9488738;01.04,10.01.03,10.01.05.01,10.03.01.03,16.03.01,70.10;"Assembly of RFC complex involves distinct subunit interations: RFC5 and RFC3 interact with the RFC4 subunit and RFC2 interacts with RFC5 and RFC4. RFC1 interacts primarily with RFC3 and RFC2. RFC complex functions as clamp loader. The complex is necessary for loading of PCNA onto dsDNA.";"";""
2800;SNARE complex (STX1A, CPLX2, SNAP-25, VAMP2);;Bovine;Q9TRF1,P84088,P32850,P63026;540853,281711,788566,282116;MI:0019- coimmunoprecipitation;12200427;20.09.07.27,20.09.16.09.05,77.03.01.01.01;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.";"";""
2801;OCT4-SOX2 DNA-protein complex;;Human;Q01860,P48431;5460,6657;MI:0413- electrophoretic mobility shift assay;12923055;11.02.03.04,16.03.01,41.05.04.01,70.10;"The authors analyzed the interaction of the two transcription factors Oct4 with Sox2 on the DNA enhancers of FGF4 (fibroblast growth factor 4) and UTF1 (undifferentiated transcription factor 1). The structural models revealed that the FGF4 and the UTF1  enhancers mediate the assembly of distinct POU/HMG-domain complexes, leading to different quaternary arrangements by swapping protein-protein interaction surfaces of Sox2.";"";""
2802;OCT1-SOX2 DNA-protein complex;;Human;P14859,P48431;5451,6657;MI:0413- electrophoretic mobility shift assay | MI:0114- x-ray crystallography;12923055;11.02.03.04,16.03.01,41.05.04.01,70.10;"The authors analyzed the interaction of the two transcription factors Oct1 with Sox2 on the DNA enhancers of FGF4 (fibroblast growth factor 4) and UTF1 (undifferentiated transcription factor 1). The structural models revealed that the FGF4 and the UTF1  enhancers mediate the assembly of distinct POU/HMG-domain complexes, leading to different quaternary arrangements by swapping protein-protein interaction surfaces of Sox2.";"";""
2803;PAX6-SOX2 DNA-protein complex;;Human;P26367,P48431;5080,6657;MI:0413- electrophoretic mobility shift assay;12923055;11.02.03.04,16.03.01,41.05.04.03,47.03.02.02,70.10;"The authors analyzed the interaction of the two transcription factors Pax6 with Sox2 on the DNA enhancer of DC5. It was demonstrated that the same Sox2 interface (the C-terminal region of HMG) is required for heterodimer formation with Oct4 on FGF4 and with Pax6 on DC5, although these two Sox2 partners are members of different transcription factor families and, as such, both unrelated in sequence and structure.";"";""
2804;CTF18-cohesion-RFC complex; CTF18-RFC complex;Human;Q8WVB6,Q8WV66,Q9BVC3,P35250,P40938,P35249,P40937;63922,54921,79075,5982,5983,5984,5985;MI:0007- anti tag coimmunoprecipitation;12930902;01.04,10.01.03,10.03.04.05,16.03.01,42.10.03,70.10;"CTF18-RFC complex interacts with PCNA homotrimer in the pressence of ATP and loads PCNA onto primed and gapped circular DNA, but not onto nicked or single-stranded circular DNA.";"";""
2805;CTF8-DCC1 subcomplex;;Human;Q8WV66,Q9BVC3;54921,79075;MI:0007- anti tag coimmunoprecipitation;12930902;10.03.04.05,16.01,42.10.03,70.10;"";"";""
2806;CTF8-CTF18-DCC1 subcomplex;;Human;Q8WVB6,Q8WV66,Q9BVC3;63922,54921,79075;MI:0007- anti tag coimmunoprecipitation;12930902;10.03.04.05,16.01,42.10.03,70.10;"";"";""
2808;RAD9-RAD1-HUS1-APE1 complex; 9-1-1-APE1 complex;Human;P27695,O60921,O60671,Q99638;328,3364,5810,5883;MI:0096- pull down | MI:0006- anti bait coimmunoprecipitation;17426133;01.03.16,10.01.05.01,10.03.01.03,32.01.09,70.10;"The 9-1-1 complex specifically stimulates the endonuclease activity of APEX1 for DNA repair.";"";""
2809;9-1-1 complex; RAD9-RAD1-HUS1 complex | 9-1-1 complex | RHR complex;Human;O60921,O60671,Q99638;3364,5810,5883;MI:0096- pull down;17426133;10.01.05.01,10.03.01.03,32.01.09,70.10;"";"";""
2810;Rad17-RFC complex; RSR complex;Human;O75943,P35250,P40938,P35249,P40937;5884,5982,5983,5984,5985;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;14624239;01.04,10.03.01.03,16.03.01,16.19.03,32.01.09,70.10;"The RSR complex works as a clamp loader, loading RHR onto DNA. RSR prefers DNA substrates posessing 5' recessed ends.";"";""
2811;BRCA1-cABL complex;;Human;P00519,P38398;25,672;MI:0006- anti bait coimmunoprecipitation;12024016;10.01.05.01,32.01.09,70.10;"BRCA1 controls c-Abl activity. Interaction occurs between th PXXP motif in the C-terminus of BRCA1 and the SH3 domain of c-Abl. ";"BRCA1 is involved in breast cancer.";""
2812;RPAP1-RPB2-RPB3 complex;;Human;P30876,P19387,Q9BWH6;5431,5432,26015;MI:0004- affinity chromatography technologies;15282305;11.02.03.01,70.10;"";"";""
2813;BRCA1-SMAD3 complex;;Human;P38398,P84022;672,4088;MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down;15735739;10.01.05.01,10.03,11.02.03.04,30.05.01.18.01,70.10;"Interaction is mediated by the MH1 domain of Smad3 and the C-terminal part of BRCA1. ";"BRCA1 is involved in breast cancer.";""
2814;BRCA1-HDAC1-HDAC2 complex;;Human;P38398,Q13547,Q92769;672,3065,3066;MI:0007- anti tag coimmunoprecipitation;10220405;10.01.05.01,14.07.04,70.10;"BRCA1 interacts with components of the histone deacetylase complex, and therefore may explain the involvement of BRCA1 in multiple processes such as transcription, DNA repair, and recombination. BRCA1 associates with HDAC1 and HDAC2 via the BRCT domain.";"BRCA1 is involved in breast cancer.";""
2815;BRCA1-BARD1-BACH1-DNA damage complex II;;Human;O14867,Q99728,P38398,P49959,O60934,Q92878,Q99708,Q92547;571,580,672,4361,4683,10111,5932,11073;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;16391231;10.01.03,10.01.05.01,10.03.01.03,32.01.09,70.10;"This complex occurs after exposure to UV irradiation. ";"BRCA1 is involved in breast cancer.";""
2816;ITGAV-ITGB3 complex;;Human;P06756,P05106;3685,3690;MI:0019- coimmunoprecipitation;8798654;16.01,34.05.01,34.07,40.01.03.01;"Alpha(v)beta3 can differentially activate cell migration and intracellular signaling pathways in a ligand-specific manner (PMID:10835423).";"";""
2817;BRCA1-BARD1-BACH1-DNA damage complex I;;Human;O14867,Q99728,P38398,P40692,P52701,Q92547;571,580,672,4292,2956,11073;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;16391231;10.01.03,10.01.05.01,10.03.01.03,32.01.09,70.10;"This complex occurs after exposure to UV irradiation. BRCA1-BARD1-BACH1 complex is required for post-damage interaction with TOPBP1. ";"BRCA1 is involved in breast cancer.";""
2818;BRCA1-BARD1-BRCA2-DNA damage complex III;;Human;Q99728,P38398,P51587;580,672,675;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;16391231;10.01.03,10.01.05.01,10.03.01.03,32.01.09,70.10;"This complex occurs after exposure to UV irradiation. ";"BRCA1 is involved in breast cancer.";""
2819;BRCA1-CtIP-CtBP complex;;Human;P38398,Q13363,Q99708;672,1487,5932;MI:0006- anti bait coimmunoprecipitation;10196224;10.01.05.01,11.02.03.04,32.01.09,70.10;"BRCA1 binds to CtBP through CtIP. Binding of BRCA1 to CtIP/CtBP is critical in mediating transcriptional regulation of p21 in response to DNA damage. ";"BRCA1 is involved in breast cancer.";""
2820;BRCA1-VCP complex;;Human;P38398,P55072;672,7415;MI:0019- coimmunoprecipitation;10855792;10.01.05.01,70.10;"VCP participates in the DNA damage-repair function as an ATP transporter, possibly facilitating the transcription-coupled repair. ";"BRCA1 is involved in breast cancer.";""
2821;hSIR2-p53 complex;;Human;Q96EB6,P04637;23411,7157;MI:0006- anti bait coimmunoprecipitation;11672523;11.02.03.04,14.07.04,32.01.09,70.10;"The authors analyzed that hSir2 directly binds the human p53 protein in vivo and specifically deacetylates the K382 residue of p53.";"";""
2822;BRCA1-BARD1-UbcH5c complex;;Human;Q99728,P38398,P61077;580,672,7323;MI:0077- nuclear magnetic resonance;12732733;14.07.05,32.01.09,70.10;"UbcH5c binds to BRCA1 RING domain and not to the BARD1 RING. ";"BRCA1 is involved in breast cancer.";""
2823;BRCA1-BARD1-UbcH7c complex;;Human;Q99728,P38398,P68036;580,672,7332;MI:0077- nuclear magnetic resonance;12732733;14.07.05,32.01.09,70.10;"UbcH7c binds to BRCA1 RING domain and not to the BARD1 RING. ";"BRCA1 is involved in breast cancer.";""
2824;BRCA1-RAD51 complex;;Human;P38398,Q06609;672,5888;MI:0006- anti bait coimmunoprecipitation;9008167;10.01.05.01,10.01.05.03,10.03.01.03,70.10;"BRCA1 and RAD51 mainly colocalize in S phase cells. ";"BRCA1 is involved in breast cancer.";""
2825;BRCA1-RNA polymerase II complex;;Human;P38398,P18074,P19447,Q00403,P29083,P29084,P35269,P13984,P32780,Q13888,Q13889,Q92759,Q13503,P24928,P30876,P19387,O15514,P19388,P61218,P62487,P52434,P36954,P52435,P53803,P62875,P20226;672,2068,2071,2959,2960,2961,2962,2963,2965,2966,2967,2968,9412,5430,5431,5432,5433,5434,5435,5436,5437,5438,5439,5440,5441,6908;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;9159119;11.02.03.01,16.03.01,70.10;"The Brca1 tumor supressor protein is associated with the transcription process.";"BRCA1 is involved in breast cancer.";""
2826;ITGB3-ITGAV-VTN complex; integrin complex;Human;P06756,P05106,P04004;3685,3690,7448;MI:0004- affinity chromatography technologies;10835423;18.02,34.05.01;"In beta(3)-LNCaP cells, alpha(v)beta(3) mediates cell migration and PI 3-kinase/AKT pathway activation on vitronectin, whereas adhesion to osteopontin does not support alpha(v)beta(3)-mediated cell migration and PI 3-kinase/AKT pathway activation.";"";""
2829;RSmad complex;;Human;Q8NFD5,Q92793,Q9Y6Q9,Q15796,P84022,Q13485,P51532,Q92922,Q8TAQ2,Q9UPN9;57492,1387,8202,4087,4088,4089,6597,6599,6601,51592;MI:0004- affinity chromatography technologies;16751102;11.02.03.04,30.05.01.18.01,70.10;"Affinity purification of proteins that selectively bind to activated RSmads.";"";""
2830;TIF1gamma-SMAD2-SMAD3 complex;;Human;Q15796,P84022,Q9UPN9;4087,4088,51592;MI:0006- anti bait coimmunoprecipitation;16751102;11.02.03.04,30.05.01.18.01,41.05.18,70.10;"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.";"";""
2831;TIF1gamma-Smad2-Smad3 complex;;Mouse;Q62432,Q8BUN5,Q99PP7;17126,17127,94093;MI:0006- anti bait coimmunoprecipitation;16751102;11.02.03.04,30.05.01.18.01,41.05.18,70.10;"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.";"";""
2832;Smad4-Smad2-Smad3 complex;;Mouse;Q62432,Q8BUN5,P97471;17126,17127,17128;MI:0006- anti bait coimmunoprecipitation;16751102;11.02.03.04,30.05.01.18.01,70.10;"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.";"";""
2833;SRm160-SRm300 complex;;Human;Q8IYB3,Q9UQ35;10250,23524;MI:0019- coimmunoprecipitation;9531537;11.04.03.01,16.03.03,70.10.06;"The authors demonstrate that although SRm160/300 can promote splicing in the absence of U1 snRNP, under "normal" splicing reaction conditions containing endogenous levels of SR family proteins, SRm160/300 associates with pre-mRNA by a U1 snRNP-dependent pathway and its binding to pre-mRNA is further stabilized by U2 snRNP. SRm160/300 also associates preferentially with a subset of specific SR proteins comigrating with SRp40 and SRp75. The results indicate that SRm160/300 and SR family proteins have overlapping but nonreciprocal functions and that cooperative interactions between these factors is critical for the splicing of specific pre-mRNAs.";"";""
2834;SMAD4-SMAD2-SMAD3 complex;;Human;Q15796,P84022,Q13485;4087,4088,4089;MI:0006- anti bait coimmunoprecipitation;16751102;11.02.03.04,30.05.01.18.01,70.10;"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.";"";""
2835;Profilin 2 complex;;Mouse;P60710,Q7TMB8,P39053,P63017,P28660,Q9JJV2,P70336,O88935,Q64332;11461,20430,13429,15481,50884,18645,19878,20964,20965;MI:0069- mass spectrometry studies of complexes | MI:0004- affinity chromatography technologies;9463375;14.10,20.09.18.09.01,42.04.03,77.03.01.01.01;"";"";""
2836;Profilin 1 complex;;Mouse;P63260,Q68FD5,P63017,P62962,Q9CWF2,Q01853;11465,67300,15481,18643,73710,269523;MI:0069- mass spectrometry studies of complexes | MI:0004- affinity chromatography technologies;9463375;14.10,20.09.18.09.01,42.04.03;"";"";""
2837;Profilin 1 complex;;Human;P63261,Q00610,P11142,P07737,Q9BVA1,P55072;71,1213,3312,5216,347733,7415;MI:0019- coimmunoprecipitation;9463375;14.10,20.09.18.09.01,42.04.03;"In brain profilin I complex links the actin cytoskeleton and endocytic membrane flow, directing actin and clathrin assembly to distinct membrane domains.";"";""
2838;AR coactivator complex; p44-PRMT-ICLN complex;Human;P54105,O14744,Q9BQA1;1207,10419,79084;MI:0007- anti tag coimmunoprecipitation;12972618;11.02.03.04.01,14.07.09,16.03.01,30.01.11,47.03.21.04,70.10;"This complex enhances AR-driven transcription.  ";"Overexpression of WDR77 (p44) correlates with prostate tumorigenesis.";""
2839;ATRX-DAXX complex; ATRX chromatin-remodeling complex;Human;P46100,Q9UER7;546,1616;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;12953102;01.04,10.01.09.05,11.02.03.04,42.10.03,70.10;"ATRX and DAXX colocalize in promyelocytic leukemia nuclear bodies. The level of this complex is significantly decreased in an ATRX patient cell line.";"";"Two other subunits of the complex were found in the analysis, which have not been further characterized: DAP50 and DAP60."
2840;uKHC-KLC1-KLC2 kinesin complex;;Mouse;Q61768,O88447,O88448;16573,16593,16594;MI:0019- coimmunoprecipitation;9624122;20.09.14.01,34.05.02,70.04.05,77.03.01.01.01;"Immunoprecipitation done from brain lysate with uKHC antibodies brings down both kinesin light chains.";"";""
2842;DAXX-Axin-p53-HIPK2 complex;;Human;O15169,Q9UER7,Q9H2X6,P04637;8312,1616,28996,7157;MI:0006- anti bait coimmunoprecipitation;17210684;01.04,11.02.03.04,14.07.03,32.01.13,40.10.02,70.10;"Axin tethers DAXX to the tumor suppressor p53. UV induces colocalization of Axin, DAXX and HIPK2 in the nucleus.";"";""
2843;ATRX-DAXX complex; ATRX chromatin-remodeling complex;Human;P46100,Q9UER7;546,1616;MI:0007- anti tag coimmunoprecipitation;14990586;01.04,10.01.09.05,11.02.03.04,42.10.03,70.10;"DAXX regulates ATRX activity by altering its cellular localization. DAXX targets ATRX to the promyelocytic leukemia protein nuclear bodies.";"";""
2844;Axin-p53-HIPK2 complex;;Human;O15169,Q9H2X6,P04637;8312,28996,7157;MI:0006- anti bait coimmunoprecipitation;15526030;11.02.03.04,32.01.13,40.10.02,70.10;"Axin stimulates the transcriptional activity of p53 selectively toward some of the p53 target genes, and induces p53-dependent cell death through facilitating HIPK2 phosphorylation of Ser(46).";"";""
2845;BAX-BAK-IRE1alpha complex;;Mouse;O08734,Q07813,Q9EQY0;12018,12028,78943;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;16645094;32.01,40.10.02.03.02,70.07;"Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha.";"";""
2846;ITGAV-ITGB3-THBS1 complex; integrin complex;Human;P06756,P05106,P07996;3685,3690,7057;MI:0004- affinity chromatography technologies;2478219;16.01,73.03.07;"The alpha(v)beta3 integrin on platelets, endothelial cells, and smooth muscle cells functions as an Arg-Gly-Asp (RGD)-dependent receptor for thrombospondin.";"";""
2847;ING4 complex (ING4, MYST2, C1orf149, PHF15);;Human;Q9HAF1,Q9UNL4,O95251,Q9NQC1;64769,51147,11143,23338;MI:0069- mass spectrometry studies of complexes | MI:0004- affinity chromatography technologies;16387653;10.03.01,41.05.16;"ING4 associates with the HBO1 HAT required for normal progression through S phase and the majority of histone H4 acetylation in vivo. ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
2848;ING4 complex (ING4, MYST2, C1orf149, PHF16);;Human;Q9HAF1,Q9UNL4,O95251,Q92613;64769,51147,11143,9767;MI:0069- mass spectrometry studies of complexes | MI:0004- affinity chromatography technologies;16387653;10.03.01,41.05.16;"ING4 associates with the HBO1 HAT required for normal progression through S phase and the majority of histone H4 acetylation in vivo. ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
2849;ITGAV-ITGB3-NOV complex; integrin complex;Human;P06756,P05106,P48745;3685,3690,4856;MI:0004- affinity chromatography technologies;12902636;16.01,34.07,77.03.03.02;"The C-terminal domain of NOV is involved in the interaction with integrins.";"";""
2850;ITGA5-ITGB1-FN-1-NOV complex; integrin complex;Human;P02751,P08648,P05556,P48745;2335,3678,3688,4856;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;12902636;16.01,34.07,77.03.03.02;"The involvement of alpha5-beta1 in the process of endothelial cell adhesion to NOV was mediated by fibronectin.";"";""
2851;ING2 complex;;Human;P29374,Q9HCU9,Q5PSV4,Q13547,Q92769,Q9H160,Q09028,Q16576,Q9H0E3,O75446,Q96ST3,Q9H7L9;5926,25855,84312,3065,3066,3622,5928,5931,79595,8819,25942,64426;MI:0069- mass spectrometry studies of complexes | MI:0004- affinity chromatography technologies;16387653;10.01.09.05,10.03.01,14.07.04,40.10.02,41.05.16,42.10.03,70.10;"ING2 is in an HDAC complex similar to ING1. ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
2852;Brg1-based SWI/SNF chromatin remodeling complex;;Human;O96019,Q12824,Q92922,Q8TAQ2;86,6598,6599,6601;MI:0047- far western blotting;16387653;10.01.09.05,10.03.01,11.02.03.04;"";"";""
2853;ITGA5-ITGB1-CAL4A3 complex; integrin complex;Human;P39060,P08648,P05556;80781,3678,3688;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;12682293;18.02.01.02.05;"Endostatin binding to alpha5-beta1 integrin leads to the inhibition of focal adhesion kinase/c-Raf/MEK1/2/p38/ERK1 mitogen-activated protein kinase pathway, with no effect on phosphatidylinositol 3-kinase/Akt/mTOR/4E-BP1 and Cap-dependent translation.";"";""
2854;PI3-kinase p85-subunit beta- PI3-kinase p110 complex;;Bovine;P32871,P23726;282306,282308;MI:0006- anti bait coimmunoprecipitation;8313896;14.07.03,30.01.09.11;"The results demonstrate that p110 is able to form a stable, active PI 3-kinase complex with either of the p85 isoforms.";"";""
2856;NuA4/Tip60 HAT complex; ING3 subcomplex;Human;O96019,Q9H0E9,Q9NPF5,Q96L91,Q9H2F5,Q92993,Q9NXR8,Q9UBU8,Q9Y265,Q9Y4A5;86,10902,55929,57634,80314,10524,54556,10933,8607,8295;MI:0047- far western blotting;16387653;01.04,10.01.02,10.01.05.01,10.01.09.05,10.03.01,14.07.04,16.03.01,40.10.02,42.10.03,70.10;"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control. ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
2857;NuA4/Tip60 HAT complex;ING3 complex;Human;O96019,Q9H0E9,Q9HAF1,Q9NPF5,Q96L91,Q9H2F5,Q52LR7,Q92993,Q9NXR8,Q9UBU8,Q9Y265,Q9Y230,Q9Y4A5,O95619;86,10902,64769,55929,57634,80314,26122,10524,54556,10933,8607,10856,8295,8089;MI:0047- far western blotting;16387653;01.04,10.01.02,10.01.05.01,10.01.09.05,10.03.01,14.07.04,16.03.01,40.10.02,42.10.03,70.10;"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control. ING subunits are probably crucial for acetylation of chromatin substrates. ";"";"An actin component which was not exactly defined was also found."
2858;HBO1 complex;;Human;Q9HAF1,Q9UNL4,Q8WYH8,O95251,Q9NQC1,Q92613,Q6IE81;64769,51147,84289,11143,23338,9767,79960;MI:0047- far western blotting;16387653;10.03.01,40.10.02;"ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
2859;ING5 complex;;Human;O95696,P55201,Q9ULD4,Q9HAF1,Q8WYH8,O95251,Q92794,Q8WYB5,Q9NQC1,Q92613,Q6IE81;23774,7862,27154,64769,84289,11143,7994,23522,23338,9767,79960;MI:0047- far western blotting;16387653;10.03.01,40.10.02;"ING5 HAT complexes interact with the MCM helicase and are essential for DNA replication to occur during S phase. ING subunits are probably crucial for acetylation of chromatin substrates.";"";""
2860;DSIF complex (DRB sensitivity-inducing factor complex);;Human;P63272,O00267;6827,6829;MI:0007- anti tag coimmunoprecipitation;10075709;11.02.03.01.04,11.02.03.04.03,18.01.07,18.02.01,70.10;"DSIF represses transcription in the presence of DRB (inhibitor of transcription elongation), thereby inducing DRB sensitivity. SPT5 forms a stable complex with SPT4 and interacts directly with the largest subunit of RNA-Polymerase II.";"";""
2861;DSIF complex (DRB sensitivity-inducing factor complex);;Human;P63272,O00267;6827,6829;MI:0226- ion exchange chromatography;9450929;11.02.03.01.04,11.02.03.04.03,18.01.07,18.02.01,70.10;"DSIF represses transcription in the presence of DRB (inhibitor of transcription elongation), thereby inducing DRB sensitivity.";"";""
2863;Serine-palmitoyltransferase (SPT) complex;;Human;O15269,O15270,Q9NUV7;10558,9517,55304;MI:0019- coimmunoprecipitation;17023427;01.06.02.03,18.02.01.01;"";"";""
2866;TEAD2-YAP DNA-protein complex;;Mouse;P48301,P46938;21677,22601;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;11358867;11.02.03.04.01,16.03.01,70.10;"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency. The authors demonstrated that TEAD-dependent transcription in vivo required YAP protein with a functional TEAD binding domain as well as a TEAD protein with a functional DNA binding domain. Localization experiments showed TEAD proteins and YAP in different cellular compartments, TEAD mainly in the nucleus, YAP mainly in the cytoplasm. It was confirmed that most of the YAP protein existed as a complex with 14-3-3 and T11 (a unidentified protein). YAP can then be transported into and out of the nucleus, where it forms a transcriptionally active complex with TEAD.";"";""
2867;TEAD1-YAP DNA-protein complex;;Mouse;P30051,P46938;21676,22601;MI:0096- pull down;11358867;11.02.03.04.01,16.03.01,70.10;"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency.";"";""
2868;TEAD3-YAP DNA-protein complex;;Mouse;P70210,P46938;21678,22601;MI:0096- pull down;11358867;11.02.03.04.01,16.03.01,70.10;"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency.";"";""
2869;TEAD4-YAP DNA-protein complex;;Mouse;Q62296,P46938;21679,22601;MI:0096- pull down;11358867;11.02.03.04.01,16.03.01,70.10;"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency.";"";""
2870;TEAD2-multiprotein complex;;Mouse;Q8VBX6,P48301,P46938,P68254;17475,21677,22601,22630;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients;11358867;11.02.03.04;"In pull down experiments the authors analysed 12 proteins (T1-T12). T1/T2 correspond to YAP, T8 to MUPP1, T10 to 14-3-3, the remaining proteins couldn't be identified. Sedimentation experiments revealed that only about 5% of the complex preparation sedimented as TEAD2-multiprotein complex, about 20 % as monomeric TEAD2 protein, about 75% as TEAD2-YAP complex.";"";""
2872;ITGA2b-ITGB3-CD9-GP1b-CD47 complex; integrin complex;Human;Q08722,P21926,P08514,P05106,(P07359,P13224);961,928,3674,3690,(2811,2812);MI:0019- coimmunoprecipitation;10429193;18.01.07,34.07,70.02,73.03.07;"The isolation of this complex was independent of platelet activation, although a twofold increase in the quantity of CD9 complex was seen after platelet activation by alpha-thrombin in the presence of CaCl2 compared with that present in EDTA.";"";""
2873;P-TEFb-7SKRNA-HEXIM1 complex;;Human;O60563,P50750,O94992;904,1025,10614;MI:0071- molecular sieving | MI:0007- anti tag coimmunoprecipitation;12832472;01.04,11.02.03.01.04,11.02.03.04,18.01.01,18.02.01,70.10;"7SK RNA is required for MAQ1 to associate with P-TEFb complex. P-TEFb is inactive when bound to MAQ1 and 7SK. The 7SK RNA/MAQ1 system appears to be a new kind of CDK regulator that may contribute to a feedback loop modulating the activity of RNAP II.";"";""
2874;Slam-SAP-FynT complex;;Mouse;P39688,O88890,Q9QUM4;14360,20400,27218;MI:0019- coimmunoprecipitation;15539156;30.01.05.01.05,36.25.16.03.03,40.02.03.01,73.03.07.02.01.02;"The mutation of SAP (SAP R78A) did not affect the levels of SAP or the aptitude of SAP to associate with SLAM, a receptor involved in TH2 regulation. However, it eliminated the ability of SAP to recruit FynT and to promote SLAM-mediated protein tyrosine phosphorylation. The authors showed that the SLAM-SAP-FynT cascade is pivotal in TH2 cytokine production. ";"Sh2d1a is involved in X-linked lymphoproliferative syndrome.";""
2875;BRD4-P-TEFb complex;;Human;O60885,O60563,P50750;23476,904,1025;MI:0006- anti bait coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays | MI:0007- anti tag coimmunoprecipitation;16109376;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"BRD4 interacts with p-TEFb through its bromodomain. Recruitment of P-TEFb to a promoter was dependent on Brd4 and was enhanced by an increase in chromatin acetylation.";"";""
2876;SNARE complex (Snap25, Vamp3, Vamp2, Napa, Stx12/13);;Rat;P54921,P60881,O70319,P63045,P63025;140673,25012,65033,24803,29528;MI:0019- coimmunoprecipitation;9817754;20.09.07.27,20.09.16.09.05;"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ";"";"Entrez Gene says that stx12 is synonym to stx13."
2877;BRD4-P-TEFb complex;;Human;O60885,O60563,P50750;23476,904,1025;MI:0007- anti tag coimmunoprecipitation;16109377;01.04,11.02.03.01.04,11.02.03.04.01,18.01.01,18.02.01.01,70.10;"";"";""
2878;P-TEFb-7SKRNA-HEXIM1 complex;;Human;O60563,P50750,O94992;904,1025,10614;MI:0007- anti tag coimmunoprecipitation;16109377;01.04,11.02.03.01.04,11.02.03.04,18.01.01,18.02.01,70.10;"";"";""
2879;CD20-LCK-FYN-p75/80 complex;;Human;P06241,P06239,P11836;2534,3932,931;MI:0019- coimmunoprecipitation;7545683;30.01.05.01.05,73.03.07.02.01.02;"Lck accounted for most of the PTK activity in the CD20 complex.";"";"At the time of annotation, the identity of the additional member p75/80 of the protein complex was not known. "
2880;SCF subcomplex (WEE1, SKP2, BTRC);;Human;Q5W141,Q13309,P30291;8945,6502,7465;MI:0019- coimmunoprecipitation;15070733;10.03.01.01.11,14.07.03,14.07.05,14.13;"";"";""
2881;Ubiquitin E3 ligase (CUL1, RBX1, SKP1A);;Human;Q13616,P62877,P63208;8454,9978,6500;MI:0019- coimmunoprecipitation;15070733;10.03.01.01.11,14.07.03,14.07.05,14.13.01.01;"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. ";"";"Hemagglutinin (HA-)tagged F-box proteins were also found in this study (not further specified)."
2882;ITGA5-ITGB3-COL6A3 complex; integrin complex;Human;P12111,P08648,P05106;1293,3678,3690;MI:0004- affinity chromatography technologies;8387021;16.01,34.07,70.02,70.27.01;"";"";""
2883;Nephrin-cadherin complex (Nphs1, Ctnnd1, Cdh3, Cd2ap);;Rat;Q7TSS5,Q9JIV6,P30999,Q9R044;316258,116777,12388,64563;MI:0019- coimmunoprecipitation | MI:0096- pull down;15331416;34.07.01,42.06.04,70.06.04,75.03.09,77.03.07.01;"Experiments were done in rat glomeruli. The results verify that nephrin, adherens junction proteins, and CD2AP are components of a multiprotein complex in glomeruli as well as in MDCK-nephrin cells.";"";"Since Ctnnd1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
2884;Respiratory chain complex I (early intermediate NDUFAF1 assembly), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate;Human;P03886,P56556,Q16795,Q9Y375,O95139,O75489,O75251;4535,4700,4704,51103,4712,4722,374291;MI:0019- coimmunoprecipitation | MI:0276- blue native page;17557076;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. NDUFAF1 is a crucial component in the early assembly of complex I  but not of the mature holoenzyme. ";"Involved in mitochondrial diseases, cardioencephalomyopathy (gene CIA30), deficiency in fibroblasts.";""
2885;ITGAV-ITGB1-SPP1 complex; integrin complex;Human;P06756,P05556,P10451;3685,3688,6696;MI:0004- affinity chromatography technologies;7532190;16.01,34.07,70.02;"";"";""
2886;Respiratory chain complex I (incomplete intermediate ND1, ND2, ND3, CIA30 assembly), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate;Human;P03886,P03891,P03897,Q9Y375;4535,4536,4537,51103;MI:0019- coimmunoprecipitation;17557076;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2887;Shc-Egfr complex, EGF stimulated;;Rat;Q9QX70,Q9Z1I0;24329,85385;MI:0006- anti bait coimmunoprecipitation;7798267;30.01.05.05,30.05.01.12.01;"EGF treatment led to rapid tyrosine phosphorylation of Shc. The authors showed that EGFR-Shc complex formation was comparable to the kinetics of Shc phosphorylation.";"";""
2888;Grb2-Egfr complex, EGF stimulated;;Rat;Q9QX70,P62994;24329,81504;MI:0006- anti bait coimmunoprecipitation;7798267;30.01.05.05,30.05.01.12.01;"Tyrosine-phosphorylated EGFRs were co-precipitated by the anti-Grb2 antibody, but the magnitude of EGFR-Grb2 complex formation was much less than for EGFR-Shc complexes.";"";""
2889;Grb2-Shc complex, EGF stimulated;;Rat;P62994,Q9Z1I0;81504,85385;MI:0006- anti bait coimmunoprecipitation;7798267;30.01.05.05,30.05.01.12.01;"The authors showed that a substantially larger amount of Grb2 associated with Shc than with EGFR.";"";""
2890;Notch1-fraction 30 complex; CSL-NotchIC-Mastermind complex;Human;Q92585,P46531,Q06330;9794,4851,3516;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation;11997524;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"Complex formation is required for neoplastic transformation by Notch. MAML1 promotes association between NotchIC (intracellular domain of Notch) and RBPSUH (CSL). NotchIC binding to CSL displaces corepressors from CSL, leading to the binding of the transcriptional coactivator MAML1 to the complex. ";"Notch1 is involved in human cancer.";""
2891;Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN); presenilin complex;Human;Q96BI3,Q92542,P49768,Q9NZ42;51107,23385,5663,55851;MI:0040- electron microscopy;16636269;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,70.02,70.08;"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP is intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.  ";"Gamma-secretase is involved in Alzheimer's disease. In combination with Notch signaling pathway gamma secretase complex is also involved in lung cancer (PMID:17804716).";""
2892;BCR-ABL (p185 fusion protein)-GRB2 complex;;Human;Q13745,P62993;0,2885;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;8112292;30.01.05.01.05,30.01.05.05;"It was shown that Grb2 binds to the Tyr177 autophosphorylation site on Bcr-Abl.  ";"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).";""
2893;BCR-ABL (p210 fusion protein)-GRB2-SOS1 complex;;Human;A1Z199,P62993,Q07889;0,2885,6654;MI:0006- anti bait coimmunoprecipitation;8112292;30.01.05.01.05,30.01.05.05;"It was shown that Grb2 binds to the Tyr177 autophosphorylation site on Bcr-Abl.  ";"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).";""
2894;Itga1-Itgb1-Tgm2 complex; integrin complex;Rat;P18614,P49134,Q6P6R6;25118,24511,56083;MI:0019- coimmunoprecipitation;10684262;16.01,34.07;"";"";""
2895;SHC-GRB2 complex;;Human;P62993,P29353;2885,6464;MI:0006- anti bait coimmunoprecipitation;8112292;30.01.05;"Bcr-Abl proteins induce the formation of a complex between tyrosine phosphorylated Shc and Grb2. Co-precipitation analysed in R1-p185, R1-p210 and in Ph(+) leucemic cell lines. No co-precipitation seen in parental R1 cells. ";"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).";""
2896;ITGA2b-ITGB3-CD47-FAK complex;;Human;Q08722,P08514,P05106,Q05397;961,3674,3690,5747;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;9169439;16.01,34.07,73.03.07;"Activation of platelets with the agonist peptide 4N1K results in the association of FAK with the IAP-alpha-IIb-beta3 complex.";"";""
2897;RBPJ-NotchIC-Mastermind complex; Mam1-RBPJ-Notch1IC complex;Human;Q92585,P46531,Q06330;9794,4851,3516;MI:0006- anti bait coimmunoprecipitation;11390662;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"Complex formation is required for neoplastic transformation by Notch. MAML1 promotes association between NotchIC (intracellular domain of Notch) and RBPSUH (CSL). NotchIC binding to CSL displaces corepressors from CSL, leading to the binding of the transcriptional coactivator MAML1 to the complex. ";"Notch1 is involved in human cancer.";""
2898;Respiratory chain complex I (intermediate I/200kD and III/250kD), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex I and III;Human;Q16795,O75306,O75489;4704,4720,4722;MI:0019- coimmunoprecipitation | MI:0276- blue native page;12941961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. Intermediate I and III show the same components (therefore annotated as one entry only) but different molecular weights.";"";""
2899;PLC-gamma-1-Lab-Blnk complex, BCR stimulated;;Mouse;Q9QUN3,Q9JHL0,Q62077;17060,56743,18803;MI:0096- pull down;12514734;30.01.05,36.25.16.03.01,43.03.07.02.01.01,70.02,73.03.07.02.01.01;"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. The authors propose that BLNK and LAB in B cells are a functionally equivalent pair to SLP-76 and LAT in T cells.";"";""
2900;PLC-gamma-2-Lab-Blnk complex, BCR stimulated;;Mouse;Q9QUN3,Q9JHL0,Q8CIH5;17060,56743,234779;MI:0096- pull down;12514734;30.01.05,36.25.16.03.01,43.03.07.02.01.01,70.02,73.03.07.02.01.01;"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. The authors propose that BLNK and LAB in B cells are a functionally equivalent pair to SLP-76 and LAT in T cells.";"";""
2901;Respiratory chain complex I (intermediate IV/310kD), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex IV;Human;P03886,Q16795,O75306,O75489;4535,4704,4720,4722;MI:0019- coimmunoprecipitation | MI:0276- blue native page;12941961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2902;Grb2-Lab-Blnk complex, BCR stimulated;;Mouse;Q9QUN3,Q60631,Q9JHL0;17060,14784,56743;MI:0096- pull down;12514734;30.01.05,36.25.16.03.01,43.03.07.02.01.01,70.02,73.03.07.02.01.01;"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. LAB subsequently associates with Grb2, thereby recruiting Grb2 and Grb2-associated proteins to lipid rafts at the membrane. The authors propose that BLNK and LAB in B cells are a functionally equivalent pair to SLP-76 and LAT in T cells.";"";""
2903;Respiratory chain complex I (intermediate V/380kD and VI/480kD), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex V and VI;Human;P03886,O43678,Q16795,O75306,O75489;4535,4695,4704,4720,4722;MI:0019- coimmunoprecipitation | MI:0276- blue native page;12941961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. Intermediate V and VI show the same components (therefore annotated as one entry only) but different molecular weights.";"";""
2904;Respiratory chain complex I (intermediate VII/650kD), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex VII;Human;P03886,O43678,P56556,Q16795,O75306,O75489,O43181,O43920,O75251,P19404;4535,4695,4700,4704,4720,4722,4724,4725,374291,4729;MI:0019- coimmunoprecipitation | MI:0276- blue native page;12941961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2905;Respiratory chain complex I (holoenzyme), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) holoenzyme;Human;P03886,O43678,P56556,Q16795,O95139,O75306,O75489,O43181,O43920,O75251,P19404;4535,4695,4700,4704,4712,4720,4722,4724,4725,374291,4729;MI:0019- coimmunoprecipitation | MI:0276- blue native page;12941961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2906;Respiratory chain complex I (intermediate II/230kD), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex II;Human;O43181,O75251,P19404;4724,374291,4729;MI:0019- coimmunoprecipitation | MI:0276- blue native page;12941961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2907;RBP-Jkappa-Notch1 complex;;Human;P46531,Q06330;4851,3516;MI:0412- electrophoretic mobility supershift assay;12374742;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"";"";""
2908;RBP-Jkappa-SHARP complex;;Human;Q06330,Q96T58;3516,23013;MI:0412- electrophoretic mobility supershift assay;12374742;11.02.03.04.03,16.03.01,30.05.02.14,70.10;"";"";""
2909;PLC-gamma-2-Syk-LAT-FcR-gamma complex;;Human;P12314,O43561,P16885,P43405;2209,27040,5336,6850;MI:0096- pull down;10469124;30.01.09.11,30.05.01.12,36.25.16.09,73.03.07.03;"Analyses done with different GST-PLC-gamma-2 fusion proteins from resting and CRP (collagen-related peptide) stimulated platelets.";"";""
2910;PLC-gamma-2-Lyn-FcR-gamma complex;;Human;P12314,P07948,P16885;2209,4067,5336;MI:0019- coimmunoprecipitation;10469124;30.01.09.11,30.05.01.12,36.25.16.09,73.03.07.03;"Analyses done with different GST-PLC-gamma-2 fusion proteins from resting and CRP (collagen-related peptide) stimulated platelets. PLC-gamma-2 associates in vivo with Lyn and FcR gamma chain. The identity of Lyn was confirmed by sequential immunoprecipitation after the kinase assay.";"";""
2911;SMRT-SKIP-CBF1 complex;;Human;Q9Y618,Q06330,Q13573;9612,3516,22938;MI:0428- imaging techniques;11509665;11.02.03.04,14.04,30.05.02.14,70.10;"CIR seems to tether SKIP to SMRT.";"";""
2912;PLC-gamma-2-SLP-76 complex;;Human;Q13094,P16885;3937,5336;MI:0019- coimmunoprecipitation;10469124;30.01.09.11,30.05.01.12,36.25.16.09,73.03.07.03;"Analyses done with  GST-PLC-gamma-2SH2(C) fusion protein from resting and CRP (collagen-related peptide) stimulated platelets. PLC-gamma-2 associates directly with SLP-76 and LAT.";"";""
2913;PLC-gamma-2-LAT complex;;Human;O43561,P16885;27040,5336;MI:0019- coimmunoprecipitation;10469124;30.01.09.11,30.05.01.12,36.25.16.09,73.03.07.03;"Analyses done with  GST-PLC-gamma-2SH2(C) fusion protein from resting and CRP (collagen-related peptide) stimulated platelets. PLC-gamma-2 associates directly with SLP-76 and LAT.";"";""
2914;Respiratory chain complex I (beta subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) beta subunit;Human;P03905,P03915,O00483,O14561,O75438,O96000,Q9NX14,O95178,O43676,O95168,O43674,O95139,P17568,O95169,Q9Y6M9,O95298;4538,4540,4697,4706,4707,4716,54539,4708,4709,4710,4711,4712,4713,4714,4715,4718;MI:0276- blue native page | MI:0063- prediction;15317750;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme. ";"";"The authors assume an additional component (homolog to the bovine 10.6K protein)."
2915;CASK-Caskin1 complex;;Rat;Q62915,Q8VHK2;29647,140722;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;12040031;14.10,34.03.01,73.03.13,77.03.01.01.01;"Caskin1 and Mint1 bind to the same site on CASK and compete with each other for CASK binding.";"";""
2916;CASK-Caskin1-Velis complex;;Rat;Q62915,Q8VHK2,Q9Z250,Q9Z252,Q792I0;29647,140722,85327,60377,60442;MI:0096- pull down;12040031;14.10,34.03.01,73.03.13,77.03.01.01.01;"Caskin1 and Mint1 bind to the same site on CASK and compete with each other for CASK binding.";"";""
2917;Grb2-Sos complex, Fc receptor gamma-R1 stimulated;;Human;P62993,Q07889;2885,6654;MI:0019- coimmunoprecipitation;9716598;30.05.01.12,36.25.16;"In literature it has been shown that Grb2 binds to the guanine nucleotide exchange factor Sos, leading to activation of Ras.";"";""
2918;Ku antigen-YY1-alphaMyHC promoter complex; Ku70-Ku80-YY1-alphaMyHC promoter complex;Human;P13010,P12956,P25490;7520,2547,7528;MI:0412- electrophoretic mobility supershift assay | MI:0006- anti bait coimmunoprecipitation;15367688;11.02.03.04.03,16.03.01,70.10;"Ku complex binds to the human alphaMyHC promoter and represses alphaMyHC expression. Ku70 and YY1 protein levels are increased in patients with heart failure. ";"Human heart failure";""
2919;Respiratory chain complex I (gamma subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) gamma subunit;Human;P03886,P03891,P03897,P03901,P03923,O15239,O95299,O95167,P56556,P51970,Q16795,O43677,O43920;4535,4536,4537,4539,4541,4694,4705,4696,4700,4702,4704,4717,4725;MI:0276- blue native page | MI:0063- prediction;15317750;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2920;Respiratory chain complex I (lambda subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) lambda subunit;Human;Q86Y39,Q9UI09,Q9P0J0,O43678,Q16718,O95182,P28331,O75306,O75489,O43181,O75380,O75251,O00217,P49821,P19404,P56181;126328,55967,51079,4695,4698,4701,4719,4720,4722,4724,4726,374291,4728,4723,4729,4731;MI:0276- blue native page | MI:0063- prediction;15317750;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2921;SHARP-CtBP complex;;Human;Q13363,P56545,Q96T58;1487,1488,23013;MI:0007- anti tag coimmunoprecipitation;16287852;11.02.03.04.03,16.03.01,30.05.02.14,70.10;"CtBP augments SHARP-mediated repression.";"";""
2922;LAT-PLC-gamma-1-p85-GRB2-SOS signaling complex, C305 activated;;Human;P62993,O43561,P27986,P19174,Q07889;2885,27040,5295,5335,6654;MI:0019- coimmunoprecipitation;9489702;30.01.09.11,30.05.01.12,36.25.16.03.03;"The authors show that upon tyrosine phosphorylation, LAT binds Grb2, PLC-gamma1, the p85 subunit of PI3K, and other critical signaling molecules. They provide evidence that LAT plays an important role in linking the TCR to cellular activation.";"";""
2923;SHARP-CtBP1-CtIP complex;;Human;Q13363,Q99708,Q96T58;1487,5932,23013;MI:0007- anti tag coimmunoprecipitation;16287852;11.02.03.04.03,16.03.01,30.05.02.14,70.10;"CtIP and CtBP augment SHARP-mediated repression.";"";""
2924;Respiratory chain complex I (beta subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) beta subunit;Bovine;P03910,P03920,Q01321,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369,Q02827;3283886,0,327704,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660,338046;MI:0276- blue native page | MI:0063- prediction;15317750;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme. ";"";"The authors found an additional 10.6K component that could not be identified."
2925;Respiratory chain complex I (lambda subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) lambda subunit;Bovine;Q8HXG6,O97725,Q95KV7,Q02370,P23935,Q05752,P15690,P17694,P23709,Q02375,P23934,P42026,P42028,P25708,P04394,P25712;326346,281742,338084,327698,327714,338063,288380,327697,287327,327680,327691,338079,287027,287014,282290,327717;MI:0276- blue native page | MI:0063- prediction;15317750;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2926;Respiratory chain complex I (gamma subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) gamma subunit;Bovine;P03887,P03892,P03898,P03902,P03924,Q02377,P34942,Q02371,Q02366,P42029,P34943,Q02376,Q02379;0,0,3283884,3283885,3283888,327673,338060,338064,327670,327710,404188,282289,338057;MI:0276- blue native page | MI:0063- prediction;15317750;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2927;Respiratory chain complex I (incomplete gamma subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) gamma subunit fragment;Bovine;P03887,P03892,P03898,P03902,Q02376;0,0,3283884,3283885,282289;MI:0047- far western blotting | MI:0004- affinity chromatography technologies;10852722;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2928;Respiratory chain complex I (lambda subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) lambda subunit;Bovine;Q02370,P23935,Q02366,Q05752,P48305,P15690,P17694,P23709,Q02375,P23934,P42026,P42028,P25708,P04394,P25712;327698,327714,327670,338063,327706,288380,327697,287327,327680,327691,338079,287027,287014,282290,327717;MI:0047- far western blotting | MI:0004- affinity chromatography technologies;10852722;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2929;Respiratory chain complex I (beta subunit) mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) beta subunit;Bovine;P03910,P03920,P52505,Q02378,Q02373,Q02374,P48305,Q02380,Q02367,Q02368,Q02372,Q02369;3283886,0,327702,327690,327701,327713,327706,338061,327665,338065,282517,327660;MI:0047- far western blotting | MI:0004- affinity chromatography technologies;10852722;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.";"";""
2930;SHARP-CtIP-RBP-Jkappa complex;;Human;Q99708,Q06330,Q96T58;5932,3516,23013;MI:0007- anti tag coimmunoprecipitation;16287852;11.02.03.04.03,16.03.01,30.05.02.14,70.10;"The ternary complex is formed only when both SHARP and CtIP are expressed.";"";""
2931;SHARP-CtBP1-CtIP-RBP-Jkappa corepressor complex;;Human;Q13363,Q99708,Q06330,Q96T58;1487,5932,3516,23013;MI:0232- transcriptional complementation assay | MI:0004- affinity chromatography technologies;16287852;11.02.03.04.03,16.03.01,30.05.02.14,70.10;"The corepressor complex containing CtIP/CtBP probably facilitates RBP-Jkappa/SHARP-mediated repression of Notch target genes.";"";""
2932;PTF1-L complex (Ptf1a, Tcf12, Rbpjl);;Rat;Q64305,O08674,P51514;117034,19668,25720;MI:0412- electrophoretic mobility supershift assay;16354684;11.02.03.04,16.03.01,41.05.04,47.03.11.09,70.10,77.03.11.09;"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl. ";"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.";"Since Rbpjl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
2933;PTF1-L complex (Ptf1a, Tcf4, Rbpjl);;Rat;Q64305,O08674,Q62655;117034,19668,84382;MI:0412- electrophoretic mobility supershift assay;16354684;11.02.03.04,16.03.01,41.05.04,47.03.11.09,70.10,77.03.11.09;"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl. ";"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.";"Since Rbpjl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
2934;PTF1-L complex (Ptf1a, Tcf3, Rbpjl);;Rat;Q64305,O08674,P21677;117034,19668,171046;MI:0412- electrophoretic mobility supershift assay;16354684;11.02.03.04,16.03.01,41.05.04,47.03.11.09,70.10,77.03.11.09;"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl. ";"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.";"Since Rbpjl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
2935;PTF1 complex (Ptf1a, Tcf12, Rbpj);;Rat;Q64305,P31266,P51514;117034,19664,25720;MI:0402- chromatin immunoprecipitation assays;16354684;11.02.03.04,16.03.01,41.05.04,41.05.13,47.03.01.01.01.02,47.03.11.09,70.10,77.03.01.01.01.02,77.03.11.09;"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl. ";"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.";"Since Rbpj from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
2936;Ecsit complex (ECSIT, MT-CO2, GAPDH, TRAF6, NDUFAF1);;Human;Q9BQ95,P04406,P00403,Q9Y375,Q9Y4K3;51295,2597,4513,51103,7189;MI:0047- far western blotting;17344420;14.10,70.16;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.";"";""
2937;PTF1-bHLH complex;;Human;Q7RTS3,Q99081;256297,6938;MI:0412- electrophoretic mobility supershift assay;11562365;11.02.03.04,16.03.01,41.05.04,47.03.11.09,70.10,77.03.11.09;"PTF1, containing P48 and a form of HEB, can bind to and mediate the acinar activity of the A element of the ELA1 gene enhancer.";"";""
2938;Ecsit complex (ECSIT, NDUFS3, TOM20);;Human;Q9BQ95,O75489,Q15388;51295,4722,9804;MI:0019- coimmunoprecipitation;17344420;14.10,70.16;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.";"";""
2939;Ecsit complex (ECSIT, MT-CO2, NDUFA1, MT-ND1, TRAF6, NDUFAF1);;Human;Q9BQ95,P00403,P03886,O15239,Q9Y375,Q9Y4K3;51295,4513,4535,4694,51103,7189;MI:0019- coimmunoprecipitation;17344420;14.10,70.16;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.";"";""
2940;Acinar cell-specific C complex; PDX1-PBX1b-MEIS2 complex;Mouse;P97367,P41778,P52946;17536,18514,18609;MI:0412- electrophoretic mobility supershift assay;9710595;11.02.03.04.01,41.05.04,47.03.11.09,70.10,77.03.11.09;"The association with PBX and MEIS partners controls the nature of the transcriptional activity of the organ-specific PDX1 transcription factor in exocrine versus endocrine cells.";"";""
2941;Acinar cell-specific C complex; PDX1-PBX1b-MEIS2 complex;Mouse;P97367,P41778,P52946;17536,18514,18609;MI:0412- electrophoretic mobility supershift assay;11279116;11.02.03.04.01,41.05.04,47.03.11.09,70.10,77.03.11.09;"This complex cooperates with PTF1-bHLH complex to activate transcription in pancreatic acinar cells.";"";"MEIS2b isoform and possibly also MEIS2d isoform are present in the complex, but MEIS2a and MEIS2c isoforms are not."
2942;Ecsit complex (ECSIT, NDUFS3, NDUFAF1);;Human;Q9BQ95,Q9Y375,O75489;51295,51103,4722;MI:0047- far western blotting;17344420;14.10,70.16;"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.";"";""
2943;Respiratory chain complex I (incomplete NDUFAF1 assembly), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate;Human;P03886,Q9Y375;4535,51103;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16218961;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. NDUFAF1 is a crucial component in the early assembly/stability of complex I.";"";""
2944;Notch1-p56lck-PI3K complex;;Human;P06239,P46531,P27986;3932,4851,5295;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;14583609;11.02.03.04.01,30.05.02.14,40.10.02.01,43.03.07.02.01.02,73.03.07.02.01.02;"Anti-apoptotic function may result from elevated expression of anti-apoptotic genes like IAP-2, Bcl-xl or FLIP.";"";""
2945;RBP-Jkappa-RING1-KyoT2 complex;;Human;Q13642,Q06330,Q06587;2273,3516,6015;MI:0007- anti tag coimmunoprecipitation;14999091;11.02.03.04.03,16.03.01,18.01.07,18.02.09,30.05.02.14,70.10;"Overexpression of RING1 And KyoT2 inhibits transactivation of RBP-Jkappa by Notch.";"";""
2946;YY1-Notch1-RBP-Jkappa complex;;Human;P46531,Q06330,P25490;4851,3516,7528;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;12913000;11.02.03.04.01,16.03.01,30.05.02.14,70.10,73.03.01,75.03.03.01;"YY1 indirectly binds to CBF1-response element via association with the intracellular domain of Notch1 (N1IC). N1IC interacts directly with CBF1(RBP-Jkappa).";"";""
2947;YY1-Notch1 complex;;Human;P46531,P25490;4851,7528;MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;12913000;16.03.01,30.05.02.14,70.10,73.03.01,75.03.03.01;"Transcription factor Ying Yang 1 (YY1) is associated with exogenous N1IC in human K562 erythroleukemic cells. The ankyrin (ANK) domain of N1IC and zinc finger domains of YY1 are essential for the association of N1IC and YY1. ";"";""
2948;Respiratory chain complex I (incomplete intermediate), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate;Human;O95299,Q16795,O95169,P28331,O75306,O43181,O75380,O75251,P49821,P19404,P56181;4705,4704,4714,4719,4720,4724,4726,374291,4723,4729,4731;MI:0276- blue native page | MI:0047- far western blotting;17438127;02.11.05,02.13.03,14.10,20.01.15,70.16.05;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2949;MAML1-RBP-Jkappa-Notch1 complex;;Mammalia;Q6T264,Q01705,P31266;103806,18128,19664;MI:0428- imaging techniques | MI:0412- electrophoretic mobility supershift assay | MI:0007- anti tag coimmunoprecipitation;11101851;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"Binding of Notch 1 to MAML1 is enhanced in the presence of RBP-Jkappa. MAML1 stabilizes the association of Notch1 with RBP-Jkappa. ";"";""
2950;MAML1-RBP-Jkappa-Notch2 complex;;Mammalia;Q6T264,O35516,P31266;103806,18129,19664;MI:0007- anti tag coimmunoprecipitation;11101851;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"MAML1 binds to the ankyrin repeat domain of all four mammalian NOTCH receptors, forms a DNA-binding complex with intracellular domain of Notch and RBP-Jkappa, and amplifies NOTCH-induced transcription of HES1. ";"";""
2951;MAML1-RBP-Jkappa-Notch3 complex;;Mammalia;Q6T264,Q61982,P31266;103806,18131,19664;MI:0007- anti tag coimmunoprecipitation;11101851;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"MAML1 binds to the ankyrin repeat domain of all four mammalian NOTCH receptors, forms a DNA-binding complex with intracellular domain of Notch and RBP-Jkappa, and amplifies NOTCH-induced transcription of HES1.";"Notch3 is involved in lung cancer (PMID:17804716)";""
2952;MAML1-RBP-Jkappa-Notch4 complex;;Mammalia;Q6T264,P31695,P31266;103806,18132,19664;MI:0007- anti tag coimmunoprecipitation;11101851;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"MAML1 binds to the ankyrin repeat domain of all four mammalian NOTCH receptors, forms a DNA-binding complex with intracellular domain of Notch and RBP-Jkappa, and amplifies NOTCH-induced transcription of HES1.";"";""
2953;Respiratory chain complex I (nuclear encoded subunits), mitochondrial; NADH:ubiquinone oxidoreductase (EC 1.6.5.3) nuclear encoded subunits |;Bovine;Q02377,P34942,Q8HXG6,O97725,Q95KV7,Q02370,Q02371,Q01321,P23935,Q02366,Q05752,P42029,P34943,P52505,Q02378,Q02373,Q8HXG5,Q02374,Q02365,P48305,Q02380,Q02367,Q02368,Q02372,Q02369,Q02376,Q02827,P15690,P17694,P23709,Q02375,Q02379,P23934,P42026,P42028,P25708,P04394,P25712;327673,338060,326346,281742,338084,327698,338064,327704,327714,327670,338063,327710,404188,327702,327690,327701,404161,327713,338073,327706,338061,327665,338065,282517,327660,282289,338046,288380,327697,287327,327680,338057,327691,338079,287027,287014,282290,327717;MI:0047- far western blotting;12837546;02.11.05,02.13.03,20.01.15,70.16.05,75.03.12.03;"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.";"";""
2954;Smad1-Notch1-p300-Pcaf complex;;Mouse;Q09472,Q01705,Q92831,P70340;2033,18128,8850,17125;MI:0007- anti tag coimmunoprecipitation;14500836;11.02.03.04.01,14.07.04,16.03.01,18.01.07,18.02.09,30.05.02.14,70.10,75.03.17;"Interaction of SMAD1 and Notch1 was enhanced in the presence of p300 and PCAF.";"";"Since p300 and P/CAF from mouse were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
2955;LCK-SLP76-PLC-gamma-1-LAT complex, pervanadate-activated;;Human;O43561,P06239,Q13094,P19174;27040,3932,3937,5335;MI:0019- coimmunoprecipitation;16938345;30.05.01.12,36.25.16.03.03;"The authors show that in pervanadate-treated Jurkat cells, but not in J.CaM1.6 cells, three tyrosine-phosphorylated proteins with molecular weights about 59, 76 and 150 Kd, corresponding to Lck, SLP76, PLC-gamma-1 were co-precipitated with LAT.";"";""
2956;PLC-gamma-1-LAT-c-CBL complex, OKT3 stimulated;;Human;P22681,O43561,P19174;867,27040,5335;MI:0019- coimmunoprecipitation;16938345;30.05.01.12,36.25.16.03.03;"The authors show that  upon OKT3 stimulation, an extensive phosphorylation of LAT was seen in J2.LAT cells, but the phosphorylation of LAT F171F191 was barely detectable.";"";""
2957;LAT-GRB2 complex, Fyn-mLck(KA) or Syk kinase activated;;Human;P62993,O43561;2885,27040;MI:0019- coimmunoprecipitation;16938345;30.05.01.12,36.25.16.03.03;"The authors show that in the absence of a kinase, the association of LAT and Grb2 was not detected. Grb2 was co-precipitated with LAT, but not with LATF171F191, in the presence of Fyn, mLck(KA) or Syk kinases.";"";""
2958;SMAD1-CBP complex;;Human;Q92793,Q15797;1387,4086;MI:0007- anti tag coimmunoprecipitation;10673036;10.01.09.05,11.02.03.04.01,14.07.04,30.05.01.18.01,42.10.03,70.10;"SMAD1 stimulates transcription cooperatively with CBP.";"";""
2959;SMAD1-OAZ-HsN3 complex;;Mammalia;P54368,P28070,Q15797;4946,5692,4086;MI:0006- anti bait coimmunoprecipitation;12097147;11.02.03.04,14.13.01.01,16.03.01,30.05.01.18.01,70.10;"The interaction of the subunits is enhanced upon BMP type I receptor activation and occur prior to the incorporation of HsN3 into the mature 20S proteasome. Furthermore, BMPs trigger the translocation of the complex to the nucleus. ";"";""
2960;SLP-76-PLC-gamma-1-ITK complex, alpha-TCR stimulated;;Human;Q08881,Q13094,P19174;3702,3937,5335;MI:0019- coimmunoprecipitation;17148460;30.01.05.01.05,30.01.09.11;"The authors speculate that SLP-76 may activate PLC-gamma-1 by regulating the ITK-mediated phosphorylation of PLC-gamma-1 at Tyr783.";"";""
2961;SLP-76-PLC-gamma-1-VAV complex, alpha-TCR stimulated;;Human;Q13094,P19174,P15498;3937,5335,7409;MI:0019- coimmunoprecipitation;17148460;30.01.05,30.01.09.11;"SLP-76 inducibly associated with both Vav and catalytically active ITK, which efficiently phosphorylated a PLC-gamma1 fragment at Tyr783 in vitro.";"";""
2962;CRK-BCAR1-DOCK1 complex;;Human;P56945,P46108,Q14185;9564,1398,1793;MI:0019- coimmunoprecipitation;11146654;30.05.02.26,36.25.16.01.03,40.10.02.04,73.03.07.02.03;"Alpha(v)beta5 integrin binds to the apoptotic cell for recruitment of this complex to the membrane.";"";""
2963;ITK-SLP-76 complex, anti-TCR stimulated;;Human;Q08881,Q13094;3702,3937;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;17420479;30.01.05.01.05,30.01.09.11,36.25.16.03.03,73.03.07.02.01.02;"The authors show that catalytically active ITK is found primarily in complex with SLP-76. Further they demonstrate that a continued interaction with SLP-76 is required to maintain ITK in an active state.";"";""
2964;ITGA9-ITGB1-ADAM1 complex; integrin complex;Mammalia;Q60813,Q13797,P05556;280668,3680,3688;MI:0004- affinity chromatography technologies;11882657;16.01;"Alpha9-beta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.";"";""
2965;ITGA9-ITGB1-ADAM3 complex; integrin complex;Mammalia;Q810R6,Q13797,P05556;11497,3680,3688;MI:0004- affinity chromatography technologies;11882657;16.01;"Alpha9-beta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.";"";""
2966;NuMA-LGN-G-alpha-i-1 complex;;Human;P63096,P81274,Q14980;2770,29899,4926;MI:0096- pull down | MI:0007- anti tag coimmunoprecipitation;15537540;10.03.01,10.03.05.01;"The authors propose that the trimeric NuMA-LGN-G-alpha complex regulates the interaction of aster MTs with the cell cortex. They analyzed with a FRET biosensor that LGN behaves as a conformational switch: in its closed state, the N and C termini interact, but NuMA or G-alpha-i can disrupt this association, allowing LGN to interact simultaneously with both proteins, resulting in their cortical localization.";"";""
2967;Itga9-Itgb1-Thbs1 complex; integrin complex;Mouse;Q91YD5,P09055,P35441;104099,16412,21825;MI:0004- affinity chromatography technologies;17413041;45.03.11;"Alpha9-beta1 integrin expressed in microvascular endothelial cells interacts with thrombospondin-1, and this interaction is involved in modulation of angiogenesis.";"";""
2968;Axin-SMAD3 complex;;Human;O15169,P84022;8312,4088;MI:0007- anti tag coimmunoprecipitation;11438668;30.05.01.18.01,70.03;"Phosphorylation of SMAD3 by T(beta)R-I is faciliated in the presence of Axin. In the absence of ligand stimulation, Axin was colocalized with Smad3 in the cytoplasm in vivo. Upon receptor activation, Smad3 was strongly phosphorylated by TGF-beta type I receptor (TbetaR-I) in the presence of Axin, and dissociated from TbetaR-I and Axin.";"";""
2969;mTORC2 complex (mTOR/FRAP1, LST8, mAVO3/RICTOR);;Human;P42345,Q9BVC4,Q6R327;2475,64223,253260;MI:0019- coimmunoprecipitation;15467718;40.01,42.04.03;"mTORC1 and mTORC2 constitute a primordial signalling network conserved in eukaryotic evolution to control the fundamental process of cell growth.";"";""
2970;mTORC1 complex (mTOR/FRAP1, LST8, RAPTOR);;Human;P42345,Q9BVC4,Q8N122;2475,64223,57521;MI:0019- coimmunoprecipitation;15467718;40.01;"mTORC1 and mTORC2 constitute a primordial signalling network conserved in eukaryotic evolution to control the fundamental process of cell growth.";"";""
2971;ITGA9-ITGB1-VEGFC complex; integrin complex;Human;Q13797,P05556,P49767;3680,3688,7424;MI:0004- affinity chromatography technologies;15590642;34.05.01,34.07,43.03.07.02.01;"Alpha9-beta1 directly binds to VEGF-C and -D and contributes to lymphangiogenesis.";"";""
2972;ITGA9-ITGB1-VEGFA complex; integrin complex;Human;Q13797,P05556,P15692;3680,3688,7422;MI:0004- affinity chromatography technologies;15590642;41.05.16;"Alpha9-beta1 integrin binds the VEGF121 isoform of VEGF-A.";"";""
2973;Ccd1-Dvl2-Rac complex;;Mouse;Q80Y83,Q60838,P63001;330938,13543,19353;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that although Ccd1 could not interact directly with Rac, Ccd1, Dvl, and Rac could coexist in the same complex, indicating that Ccd1 inhibited Dvl-mediated JNK activation by forming a ternary complex of Ccd1·Dvl·Rac, in which Dvl·Rac is somehow blocked from further activating JNK. The authors do not exactly describe the Rac GTPase.";"";""
2974;Dvl2-Rac complex;;Mouse;Q60838,P63001;13543,19353;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that although Ccd1 could not interact directly with Rac, Ccd1, Dvl, and Rac could coexist in the same complex, indicating that Ccd1 inhibited Dvl-mediated JNK activation by forming a ternary complex of Ccd1·Dvl·Rac, in which Dvl·Rac is somehow blocked from further activating JNK. The authors do not exactly describe the Rac GTPase.";"";""
2975;SMAD3-E2F4/5-p107-DP1 complex;;Human;Q16254,Q15329,P28749,P84022,Q14186;1874,1875,5933,4088,7027;MI:0007- anti tag coimmunoprecipitation;12150994;30.05.01.18.01,70.03;"This complex preexists in the cytoplasm. In response to TGF-beta, this complex moves to the nucleus and associates with SMAD4.";"";""
2976;Ccd1-Dvl2 complex;;Mouse;Q80Y83,Q60838;330938,13543;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that Ccd1·Dvl complex formation is required for Ccd1 inhibition of Dvl-mediated JNK activation.";"";""
2977;Ccd1-Axin complex;;Mouse;O35625,Q80Y83;12005,330938;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that Ccd1 competes against MEKK1 binding to Axin in a dose-dependent manner, although MEKK1 and Ccd1 bind to separate regions far apart in Axin.";"";""
2978;Mekk1-Axin complex;;Mouse;O35625,P53349;12005,26401;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that Ccd1 competes against MEKK1 binding to Axin in a dose-dependent manner, although MEKK1 and Ccd1 bind to separate regions far apart in Axin.";"";""
2979;Axin-Mekk4 complex;;Mouse;O35625,O08648;12005,26407;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that Ccd1 did not disrupt the Axin-MEKK4 complex. They showed further that Ccd1 physically interacted with MEKK4 in their physiological concentrations and prevented MEKK4 from binding to Axin.";"";""
2980;Ccd1-Mekk4 complex;;Mouse;Q80Y83,O08648;330938,26407;MI:0007- anti tag coimmunoprecipitation;15262978;30.01.05.01.02;"The authors showed that Ccd1 did not disrupt the Axin-MEKK4 complex. They showed further that Ccd1 physically interacted with MEKK4 in their physiological concentrations and prevented MEKK4 from binding to Axin.";"";""
2981;Nkx3.2-SMAD1 complex;;Mammalia;P97503,P70340;12020,17125;MI:0007- anti tag coimmunoprecipitation;14612411;11.02.03.04,30.05.01.18,70.10;"Complex formation is enhanced in the presence of BMP signalling. ";"";""
2982;Nkx3.2-SMAD1-SMAD4 complex;;Mammalia;P97503,P70340,P97471;12020,17125,17128;MI:0007- anti tag coimmunoprecipitation;14612411;11.02.03.04,30.05.01.18,70.10;"Complex formation is enhanced in the presence of BMP signalling. ";"";""
2983;Nkx3.2-SMAD1-SMAD4-HDAC1 complex;;Mammalia;O09106,P97503,P70340,P97471;433759,12020,17125,17128;MI:0007- anti tag coimmunoprecipitation;14612411;10.01.09.05,11.02.03.04.03,14.07.04,30.05.01.18,42.10.03,70.10;"Complex formation is enhanced in the presence of BMP signalling. HDAC activity is necessary for transcriptional repression of Nkx3.2. ";"";""
2984;Nkx3.2-SMAD1-SMAD4-HDAC-Sin3A complex;;Mammalia;O09106,P97503,Q60972,Q60973,Q60520,P70340,P97471;433759,12020,19646,245688,20466,17125,17128;MI:0007- anti tag coimmunoprecipitation;14612411;10.01.09.05,11.02.03.04.03,14.07.04,30.05.01.18,42.10.03,70.10;"Complex formation is enhanced in the presence of BMP signalling. HDAC activity is necessary for transcriptional repression of Nkx3.2. ";"";""
5851;p65-p50 Nf(kappa)B complex, Il-1-beta induced;;Rat;Q63369,Q7TQN4;81736,309165;MI:0412- electrophoretic mobility supershift assay;16556731;11.02.03.04.01,16.03.01,30.01.05.01.04;"The results suggest that in INS-1E (beta cell line) cells the cytokines IL-1-beta or TNF-alpha induce a complex preferentially constituted by p65 homodimers, with a minor contribution by the p65/p50 heterodimer. The results further show that cytokine induced NF(kappa)B activation in insulin-producing cells is more intense and sustained than in fibroblasts.";"In pancreatic beta cells the cytokine induced p65-p50 Nf(kappa)B complex is involved in Diabetes mellitus, type I.";""
2985;mTOR-signaling complex; Nutrient-sensitive complex NSC;Human;P42345,Q8N122;2475,57521;MI:0019- coimmunoprecipitation;12150925;40.01;"mTOR/RAFT1/FRAP is the target  of the immunosuppressive drug  rapamycin and the central  component of a nutrient- and hormone-sensitive signaling pathway that regulates cell growth.";"";""
2986;FKBP12-FK506 complex;;Rat;Q62658,P42346;25639,56718;MI:0047- far western blotting;7822316;40.01;"";"";""
2987;FKBP12-FK506 complex;;Mouse;P26883,Q9JLN9;14225,56717;MI:0047- far western blotting | MI:0004- affinity chromatography technologies;7822316;40.01;"FRAP is the target of the FKBP12-rapamycin complex as well as a central component of a nutrient- and hormone-sensitive pathway that controls cellular growth (PMID:14560962).";"";""
2989;ITGA9-ITGB1-ADAM8 complex; integrin complex;Human;P78325,Q13797,P05556;101,3680,3688;MI:0004- affinity chromatography technologies;16995821;16.01,34.07,45.03.05.07,75.03.07;"";"";""
2990;mTOR-signaling complex (FRAP1/mTOR, GBL, RAPTOR);;Human;P42345,Q9BVC4,Q8N122;2475,64223,57521;MI:0019- coimmunoprecipitation;12718876;40.01;"";"";""
2991;mTOR-signaling complex (mTOR/FRAP1, RAPTOR);;Human;P42345,Q8N122;2475,57521;MI:0019- coimmunoprecipitation;12150926;40.01;"";"";""
2992;SMAD7-SMURF2 complex;;Human;O15105,Q9HAU4;4092,64750;MI:0007- anti tag coimmunoprecipitation;11163210;14.07.05,14.13.01.01,18.01.07,18.02.07,70.03,70.10;"SMURF is localized in the nucleus, but binding to SMAD7 induces export to the cytoplasm.";"";""
2993;Axin-GSK-3-beta complex;;Mammalia;O70239,P18266;79257,84027;MI:0007- anti tag coimmunoprecipitation;9482734;30.05.02.20;"Endogenous Axin forms a complex with and is phosphorylated by GSK-3b.";"";""
2994;Axin-GSK-3-alpha complex;;Mammalia;O70239,P18265;79257,50686;MI:0007- anti tag coimmunoprecipitation;9482734;30.05.02.20;"Endogenous Axin forms a complex with and is phosphorylated by GSK-3a.";"";""
2995;Axin-beta-catenin complex;;Mammalia;O70239,Q9WU82;79257,84353;MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;9482734;30.05.02.20;"Residues 298-506 of rAxin are sufficient and necessary to form a complex with b-catenin.";"";""
2996;SMAD7-SMURF1 complex;;Mammalia;O15105,Q9HCE7;4092,57154;MI:0007- anti tag coimmunoprecipitation;11278251;14.07.05,14.13.01.01,18.01.07,18.02.07,70.03,70.10;"SMAD7 associates with SMURF1 in the nucleus and is exported to the cytoplasm. ";"";""
2997;SMAD7-SMURF1-TGF-beta receptor complex;;Mammalia;O15105,Q9HCE7,P36897,P37173;4092,57154,7046,7048;MI:0007- anti tag coimmunoprecipitation;11278251;14.07.05,14.13.01.01,30.05.01.18.01,70.03;"SMAD7 enhances the interaction between SMURF1 and the TGF-beta receptor complex. ";"";""
2998;Axin-PP2A A-PP2A C-GSK3-beta-beta-catenin complex;;Human;O15169,P35222,P49841,Q15172;8312,1499,2932,5525;MI:0007- anti tag coimmunoprecipitation;11818547;30.05.02.20;"The incubation of the lysates with casein kinase I isoform epsilon decreases the association of PP2A C and A with the beta-catenin degradation complex.";"";"The authors describe as additional component of the complex "protein phosphatase PP2A C", that couldn't be identified. "
2999;Smad2 homotrimer complex;;Mammalia;Q62432;17126;MI:0007- anti tag coimmunoprecipitation | MI:0030- crosslink | MI:0071- molecular sieving;9670020;11.02.03.04.01,30.05.01.18.01;"Smad2 exists as monomer and forms homotrimers after phosphorylation by TGF-beta I receptor. ";"";""
3000;Smad2-Smad3 complex;;Mammalia;Q62432,Q8BUN5;17126,17127;MI:0007- anti tag coimmunoprecipitation;9670020;11.02.03.04.01,30.05.01.18.01;"";"";""
3001;Smad2-Smad4 heteromer complex;;Mammalia;Q62432,P97471;17126,17128;MI:0071- molecular sieving;9670020;11.02.03.04.01,30.05.01.18.01;"Complexes with two molecules of Smad4 and only one molecule of Smad2 also exist. ";"";""
3002;Smad3-Smad4 complex;;Mammalia;Q8BUN5,P97471;17127,17128;MI:0412- electrophoretic mobility supershift assay;9670020;11.02.03.04.01,16.03.01,30.05.01.18.01,70.10;"";"";""
3003;Smad3 homotrimer complex;;Mammalia;Q8BUN5;17127;MI:0412- electrophoretic mobility supershift assay;9670020;11.02.03.04.01,16.03.01,30.05.01.18.01;"In the absence of Smad4, Smad3 can form homomers. ";"";""
3004;APC-Axin-1-beta-catenin complex; 23S APC-containing complex;Human;P25054,O15169,P35222;324,8312,1499;MI:0029- cosedimentation through density gradients;16188939;30.05.02.20;"";"";""
3005;TGF-beta-receptor type I homodimer complex;;Rat;P80204;29591;MI:0029- cosedimentation through density gradients;9472030;16.01,30.05.01.18.01,70.07;"T-beta-RI can bind TGF-beta only in the presence of T-beta RII.";"";""
3006;TGF-beta-receptor type II homodimer complex;;Mammalia;Q62312;21813;MI:0029- cosedimentation through density gradients;9472030;16.01,30.05.01.18.01,70.07;"The type II receptor can bind TGF-beta in the absence of T-beta-RI. ";"";""
3007;TGF-beta-receptor type I homodimer complex;;Mammalia;Q64729;21812;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;9472030;16.01,30.05.01.18.01,70.07;"T-beta-RI can bind TGF-beta only in the presence of T-beta RII. ";"";""
3008;60S APC containing complex;;Human;P25054,P46940,(Q71U36,P68363,Q9BQE3),(P23258,Q9NRH3);324,8826,(7846,10376,84790),(7283,27175);MI:0029- cosedimentation through density gradients | MI:0226- ion exchange chromatography;17126424;42.04.03,70.03,75.03.09;"The authors propose that 60S APC is a discrete high molecular weight complex with a novel function in cytoskeletal regulation in epithelial cells apart from its well established role in targeting catenin destruction or its proposed role in microtubule plus end stabilization.";"";""
3009;TFIID complex; TFIID holoenzyme complex;Human;P21675,Q15544,Q16514,Q6P1X5,O00268,Q15542,P49848,Q16594,P20226;6872,6882,6883,6873,6874,6877,6878,6880,6908;MI:0019- coimmunoprecipitation;16895980;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"The subunit stoichiometry is predicted by Sanders et al. (PMID:12138208).";"";""
3010;TFIID subcomplex; TFIID (stable core) subcomplex;Human;Q16514,O00268,Q15542,P49848,Q16594;6883,6874,6877,6878,6880;MI:0019- coimmunoprecipitation;16895980;11.02.03.01.01,11.02.03.04,16.03.01,70.10;"The subunit stoichiometry is predicted by Sanders et al. (PMID:12138208).";"";""
3011;APC-IQGAP1-Rac1 complex;;Mammalia;P25054,P46940,P63000;324,8826,5879;MI:0006- anti bait coimmunoprecipitation;15572129;34.05.01,42.04,70.04,73.03.17;"When EGFP-APC-M1 (aa221-968) was immunoprecipitated from the cells expressing EGFP-APC-M1 and constitutively active Rac1 (Rac1V12), both Rac1V12 and IQGAP1 were coimmunoprecipitated. The authors showed that activated Rac1 and Cdc42 formed a tripartite complex with IQGAP1 and APC.";"";""
3012;APC-IQGAP1-Cdc42 complex;;Mammalia;P25054,P60953,P46940;324,998,8826;MI:0006- anti bait coimmunoprecipitation;15572129;34.05.01,42.04,70.04,73.03.17;"When EGFP-APC-M1 (aa221-968) was immunoprecipitated from the cells expressing EGFP-APC-M1 and constitutively active Cdc42 (Cdc42V12), both Cdc42V12 and IQGAP1 were coimmunoprecipitated. The authors showed that activated Rac1 and Cdc42 formed a tripartite complex with IQGAP1 and APC.";"";""
3013;EB1-APC-mDia1 complex;;Mouse;Q61315,O08808,Q61166;11789,13367,13589;MI:0006- anti bait coimmunoprecipitation;15311282;34.05.01,42.04.05,70.04.05,73.03.17,77.03.01.01.01;"The authors showed that EB1 and APC interacted with mDia directly, through domains that were distinct from those that interact with each other.";"";""
3014;Cohesin complex, incomplete (Stag3, Scp1, Ss181);;Mouse;Q7TQF3,O70576,Q62209;269397,50878,20957;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3015;p27-cyclinE-Cdk2 - Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, CKS1B, RBX1) complex;;Human;P24864,P24941,P46527,P61024,Q13616,P62877,P63208,Q13309;898,1017,1027,1163,8454,9978,6500,6502;MI:0007- anti tag coimmunoprecipitation;17409098;10.03.01.01,14.07.03,14.07.05,18.02;"p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes. Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression.";"Overexpression of p27 in certain cancer cells prevents DNA replication and tumor formation in nude mice, whereas the loss of p27 has been reported in many human cancers and predicts a poor prognosis in breast, prostate, colon, gastric, lung, and esophageal cancers. In several types of cancers, there is a strong correlation between the loss of p27 and induction of Skp2, a subunit of the SCFSkp2/Cks1 (Skp1, Cul1, Roc1, Skp2, Cks1 complex) ubiquitin E3 ligase that targets p27 for ubiquitination and degradation.";""
3016;Cohesin complex, incomplete (Stag3, Sycp3);;Mouse;O70576,P70281;50878,20962;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3017;Cohesin complex, incomplete (Stag3, Crest/Ss18I1);;Mouse;Q7TQF3,O70576;269397,50878;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3018;Cohesin complex, incomplete (Sycp2, Crest/Ss18I1);;Mouse;Q7TQF3,Q9CUU3;269397,320558;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3019;Cohesin complex, incomplete (Smc4, Crest/Ss18I1);;Mouse;Q8CG47,Q7TQF3;70099,269397;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3020;Cohesin complex, incomplete (Rec8, Crest/Ss18I1);;Mouse;Q8C5S7,Q7TQF3;56739,269397;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3021;Cohesin complex, incomplete (Smc1b, Crest/Ss18I1);;Mouse;Q920F6,Q7TQF3;140557,269397;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3022;Cohesin complex, incomplete (Sycp1, Crest/Ss18I1, Rec8);;Mouse;Q8C5S7,Q7TQF3,Q62209;56739,269397,20957;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3023;Cohesin complex, incomplete (Smc1b, Sycp1, Crest/Ss18I1);;Mouse;Q920F6,Q7TQF3,Q62209;140557,269397,20957;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3024;Cohesin complex, incomplete (Smc3, Sycp1, Crest/Ss18I1);;Mouse;Q9CW03,Q7TQF3,Q62209;13006,269397,20957;MI:0006- anti bait coimmunoprecipitation;15870106;10.03.01.01.11,10.03.04.05,16.03.01,42.10.03,70.10.03;"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.";"";""
3025;TGF-beta receptor II-TGF-beta3 complex;;Human;P10600,P37173;7043,7048;MI:0404- comigration in non denaturing gel electrophoresis;16289576;14.10,16.01,30.05.01.18.01,70.02;"TGF-beta 3 binds to TGF-beta receptor type II sequentially.";"";""
3026;TGF-beta receptor II-TGF-beta1 complex;;Human;P01137,P37173;7040,7048;MI:0404- comigration in non denaturing gel electrophoresis;16289576;14.10,16.01,30.05.01.18.01,70.02;"TGF-beta 1 binds to TGF-beta receptor type II sequentially.";"";""
3027;TGF-beta receptor II-TGF-beta receptor I-TGF-beta1 complex;;Human;P01137,P36897,P37173;7040,7046,7048;MI:0404- comigration in non denaturing gel electrophoresis;16289576;30.05.01.18.01,70.02;"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II.";"";""
3028;TGF-beta receptor II-TGF-beta receptor I-TGF-beta3 complex;;Human;P10600,P36897,P37173;7043,7046,7048;MI:0404- comigration in non denaturing gel electrophoresis;16289576;30.05.01.18.01,70.02;"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II.";"";""
3029;Drosha complex;;Mouse;Q501J6,Q61656,Q9EQM6,O35286,O35737,Q9D0E1,Q5HZJ0,Q921F2;67040,13207,94223,13204,59013,76936,14000,230908;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;17435748;11.04,16.03.03,70.10;"The authors purified the large complex of mouse Drosha and showed its function in pre-miRNA and 5.8S rRNA generation in vitro. They speculate that p68 and p72 DEAD-box RNA helicase subunits may function to specifically recognize and stably bind to certain structures of pri-miRNAs and 12S pre-rRNA, and to initiate cleavage at precise RNA sites by Drosha.";"";""
3030;TGF-beta receptor II-TGF-beta receptor I-TGF-beta1 complex;;Mammalia;P01137,P36897,P37173;7040,7046,7048;MI:0006- anti bait coimmunoprecipitation;8051105;30.05.01.18.01,70.02,77.03.09.01;"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II. ";"";"Since TGFBR1/2 and TGF-beta1 from mink were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
3031;TGF-beta receptor II-TGF-beta receptor I-TGF-beta1 complex;;Mammalia;P01137,P36897,P37173;7040,7046,7048;MI:0006- anti bait coimmunoprecipitation;8051105;30.05.01.18.01,70.02,77.03.09.01;"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II. ";"";""
3032;RNA-induced silencing complex, RISC;;Human;Q9UPY3,Q9UKV8,P08238,Q15633;23405,27161,3326,6895;MI:0007- anti tag coimmunoprecipitation;16357216;11.02.03.04.07,11.04,16.03.03,70.03;"";"";""
3033;PAC3-PAC4 complex;;Human;Q9BT73,Q5JS54;84262,389362;MI:0007- anti tag coimmunoprecipitation;17707236;14.10;"20S proteasome assembly is orchestrated by two distinct pairs of chaperones in mammals, the PAC1-PAC2 complex and the PAC3-PAC4 complex. ";"";"Since human PAC4 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3034;PAC1-PAC2 complex;;Human;O95456,Q969U7;8624,56984;MI:0007- anti tag coimmunoprecipitation;16251969;14.01,14.10;"20S proteasome assembly is orchestrated by two distinct pairs of chaperones in mammals, the PAC1-PAC2 complex and the PAC3-PAC4 complex.";"";""
3035;LAT2-ITGB1 complex;;Human;P05556,Q9UHI5;3688,23428;MI:0019- coimmunoprecipitation;11507094;34.07.01,75.03.09;"CD98-beta1 integrin association is required for focal adhesion kinase-dependent phosphoinositol 3-hydroxykinase activation and cellular transformation.";"";""
3036;Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, CKS1B, RBX1);;Human;P61024,Q13616,P62877,P63208,Q13309;1163,8454,9978,6500,6502;MI:0007- anti tag coimmunoprecipitation;17409098;10.03.01,14.07.05;"";"Overexpression of p27 in certain cancer cells prevents DNA replication and tumor formation in nude mice, whereas the loss of p27 has been reported in many human cancers and predicts a poor prognosis in breast, prostate, colon, gastric, lung, and esophageal cancers. In several types of cancers, there is a strong correlation between the loss of p27 and induction of Skp2, a subunit of the SCFSkp2/Cks1 (Skp1, Cul1, Roc1, Skp2, Cks1 complex) ubiquitin E3 ligase that targets p27 for ubiquitination and degradation.";""
3037;Ubiquitin E3 ligase (Fbxl20, Skp1, Cul1); SCRAPPER;Mouse;Q9WTX6,Q9CZV8,Q9WTX5;26965,72194,21402;MI:0007- anti tag coimmunoprecipitation | MI:0019- coimmunoprecipitation;17803915;14.07.05,34.03.01,70.02,75.03.17;"SCRAPPER-dependent ubiquitination of active zone protein RIM1 regulates synaptic vesicle release.";"";""
3038;SMAD2-SMAD4-FAST1 complex;;Human;O75593,Q15796,Q13485;8928,4087,4089;MI:0007- anti tag coimmunoprecipitation;9389648;11.02.03.04.01,16.03.01,30.05.01.18.01,70.10;"This complex is built only in the presence of TGF-beta signaling. ";"SMAD4 is involved in pancreatic carcinoma.";""
3039;SMAD2-FAST1 complex;;Human;O75593,Q15796;8928,4087;MI:0007- anti tag coimmunoprecipitation;9389648;16.03.01,30.05.01.18.01,70.10;"TGF-beta induces formation of the SMAD2-FAST1 complex.";"";""
3040;Multisynthetase complex; Aminoacyl tRNAsynthetase multienzyme complex;Human;P14868,O43324,P07814,P41252,Q13155,Q15046,Q9P2J5,P56192,P47897,P54136,Q12904;1615,9521,2058,3376,7965,3735,51520,4141,5859,5917,9255;MI:0028- cosedimentation in solution | MI:0226- ion exchange chromatography;16169847;12.10,70.03,70.10;"The characteristic "core" complex of aminoacyl tRNAsynthetase in higher eukaryotes is composed of nine synthetase activities. These are specific for arginine, aspartate, glutamate, glutamine, isoleucine, leucine, lysine, methionine, and proline. There are also three auxiliary proteins in the multisynthetase complex: p43, p38, and p18. These are involved in protein-protein interactions within the particle and with other protein synthesis factors.";"";""
3041;TGF-beta-receptor type II homodimer complex;;Human;P37173;7048;MI:0007- anti tag coimmunoprecipitation;7521335;16.01,30.05.01.18.01,70.02;"TGF-beta receptor type II forms a homomeric complex in the absence of the ligand TGF-beta.";"";""
3042;TGF-beta-receptor II-TGF-beta1 complex;;Human;P01137,P37173;7040,7048;MI:0007- anti tag coimmunoprecipitation;7521335;14.10,16.01,30.05.01.18.01,70.02;"";"";""
3043;BMP2-BRIA complex;;Human;P12643,P12644,P36894;650,652,657;MI:0071- molecular sieving;10881198;30.05.01.18.01,41.05.04,45.03.05.05,45.03.05.07;"";"";""
3044;SKI-NCOR1-SIN3A-HDAC1 complex;;Human;Q13547,O75376,Q96ST3,P12755;3065,9611,25942,6497;MI:0006- anti bait coimmunoprecipitation;10049357;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"The oncogenic form of Ski, v-Ski, which lacks the mSin3A binding domain, abrogates transcriptional repression.";"";""
3045;hs4 enhancer complex (faster migrating complex);;Human;P19838,P14859,P09086,Q04206,P25490;4790,5451,5452,5970,7528;MI:0412- electrophoretic mobility supershift assay;14707079;11.02.03.04,16.03.01,30.01.05.01.04,43.03.07.02.01.01,70.10,73.03.07.02.01.01;"This complex exists in healthy and malignant B-cell lines.";"";""
3046;hs4 enhancer complex (slow migrating complex);;Human;Q01201,P25490;5971,7528;MI:0412- electrophoretic mobility supershift assay | MI:0402- chromatin immunoprecipitation assays | MI:0006- anti bait coimmunoprecipitation;14707079;11.02.03.04,16.03.01,30.01.05.01.04,40.10.02.01,43.03.07.02.01.01,70.10,73.03.07.02.01.01;" ";"This complex was observed only in patients with diffuse large B cell lymphoma (DLBCA).";""
3047;Parvulin-associated pre-rRNP complex; Parvulin-associated preribosomal ribonucleoprotein complex;Mouse;P97452,Q9JJ80,P21127,P53569,Q8K363,Q9JIK5,Q9ESV0,Q921N6,Q61656,Q9D0R4,O43143,Q9D903,Q9D8N0,P35550,P11276,Q9DBE9,O95995,Q99LH1,Q99ME9,Q91VE6,Q9BWT6,Q9D0I8,Q7TPV4,P09405,Q922K7,Q6DFW4,Q9D6Z1,Q9EQ61,Q9Y237,Q9NW13,P27635,P62906,P47963,P19253,Q9CR57,Q9CZM2,P35980,P62717,P84099,O09167,P61255,P27659,Q9D8E6,P47962,P47911,P14148,P12970,P62918,P14869,P62908,P97351,P62702,P62754,P62242,P46781,P56183,Q9CYH6,O76021,Q9ULW0,P68363,P99024,Q9JJA4;12181,67239,984,12607,66942,56200,27225,228889,13207,52513,1665,69072,67160,14113,14268,56095,2622,230737,69237,67949,84057,69902,18432,17975,110109,55989,67134,64934,5303,55131,6134,4736,270106,22121,67115,66480,19899,76808,19921,19933,19941,27367,67891,19983,19988,19989,27176,26961,11837,27050,20091,20102,20104,20116,6203,18114,59014,26156,22974,10376,22154,57750;MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;11960984;12.01,70.10;"The authors propose that the hParvulin-associating rRNP complexes isolated represent those formed during postmitotic nucleolar reformation before rDNA transcription or premitotic nucleolar disassembly.";"";"Since human and mouse cell lines were investigated, not all of the identified protein are from mouse."
3048;mSin3A complex;;Human;Q13547,Q92769,Q09028,Q16576,Q96ST3;3065,3066,5928,5931,25942;MI:0006- anti bait coimmunoprecipitation;9150133;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"";"";"Three other subunits of the complex were found in the analysis, which have not been further characterized: p250, p180, p30."
3049;Mad-Max-mSin3a complex;;Mouse;P28574,P50538,Q60520;17187,17119,20466;MI:0006- anti bait coimmunoprecipitation;7889570;11.02.03.04.03,16.03.01,70.10;"Mad-Max represses transcription by tethering mSin3 to DNA as a corepressor.";"";""
3050;Mad-Max-mSin3B complex;;Mouse;P28574,P50538,Q62141;17187,17119,20467;MI:0412- electrophoretic mobility supershift assay;7889570;11.02.03.04.03,16.03.01,70.10;"Mad-Max represses transcription by tethering mSin3 to DNA as a corepressor.";"";""
3051;MAD-MAX complex;;Human;P61244,Q05195;4149,4084;MI:0006- anti bait coimmunoprecipitation;8224841;11.02.03.04.03,16.03.01,70.10;"Cell differentiation is accompanied by a change from MYC-MAX complexes (undifferentiated cells) to MAD-MAX complexes (differentiated cells). The ability of MAD to compete with MYC for binding to MAX and to repress MYC transcriptional activation suggests that MAD opposes the function of MYC.";"";""
3052;MYC-MAX complex;;Human;P61244,P01106;4149,4609;MI:0006- anti bait coimmunoprecipitation;8224841;11.02.03.04.01,16.03.01,70.10;"Cell differentiation is accompanied by a change from MYC-MAX complexes (undifferentiated cells) to MAD-MAX complexes (differentiated cells). The ability of MAD to compete with MYC for binding to MAX and to repress MYC transcriptional activation suggests that MAD opposes the function of MYC.";"";""
3053;mSin3A-HDAC1-HDAC2 complex;;Human;Q13547,Q92769,Q96ST3;3065,3066,25942;MI:0006- anti bait coimmunoprecipitation;9150134;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"";"";""
3054;MAD1-mSin3A-HDAC2 complex;;Human;Q92769,Q05195,Q96ST3;3066,4084,25942;MI:0007- anti tag coimmunoprecipitation;9150134;10.01.09.05,11.02.03.04,14.07.04,42.10.03,70.10;"MAD-MAX complex functions as transcriptional repressor by recruiting the mSin3A-HDAC complex.";"";""
3055;Nop56p-associated pre-rRNA complex; Nop56p-associated pre-ribosomal ribonucleoprotein complex;Human;P62736,P63267,Q8TDN6,Q9NR30,Q08211,Q99848,P68104,P13639,P22087,Q9BVP2,Q92522,P16402,Q99879,P09651,P52272,Q00839,Q9NZI8,Q12905,Q12906,Q9Y383,Q9NX58,Q9BQG0,P55209,P19338,P55769,Q9Y2X3,O00567,Q14978,P06748,Q13610,Q9NW13,P27635,P62906,P62913,P30050,P26373,P40429,P50914,P61313,P18621,Q07020,Q02543,P84098,P46778,P35268,P62829,P62750,P83731,P61254,P61353,P46776,P46779,P47914,P39023,P62888,P62899,P62910,P42766,P18077,Q9Y3U8,P83881,P61513,P62891,P36578,P46777,Q02878,P18124,P62424,P62917,P32969,P05388,P05386,P05387,P62280,P25398,P62277,P62263,P62841,P62244,P62249,P08708,P62269,P15880,P62266,P62847,P62273,P61247,P62753,P62081,P62241,P46781,O76021,Q6P3W7,P05141,P37108,Q96SB4,Q13428,P11387,Q71U36,Q9H4B7,P49411,Q01081,P26368,P67809;59,72,55299,9188,1660,10969,1915,1938,2091,26354,8971,3007,8342,3178,4670,3192,10642,3608,3609,51631,55646,10514,4673,4691,4809,51602,10528,9221,4869,11137,55131,6134,4736,6135,6136,6137,23521,9045,6138,6139,6141,6142,6143,6144,6146,9349,6147,6152,6154,6155,6157,6158,6159,6122,6156,6160,6161,11224,6165,25873,6173,6168,6170,6124,6125,6128,6129,6130,6132,6133,6175,6176,6181,6205,6206,6207,6208,6209,6210,6217,6218,6222,6187,6228,6229,6235,6189,6194,6201,6202,6203,26156,55681,292,6727,6732,6949,7150,7846,81027,7284,7307,11338,4904;MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;12777385;12.01,70.10;"Identification of pre-rRNA species within hNop56p-associated pre-ribosomal ribonucleoprotein complexes, coupled with the known functions of yeast orthologs of the probable trans-acting factors identified in man, demonstrated that hNop56p functions in the early to middle stages of 60 S subunit synthesis.";"";""
3056;Microprocessor complex; small Drosha complex (DGCR8-DROSHA);Human;Q8WYQ5,Q9NRR4;54487,29102;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving;15531877;11.04,16.03.03,70.10;"This complex is responsible for pre-miRNA processing. ";"DGCR8 is deleted in DiGeorge syndrome.";""
3057;ITGA10-ITGB1 complex;;Human;O75578,P05556;8515,3688;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;9685391;40.01.03;"";"";""
3058;ITGA11-ITGB1 complex;;Human;Q9UKX5,P05556;22801,3688;MI:0019- coimmunoprecipitation;10464311;16.01,34.05.01;"";"";""
3059;ITGA11-ITGB1-COL1A1 complex; integrin complex;Human;P02452,Q9UKX5,P05556;1277,22801,3688;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;10464311;30.05.02.26;"";"";""
3060;RNA polymerase II complex (RPB1, RAP74, CDK8, CYCC, SRB7, BAF190, BAF47), chromatin structure modifying;;Human;P24863,P49336,P35269,Q13503,P24928,Q12824,(P51531,P51532);892,1024,2962,9412,5430,6598,(6595,6597);MI:0047- far western blotting;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";""
3061;RNA polymerase II complex (CBP, PCAF, RPB1, BAF47, CYCC, CDK8), chromatin structure modifying;;Human;P24863,P49336,Q92793,Q92831,P24928,Q12824;892,1024,1387,8850,5430,6598;MI:0226- ion exchange chromatography;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";""
3062;RNA polymerase II complex, incomplete (CBP, RPBI, PCAF, BAF47), chromatin structure modifying;;Human;Q92793,Q92831,P24928,Q12824;1387,8850,5430,6598;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";""
3063;Brg1-associated complex II;;Human;O96019,O14497,O14744,P51532,Q12824,Q92922,Q8TAQ2;86,8289,10419,6597,6598,6599,6601;MI:0007- anti tag coimmunoprecipitation | MI:0029- cosedimentation through density gradients;11238380;10.01.09.05,11.02.03.04,16.03.01,42.10.03,70.10;"";"";"In a following paper (PMID:14559996) p66 has been identified as PRMT5."
3064;RNA polymerase II complex, chromatin structure modifying;;Human;P24863,P49336,Q14919,Q00403,P29083,P35269,P32780,Q13503,Q6UW60,P24928,Q12824,Q92922,Q8TAQ2,P20226,(P51531,P51532),(Q96GM5,Q92925,Q6STE5);892,1024,10589,2959,2960,2962,2965,9412,54760,5430,6598,6599,6601,6908,(6595,6597),(6602,6603,6604);MI:0004- affinity chromatography technologies;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";""
3065;RNA polymerase II complex, chromatin structure modifying;;Human;O96019,P24863,P49336,Q13503,Q12824,Q92922,Q8TAQ2,Q969G3,(Q96GM5,Q92925,Q6STE5);86,892,1024,9412,6598,6599,6601,6605,(6602,6603,6604);MI:0047- far western blotting;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";"At the time of annotation, the additional member (BAF110) of the protein  complex was not found in the UniProt database."
3066;RNA polymerase II complex, chromatin structure modifying;;Human;P24863,P49336,Q92793,P19447,Q00403,P35269,Q13889,Q13503,Q92831,P24928,P51531,P51532,Q12824;892,1024,1387,2071,2959,2962,2967,9412,8850,5430,6595,6597,6598;MI:0047- far western blotting | MI:0226- ion exchange chromatography;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";""
3067;RNA polymerase II complex, incomplete (CDK8 complex), chromatin structure modifying;;Human;P24863,P51946,P49336,P35269,Q13503,Q12824,Q92922,Q8TAQ2;892,902,1024,2962,9412,6598,6599,6601;MI:0047- far western blotting;9710619;10.01.09.05,11.02.03.01,16.03.01,70.10;"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex. ";"";""
3068;Fertilin complex (Adam1a, Adam2);;Mouse;Q60813,Q60718;280668,11495;MI:0019- coimmunoprecipitation;15194697;20.01.10;"ADAM1a/ADAM2 fertilin may be implicated in the selective transport of specific sperm proteins including ADAM3 from the endoplasmic reticulum of testicular germ cells onto the cell surface.";"";""
3069;Rich1-Amot-Par-3 polarity complex;;Rat;Q8VHG2,Q99N37,Q9Z340;27494,63994,81918;MI:0007- anti tag coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;16678097;18.01.03,18.02.01.01.01,30.01.05.05,40.01.03,41.05.19,42.06,70.06,75.03.09,77.03.01.01.01;"The results confirm that Rich1, Amot, and Par-3 associate in vivo.";"";"Since Amot from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
3070;CTF18-cohesion-RFC-POLH complex;;Human;Q8WVB6,Q8WV66,Q9BVC3,Q9Y253,P35250,P40938,P35249,P40937;63922,54921,79075,5429,5982,5983,5984,5985;MI:0004- affinity chromatography technologies | MI:0027- cosedimentation | MI:0019- coimmunoprecipitation;17545166;10.01.03,10.01.05,16.03.01,70.10;"The interaction of CTF18-cohesion-RFC complex  with  DNA-polymerase eta allows DNA replication fork to overcome interference by various template structures, including damaged DNA and DNA-protein complexes that maintain chromosome cohesion.";"";""
3071;CTLH complex; RANBPM-MKLN1-MAEA-RMND5A-ARMC8 complex;Human;Q8IUR7,Q7L5Y9,Q9UL63,Q96S59,Q9H871;25852,10296,4289,10048,64795;MI:0019- coimmunoprecipitation;17467196;10.03.04.05,34.05.01,42.04.05,70.03,70.10;"This complex might be involved in the regulation of microtubule dynamics, cell migration , nucleokinesis and chromosome segregation. CTHL complex contains alpha and beta splice variants of ARMC8.";"";""
3072;CCT complex (chaperonin containing TCP1 complex), testis specific; TRiC;Mouse;P11983,P80314,P80318,P80315,P80316,Q61390,P80313,P42932;21454,12461,12462,12464,12465,12467,12468,12469;MI:0029- cosedimentation through density gradients | MI:0091- chromatography technologies;9013858;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated. Sequence analysis of the TriC subunits was shown in PMID:9013858, PMID:2377466, PMID:7953530, and PMID:7890169.";"";""
3073;CCT complex (chaperonin containing TCP1 complex); TRiC;Bovine;Q32L40,Q3ZBH0,Q3T0K2,Q2T9X2,Q3T115,Q3MHL7,Q2NKZ1,Q3ZCI9;512043,505313,504735,613336,533784,521540,514355,281047;MI:0027- cosedimentation | MI:0091- chromatography technologies;12456645;14.01,16.01,16.19.03,70.03;"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated.";"";""
3074;CCT:PFD complex, testis specific;;Mammalia;Q32L40,Q3ZBH0,Q3T0K2,Q2T9X2,Q3T115,Q3T084,Q2NKZ1,Q3ZCI9,O60925,Q9UHV9,Q9NQP4,Q99471,O15212,P61758;512043,505313,504735,613336,533784,538090,514355,281047,5201,5202,5203,5204,10471,7411;MI:0040- electron microscopy | MI:0028- cosedimentation in solution | MI:0226- ion exchange chromatography;12456645;14.01,16.01;"The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Three-dimensional reconstruction of the CCT:PFD complex based on cryoelectron microscopy reveals that PFD binds to each of the two CCT rings. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated.";"";""
3075;UTX-MLL2/3 complex;;Human;Q9UBL3,Q86XN7,O14686,Q8NEZ4,Q86UW6,Q14686,Q6ZW49,Q15291,Q5H9R7,O15550,P61964,Q9Y2X9;9070,80209,8085,58508,55728,23054,22976,5929,55291,7403,11091,23528;MI:0007- anti tag coimmunoprecipitation;17761849;11.02.03.04.01,14.07.09,18.01.01,70.10;"Methylation of histone H3 lysine 27 (H3K27) is a post-translational modification highly correlated with genomic silencing. UTX, a member of JmjC-family proteins, is a di- and trimethyl H3K27 demethylase. Results uncover a concerted mechanism for transcriptional activation in which cycles of H3K4 methylation by MLL2/3 are linked with demethylation of H3K27 through UTX.";"";""
3076;Srf-Elk1 complex;;Rat;A4GTP4,Q9JM73;314436,20807;MI:0006- anti bait coimmunoprecipitation;15014501;11.02.03.04.03,45.03.12.02,75.03.12.02;"The authors demonstrate that myocardin and Elk-1 compete for interaction with a common docking site on SRF and that Elk-1 acts as a signal-responsive repressor of smooth muscle gene expression by displacing myocardin from SRF within the context of native chromatin.";"";"Since Srf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
3077;Srf-Myocd complex;;Rat;Q8R5I7,Q9JM73;246297,20807;MI:0006- anti bait coimmunoprecipitation;15014501;11.02.03.04.01,45.03.12.02,75.03.12.02;"The authors demonstrate that myocardin and Elk-1 compete for interaction with a common docking site on SRF and that Elk-1 acts as a signal-responsive repressor of smooth muscle gene expression by displacing myocardin from SRF within the context of native chromatin.";"";"Since Srf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
3078;DGCR8-NCL complex;;Human;Q8WYQ5,P19338;54487,4691;MI:0007- anti tag coimmunoprecipitation | MI:0416- fluorescence microscopy;17765891;11.04,16.03.03,70.10.07;"The authors demonstrated that certain RNA may be involved in the interaction between DGCR8 and Nucleolin, and removal of RNA induces dissociation of these two proteins. The results suggest that DGCR8 may be involved in maturation of miRNA at the nucleolus and nucleoplasm with Nucleolin.";"";""
3079;DGCR8-ILF3 complex;;Human;Q8WYQ5,Q12906;54487,3609;MI:0019- coimmunoprecipitation;17765891;11.04,16.03.03,70.10.07;"The authors found that ILF3 is associated with both DGCR8 and Exportin5 (XPO5), although DGCR8 is not associated with XPO5.";"";""
3080;ILF3-XPO5 complex;;Human;Q12906,Q9HAV4;3609,57510;MI:0019- coimmunoprecipitation;17765891;11.04,16.03.03,20.01.21,70.10;"The authors found that ILF3 is associated with both DGCR8 and Exportin5 (XPO5), although DGCR8 is not associated with XPO5.";"";""
3081;Microprocessor complex; small Drosha complex (DGCR8-DROSHA);Human;Q8WYQ5,Q9NRR4;54487,29102;MI:0007- anti tag coimmunoprecipitation | MI:0416- fluorescence microscopy;17765891;11.04,16.03.03,70.10.07;"The authors speculate that DGCR8 might play a significant role in the pri-miRNA recognition before interacting with DROSHA. In the coimmunoprecipitation assay DROSHA is seen as three isoforms (DROSHA-a, -b, -c). ";"DGCR8 is deleted in DiGeorge syndrome.";""
3082;DGCR8 multiprotein complex;;Human;Q92841,P17844,Q8WYQ5,Q08211,P35637,P31943,O43390,Q00839,P11021,Q12906,P19338;10521,1655,54487,1660,2521,3187,10236,3192,3309,3609,4691;MI:0007- anti tag coimmunoprecipitation | MI:0416- fluorescence microscopy;17765891;11.04,70.10;"";"";""
3083;Nucleic and chromatin Fanconi complex;;Human;O15360,Q00597,Q9HB96,Q9NPI8,O15287;2175,2176,2178,2188,2189;MI:0004- affinity chromatography technologies;15082718;32.01.09,70.10;"";"";""
3084;CCND1-CDK4 complex;;Human;P24385,P11802;595,1019;MI:0019- coimmunoprecipitation;9447971;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.";"";""
3085;CCND2-CDK4 complex;;Human;P30279,P11802;894,1019;MI:0019- coimmunoprecipitation;9447971;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.";"";""
3086;CCND3-CDK4 complex;;Human;P30281,P11802;896,1019;MI:0019- coimmunoprecipitation;9447971;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.";"";""
3087;CCND1-CDK6 complex;;Human;P24385,Q00534;595,1021;MI:0019- coimmunoprecipitation;9447971;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.";"";""
3088;CCND2-CDK6 complex;;Human;P30279,Q00534;894,1021;MI:0019- coimmunoprecipitation;9447971;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.";"";""
3089;CCND3-CDK6 complex;;Human;P30281,Q00534;896,1021;MI:0019- coimmunoprecipitation;9447971;10.03.01.01,14.07.03,18.01.01,18.02,70.10;"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.";"";""
3090;Kv4.2-Kchip4 channel complex;;Rat;Q63881,Q99MG9;65180,259243;MI:0019- coimmunoprecipitation;15356203;20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.";"";""
3091;Kv4.3-Kchip1 channel complex;;Rat;Q62897,Q8R426;65195,65023;MI:0019- coimmunoprecipitation;15356203;20.01.01.01,20.03.01.01,34.03.03,70.02,73.03.13,77.03.01.01.01;"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.";"";""
3092;APP-TOMM40 complex;;Human;P05067,O96008;351,10452;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16943564;14.04,70.16,77.03.01.01.01;"Mitochondrial accumulation of APP is associated with decreased cytochrome c oxidase activity and increased levels of H2O2 in mitochondria. Reduced mitochondrial cytochrome c oxidase activity and increased oxidative stress have been associated with the pathogenesis of AD.";"";""
3093;APP-TIMM23 complex;;Human;P05067,O14925;351,10431;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;16943564;14.04,70.16,77.03.01.01.01;"Mitochondrial accumulation of APP is associated with decreased cytochrome c oxidase activity and increased levels of H2O2 in mitochondria. Reduced mitochondrial cytochrome c oxidase activity and increased oxidative stress have been associated with the pathogenesis of AD.";"Alzheimer's disease";""
3094;Metaxin complex;;Mouse;P47802,O88441;17827,53375;MI:0018- two hybrid;10381257;20.01.10,41.03.03,70.16.01;"";"";""
3095;Itgav-Itgb3-Tgm2 complex; integrin complex;Rat;P43406,Q8R2H2,Q9WVJ6;16410,29302,56083;MI:0019- coimmunoprecipitation;10684262;16.01,34.07,70.02;"Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions. ";"";"Since Itgav from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3096;ITGA6-ITGB4-SHC1-GRB2 complex;;Human;P62993,P23229,P16144,P29353;2885,3655,3691,6464;MI:0019- coimmunoprecipitation | MI:0096- pull down;7556090;30.05.02,42.04,75.03.09,77.03.02.05;"The signal transduction by the alpha6beta4 integrin is mediated by an associated tyrosine kinase and that phosphorylation of distinct sites in the beta 4 tail mediates assembly of the hemidesmosomal cytoskeleton and recruitment of Shc/Grb2.";"";""
3097;TIMM17-TIMM23 complex;;Human;Q99595,O14925;10440,10431;MI:0019- coimmunoprecipitation;8893850;14.04,70.16.05;"The Tim17 proteins of distinct organisms were indistinguishable, indicating a high evolutionary conservation.";"";""
3098;TIM50a-SMN1 complex;;Human;Q16637,Q3ZCQ8;6606,92609;MI:0018- two hybrid;16008839;11.04.03.01,11.04.05,14.10,16.03.03,20.01.21,20.09.01,70.10;"There are two isoforms of TIM50: The nuclear isoform, TIM50a, participates in the release of snRNPs and SMN from the Cajal body (this complex), the mitochondrial isoform is an essential component of the TIM23 complex and regulates mitochondrial integrity and cell death. TIM50a is 103 aa longer (N-terminal) than TIM50.";"Spinal muscular atrophy";""
3099;TIM50a-coilin complex;;Human;P38432,Q3ZCQ8;8161,92609;MI:0018- two hybrid;16008839;11.04.03.01,11.04.05,14.10,16.03.03,20.01.21,20.09.01,70.10;"There are two isoforms of TIM50: The nuclear isoform, TIM50a, participates in the release of snRNPs and SMN from the Cajal body (this complex), the mitochondrial isoform is an essential component of the TIM23 complex and regulates mitochondrial integrity and cell death. TIM50a is 103 aa longer (N-terminal) than TIM50. ";"Spinal muscular atrophy";""
3100;Yy1-Ppargc1a complex;;Mouse;O70343,Q00899;19017,22632;MI:0096- pull down;18046414;11.02.03.04.01,70.10;"mTOR controls mitochondrial oxidative function to maintain energy homeostasis in response to nutrient and hormonal signals through a YY1-Ppargc1a transcriptional complex. Results indicate that the nutrient sensor mTOR (Frap1) controls mitochondrial respiration by regulating the transcriptional function of the Yy1-Ppargc1a complex by directly altering the physical interaction of the two subunits.  ";"Cells treated with amTOR inhibitor developed symptoms of diabetes.";""
3101;Yy1-Ppargc1a-Frap1 complex;;Mouse;Q9JLN9,O70343,Q00899;56717,19017,22632;MI:0096- pull down;18046414;11.02.03.04.01,70.10;"mTOR controls mitochondrial oxidative function to maintain energy homeostasis in response to nutrient and hormonal signals through a YY1-Ppargc1a transcriptional complex. Results indicate that the nutrient sensor mTOR (Frap1) controls mitochondrial respiration by regulating the transcriptional function of the Yy1-Ppargc1a complex by directly altering the physical interaction of the two subunits.  ";"Cells treated with amTOR inhibitor developed symptoms of diabetes.";""
3102;DHX9-ADAR-vigilin-DNA-PK-Ku antigen complex;;Human;P55265,Q08211,Q00341,P78527,P13010,P12956;103,1660,3069,5591,7520,2547;MI:0007- anti tag coimmunoprecipitation;15723802;10.01.09.05,10.03.04.05,11.06.03.01,16.03.03,42.10.03,70.10;"Vigilin and DDP1 bind specifically to Inosine-containing RNAs.";"";""
3103;ITGAV-ITGB3-SLC3A2 complex; integrin complex;Human;P06756,P05106,P08195;3685,3690,6520;MI:0019- coimmunoprecipitation;18032696;34.05,34.07,70.02;"";"";""
3104;ITGB1-NRP1 complex;;Human;P05556,O14786;3688,8829;MI:0019- coimmunoprecipitation;17726369;34.07,70.02;"NP-1 interacts with integrin beta1 to coordinate signaling events that promote cell adherence and invasiveness.";"";""
3105;Itga7-Itgb11-Lama2 complex; integrin complex;Rat;Q63258,P49134,Q60675;81008,24511,16773;MI:0019- coimmunoprecipitation;17598176;34.07,70.02;"Alpha7-beta1 integrin is a Schwann cell receptor for laminin-2 that provides transmembrane linkage between the Schwann cell basal lamina and cytoskeleton. ";"";"Since Lama2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3106;Itga7-Itgb11-Ptk2 complex; integrin complex;Rat;Q63258,P49134,O35346;81008,24511,25614;MI:0019- coimmunoprecipitation;17598176;30.05.02.26,70.02;"Alpha7-beta1 integrin, but not alpha6-beta1 integrin or dystroglycan, associates with the intracellular signaling protein focal adhesion kinase (FAK) in Schwann cells.";"";""
3110;ITGAV-P2RY2-GNA12 complex;;Human;Q5PPR5,P06756,P41231;2768,3685,5029;MI:0019- coimmunoprecipitation;17452627;34.05.01,70.02;"Alpha(v) integrin complexes provide the P2Y2R with access to G12, thereby allowing activation of this heterotrimeric G protein that controls actin cytoskeletal rearrangements required for chemotaxis.";"";""
3111;ITGA9-ITGB1-SPP1 complex; integrin complex;Human;Q13797,P05556,P10451;3680,3688,6696;MI:0004- affinity chromatography technologies;16005200;16.01,34.07;"";"";""
3112;ITGA5-ITGB1-SPP1 complex; integrin complex;Human;P08648,P05556,P10451;3678,3688,6696;MI:0004- affinity chromatography technologies;16005200;16.01,34.07;"";"";""
3113;MAML1-RBP-Jkappa-Notch1 complex;;Human;Q92585,P46531,Q06330;9794,4851,3516;MI:0114- x-ray crystallography;16530044;11.02.03.04.01,16.03.01,30.05.02.14,70.10;"RBPJ and the Ankyrin domain of Notch1 create a groove to bin MAML-1.";"";""
3114;Itgax-Itgb2-Icam4 complex;;Mouse;Q9ERM2,Q9QXH4,P11835;78369,16411,16414;MI:0004- affinity chromatography technologies;16985175;34.07,73.03.07.01;"Inhibition of erythrophagocytosis by anti-ICAM-4 and anti-integrin antibodies suggests a role for these interactions in removal of senescent red cells.";"";""
3115;ITGA2B-ITGB3-ICAM4 complex;;Human;Q14773,P08514,P05106;3386,3674,3690;MI:0004- affinity chromatography technologies;12477717;34.07,73.03.07.01;"";"";""
3116;Rab27a-melanophilin-myosin-Va complex;;Mouse;Q91V27,Q99104,Q9ERI2;171531,17918,11891;MI:0006- anti bait coimmunoprecipitation;12531900;43.03.03,70.02;"This complex is responsible for melanosome transport.  ";"Rab27a is involved in Griscelli syndrome.";""
3117;ITGB5-ITGAV-VTN complex; integrin complex;Human;P06756,P18084,P04004;3685,3693,7448;MI:0019- coimmunoprecipitation;1694173;16.01,34.07;"In purified form, alpha(v)-beta5 preferentially binds to vitronectin.";"";""
3118;SMN1-SIP1-SNRP complex;;Human;O14893,Q16637,P14678,P62314,P62316,P62318,P62304;8487,6606,6628,6632,6633,6634,6635;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0047- far western blotting;9323129;70.03,70.10;"SMN (Survival of Motor Neurons) and its associated protein SIP1 are in  a complex with spliceosomal snRNP proteins. The SMN/SIP1 complex is very stable. ";"Spinal muscular atrophy (SMA)";""
3119;Kif17-Lin10-Lin2-Lin7-NR2B complex;;Mouse;O70589,Q6PER2,Q01097,Q99PW8,(Q8JZS0,O88951);12361,234678,14812,16559,(108030,22342);MI:0019- coimmunoprecipitation;10846156;20.09.14,34.05.02,41.05.13,43.03.13,73.03.13;"The authors suggest that KIF17, a neuron-specific molecular motor with microtubule plus-end-directed motility interacts directly with a mLin-10 PDZ domain, resulting in the transport of NR2B in dendrites. They propose this motor-cargo complex as the sorting machinery for NR2B.";"";""
3120;OCT1-OBF1-DNA-TLE1 complex;;Human;Q16633,P14859,Q04724;5450,5451,7088;MI:0412- electrophoretic mobility supershift assay;16103132;11.02.03.04.03,16.03.01,70.10;"Transcription activation by Oct1 in conjunction with OBF1 can be prevented by TLE1. ";"";""
3121;OCT2-TLE4 complex;;Human;P09086,Q04727;5452,7091;MI:0096- pull down;16103132;11.02.03.04.03,16.03.01,70.10;"";"";""
3122;OCT1-OBF1-DNA complex;;Human;Q16633,P14859;5450,5451;MI:0412- electrophoretic mobility supershift assay;16103132;11.02.03.04.01,16.03.01,70.10;"";"";""
3123;TLE2 homodimer complex;;Human;Q04725;7089;MI:0096- pull down;9874198;11.02.03.04.03,16.01,18.01.07,18.02.09,70.10;"TLE2 dimer has no DNA-binding ability but can be recuited to specific DNA sites through interaction with DNA-binding proteins. ";"";""
3124;TLE1-TLE2 complex;;Human;Q04724,Q04725;7088,7089;MI:0096- pull down | MI:0018- two hybrid;9874198;11.02.03.04.03,16.01,18.01.07,18.02.09,70.10;"TLE1/2 heterodimer has no DNA-binding ability but can be recuited to specific DNA sites through interaction with DNA-binding proteins.  ";"";""
3125;TLE1 homodimer complex;;Human;Q04724;7088;MI:0018- two hybrid;9874198;11.02.03.04.03,16.01,18.01.07,18.02.09,70.10;"TLE1 dimer has no DNA-binding ability but can be recuited to specific DNA sites through interaction with DNA-binding proteins. ";"";""
3126;Tle2-Hes1 complex;;Rat;Q04666,Q496Z7;29577,299636;MI:0096- pull down | MI:0018- two hybrid;9874198;11.02.03.04.03,16.03.01,30.05.02.14,41.05.13,70.10;"";"";""
3127;TLE-Histone H3 complex;;Human;(P84243,P68431,Q71DI3),(Q04724,Q04725,Q04726,Q04727);(3020,8350,126961),(7088,7089,7090,7091);MI:0047- far western blotting;9334241;10.01.09.05,11.02.03.04.03,42.10.03,70.10;"The authors postulate that TLEs regulate gene expression by interacting with nucleosomes through associations with the N-terminus of H3 proteins.";"";""
3128;Gamma-secretase complex (APH1B, PSEN1, PSENEN, NCSTN);;Human;Q8WW43,Q92542,P49768,Q9NZ42;83464,23385,5663,55851;MI:0019- coimmunoprecipitation;15286082;14.07.11,18.01.05,18.02.09,30.01.05.03,30.05.02.14,70.02,70.08;"A multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin processes a number of type I transmembrane proteins such as the beta-amyloid precursor protein and the cell surface receptor notch-1. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.";"";""
3129;STAT6-p100-RHA complex;;Human;Q08211,Q7KZF4,P42226;1660,27044,6778;MI:0402- chromatin immunoprecipitation assays;16914450;10.01.02,10.01.09.05,11.02.03.04.01,16.03.01,70.10;"Experiments show that p100 protein mediates the assembly of the ternary complex  STAT6-p100-RHA. Chromatin immunoprecipitation studies show that RHA together with p100 enhance the binding of STAT6 on the human Ig-epsilon promoter after IL-4 stimulation. The authors propose that the ternary protein complex may facilitate the unwinding of the chromatin structure and accessibility of the promoter.";"";""
3130;Tle3-Aes complex; Grg3b-Grg5 complex;Mouse;P63002,Q08122;14797,21887;MI:0096- pull down | MI:0018- two hybrid;8955148;11.02.03.04.03,16.01,18.01.07,18.02.09,70.10;"Tle3/Grg3 and Aes/Grg5 heterodimer represses transcription by interacting with transcription factors, thereby regulating cell proliferation and differentiation.";"";""
3131;Hes1-TLE1 complex;;Mammalia;Q04666,Q04724;29577,7088;MI:0018- two hybrid | MI:0096- pull down;8687460;11.02.03.04.03,16.03.01,30.05.02.14,41.05.13,70.10;"";"";""
3132;OCT1-OBF1-DNA complex;;Human;Q16633,P14859;5450,5451;MI:0412- electrophoretic mobility supershift assay;12727885;11.02.03.04.01,16.03.01,70.10,73.03.07.02.01.01;"The OCT1 dimer is a better substrate for OBF1 than the monomer. OBF1 stabilizes the OCT1 dimer DNA complex by reducing its dissociation rate.";"";""
3133;Phosphatidylinositol 3-kinase (PIK3CA, PIK3R1);;Human;P42336,P27986;5290,5295;MI:0114- x-ray crystallography;18079394;16.19.03,30.05.01.12,70.02;"Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate phosphatidylinositol 4,5-bisphosphate at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3 ), which, in turn, initiates a vast array of signaling events. PI3Ks are heterodimers, composed of catalytic and regulatory subunits, that are activated by growth factor-receptor tyrosine kinases.";"In different types of cancer PIK3CA was found to be mutated. Defects in the phosphatidylinositol 3-kinase pathway contribute to type II diabetes.";""
3134;Na(+)/K(+) ATPase;;Pig;P05024,P05027,Q04646;397481,396898,11936;MI:0114- x-ray crystallography;18075585;16.19.03,20.01.01.01,20.03.22,70.02,77.03.07.01;"";"";"Since ATP1G1 from pig was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3135;TLE1 corepressor complex (MASH1 promoter-corepressor complex);;Human;P34932,P19338,Q15233,P06748,P09874,Q92878,Q04724,Q02880;3308,4691,4841,4869,142,10111,7088,7155;MI:0071- molecular sieving;15607978;11.02.03.04.03,16.01,16.03.01,18.01.07,18.02.09,43.03.13,70.10,77.03.01.01.01;"The TLE1 complex is required for HES1-mediated transcription repression. PARP1 is inactive in the TLE1 complex. After Ca(2+) induction, kinase CaMKII-delta activates PARP1 leading to dismissal of the TLE1 corepresspor complex from HES1.";"";""
3136;Hes1-Tle1 complex;;Rat;Q04666,Q62440;29577,21885;MI:0402- chromatin immunoprecipitation assays;15607978;11.02.03.04.03,16.03.01,30.05.02.14,41.05.13,70.10;"";"";"Since Tle1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3137;MASH1 promoter-coactivator complex;;Human;Q92793,Q14469,P62805,Q15233,P09874,Q92831,P24928,P12931,(P84243,P68431,Q71DI3);1387,3280,554313,4841,142,8850,5430,6714,(3020,8350,126961);MI:0402- chromatin immunoprecipitation assays;15607978;11.02.03.04.01,16.01,16.03.01,18.01.07,18.02.09,30.05.02.14,43.03.13,70.10,77.03.01.01.01;"Poly(ADP-ribosyl)ation activity of PARP1 is required for dismissal of the TLE1-corepressor complex.";"";""
3138;POSH-AKT2 complex;;Human;P31751,Q7Z6J0;208,57630;MI:0019- coimmunoprecipitation;14504284;30.01.05.01.02;"A POSH mutant unable to bind to Akt2 exhibits increased binding to MLK3. This increased binding of MLK3 to POSH is accompanied by increased activation of the JNK signaling pathway. The results suggest that Akt2 negatively regulates the POSH/JNK signaling complex by phosphorylating MLK3 and promoting the disassembly of the JNK signaling complex.";"";""
3139;CRLR-RAMP1-ARRB2 complex;;Mammalia;P29067,Q16602,O60894;25388,10203,10267;MI:0663- confocal microscopy;11535606;30.05.02.24,70.02;"When RAMP1 is expressed with CRLR, it is targeted to the cell surface as a 1:1 heterodimer. CGRP (calcitonin gene-related peptide) binding and receptor activation lead to the phosphorylation of CRLR and the internalization of the receptor as a stable complex. The authers describe that upon a 30-min CGRP treatment, the beta-arrestin2-YFP was redistributed into endocytic vesicles where it co-localized with myc-RAMP1 and HA-CRLR.";"";""
3140;CRLR-RAMP2 complex;;Human;Q16602,O60895;10203,10266;MI:0019- coimmunoprecipitation;11387328;30.05.02.24,70.02;"The results demonstrate that RAMP2 and RAMP3 and not only RAMP1 can promote the full maturation of CRLR, leading to its terminal glycosylation, and only the fully processed receptors were found to bind AM (adrenomedullin) and CGRP (calcitonin gene-related peptide).";"";""
3141;CRLR-RAMP3 complex;;Human;Q16602,O60896;10203,10268;MI:0019- coimmunoprecipitation;11387328;30.05.02.24,70.02;"The results demonstrate that RAMP2 and RAMP3 and not only RAMP1 can promote the full maturation of CRLR, leading to its terminal glycosylation, and only the fully processed receptors were found to bind AM (adrenomedullin) and CGRP (calcitonin gene-related peptide).";"";""
3142;CAMK2-delta-MASH1 promoter-coactivator complex;;Human;Q13557,Q92793,Q14469,Q15233,P09874,Q92831,P24928,P12931;817,1387,3280,4841,142,8850,5430,6714;MI:0402- chromatin immunoprecipitation assays;15607978;11.02.03.04.01,16.01,16.03.01,18.01.07,18.02.09,30.05.02.14,43.03.13,70.10,77.03.01.01.01;"HES1 is phosphorylated by CAMKII-delta during neural stem cell differentiation. This phosphorylation is linked to recruitment of coactivator complexes on the MASH1 promoter.";"";""
3143;Sos1-Abi1-Eps8 complex;;Mouse;Q8CBW3,Q08509,Q62245;11308,13860,20662;MI:0007- anti tag coimmunoprecipitation;11777939;30.01.05.05.01,30.05.01.12;"The authors describe the formation of either a Sos-1-Grb2 (S/G) or a Sos-1-E3b1-Eps8 (S/E/E8) complex, endowed with Ras- and Rac-specific GEF activities, respectively. Sos-1-Grb2 complex is disrupted upon RTKs (receptor tyrosine kinases) activation, whereas the S/E/E8 complex is not.";"";""
3144;Sos1-Grb2 complex;;Mammalia;P62993,Q07889;2885,6654;MI:0096- pull down;11777939;30.01.05.05.01,30.05.01.12;"The authors describe the formation of either a Sos-1-Grb2 (S/G) or a Sos-1-E3b1-Eps8 (S/E/E8) complex, endowed with Ras- and Rac-specific GEF activities, respectively. Sos-1-Grb2 complex is disrupted upon RTKs (receptor tyrosine kinases) activation, whereas the S/E/E8 complex is not. ";"";""
3145;Coatomer complex;;Rabbit;Q5XJY5,Q8CIE6,Q9JIF7,O55029,O89079,Q9QZE5,P61924;213827,12847,70349,50797,59042,54161,56447;MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;9482852;20.01.10,20.09.07.25,42.09,70.03,70.09,77.03.11.07;"The coatomer complex is described as a cytosolic complex of seven subunits alpha- to zeta-coat proteins (COPs), that with ADP ribosylation factor (ARF1) cover the surface of COPI-coated vesicles.";"";"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
3146;Coatomer-Arf1 complex;;Rabbit;Q5XJY5,P84078,Q8CIE6,Q9JIF7,O55029,O89079,Q9QZE5,P61924;213827,11840,12847,70349,50797,59042,54161,56447;MI:0029- cosedimentation through density gradients;9482852;20.01.10,20.09.07.25,42.09,70.08,70.09,77.03.11.07;"The authors describe that ARF1-GTP is tightly bound to the membrane and coatomer can be recruited from the cytosol to the Golgi membrane only after binding ARF1-GTP.";"";"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
3147;Beta/delta-coat protein subcomplex;;Rabbit;Q5XJY5,Q9JIF7;213827,70349;MI:0019- coimmunoprecipitation | MI:0226- ion exchange chromatography;9482852;20.01.10,20.09.07.25,42.09,70.03,70.09,77.03.11.07;"After dissociation/reassociation of the coatomer  with DMMA the authors isolated a subcomplex of coatomer consisting of beta- and delta-COPs that is able to bind to Golgi membranes in an ARF1- and GTP-dependent manner.";"";"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
3148;Arf1-beta/delta-coat protein subcomplex;;Rabbit;Q5XJY5,P84078,Q9JIF7;213827,11840,70349;MI:0029- cosedimentation through density gradients;9482852;20.01.10,20.09.07.25,42.09,70.08,70.09,77.03.11.07;"After dissociation/reassociation of the coatomer  with DMMA the authors isolated a subcomplex of coatomer consisting of beta- and delta-COPs that is able to bind to Golgi membranes in an ARF1- and GTP-dependent manner.";"";"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. "
3149;NK-3-Groucho-HIPK2-SIN3A-RbpA48-HDAC1 complex;;Human;Q13547,Q9H2X6,Q09028,Q96ST3,(Q99801,P78367),(Q04724,Q04725,Q04726,Q04727,Q9H808);3065,28996,5928,25942,(4824,579),(7088,7089,7090,7091,79816);MI:0007- anti tag coimmunoprecipitation | MI:0096- pull down;10559189;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"The authors postulate that the Nk-3 homeodomain protein recruits a corepressor complex containing Groucho protein, HIPK2 and a histone deacetylase complex to repress transcription.";"";""
3150;NK-3-Groucho complex;;Human;(Q99801,P78367),(Q04724,Q04725,Q04726,Q04727,Q9H808);(4824,579),(7088,7089,7090,7091,79816);MI:0096- pull down;10559189;11.02.03.04.03,70.10;"NK-3 homeodomain protein can associate wih the human Groucho homolog TLE in the absence of DNA. This interaction translocates Groucho proteins from the cytoplasm into the nucleus.";"";""
3151;Sulphiredoxin-peroxiredoxin complex;;Human;Q06830,Q9BYN0;5052,140809;MI:0114- x-ray crystallography;18172504;16.19.03,30,70.03;"Typical 2-Cys peroxiredoxins (Prxs) have an important role in regulating hydrogen peroxide-mediated cell signalling. In this process, Prxs can become inactivated through the hyperoxidation of an active site Cys residue to Cys sulphinic acid. The unique repair of this moiety by sulphiredoxin (Srx) restores peroxidase activity and terminates the signal.";"";""
3152;Notch1(N-TM)-Notch1(N-EC) heterodimer complex; Notch1(p120)-Notch1(p200) heterodimer;Mouse;Q01705;18128;MI:0006- anti bait coimmunoprecipitation;9653148;16.01,30.05.02.14;"";"";"The Furine-like protease proteolytically processes Notch 1 precursor (p300) into an intracellular part (N-TM or p120) bound to the plasma membrane and into an extracellular part, N-EC or p200. Both parts form a heterodimeric complex able to bind the ligand Delta."
3153;GNAQ-GEFT-RHOA complex;;Human;Q86VW2,P50148,P61586;115557,2776,387;MI:0114- x-ray crystallography;18096806;16.19.05;"It is assumed that the complex is involved in signal transduction.";"";""
3154;Notch2(N-TM)-Notch2(N-EC)-Delta complex;;Human;Q04721,(O00548,Q9NYJ7,Q9NR61);4853,(28514,10683,54567);MI:0006- anti bait coimmunoprecipitation;9244302;30.05.02.14,70.02;"In the trans-Golgi-network Notch2 is cleaved into the transmembrane Notch2(N-TM) subunit and into the extracellular Notch2(N-EC) subunit. Both subunits form a heterodimeric complex. The ligand Delta binds only to the heterodimeric form of Notch.";"";""
3155;Bipartite complex (TFC4, CTNNB1);;Human;P35222,Q9NQB0;1499,6934;MI:0019- coimmunoprecipitation;17072303;11.02.03.01,30.05.02.20;"As a consequence of engaging the canonical Wnt pathway, a beta-catenin-T-cell factor (TCF) transcriptional complex is generated, which has been postulated to trigger the epithelial-mesenchymal transition (EMT) that characterizes the tissue-invasive phenotype of breast cancer.";"";""
3156;CBF1-HDAC1-SMRT complex;;Human;Q13547,Q9Y618,Q06330;3065,9612,3516;MI:0007- anti tag coimmunoprecipitation;9694793;10.01.09.05,11.02.03.04.03,14.07.04,42.10.03,70.10;"CBF1 interacts with a corepressor complex containing HDAC1 and SMRT. Activation of Notch disrupts the formation of the repressor complex by competing of SMRT and Notch for binding with CBF1.";"";""
3157;Prolactin (PRL) - PRL receptor (PRLR) complex; H1:R2 complex;Human;P01236,P16471;5617,5618;MI:0019- coimmunoprecipitation;16556730;30.05.02;"H1:R2 complex consists of one prolactin molecule and one receptor dimer. The process of receptor dimerization can be either constitutive or ligand dependent.";"";""
3158;RIAM-Rap1-GTP-profilin complex;;Mammalia;Q7Z5R6,P07737,P62834;54518,5216,5906;MI:0007- anti tag coimmunoprecipitation;15469846;34.07,42.04.03;"The results indicate that RIAM can function as a link between Rap1-GTP and the actin regulator Profilin either by direct RIAM binding to Profilin or by RIAM recruitment of Ena/VASP-Profilin complexes. ";"";""
3159;RIAM-profilin complex;;Human;Q7Z5R6,P07737;54518,5216;MI:0018- two hybrid;15469846;34.07,42.04.03;"RIAM  interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics.";"";""
3160;RIAM-VASP complex;;Human;Q7Z5R6,P50552;54518,7408;MI:0096- pull down;15469846;34.07,42.04.03;"RIAM  interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics.";"";""
3161;PRL receptor (PRLR) dimer complex;;Human;P16471;5618;MI:0019- coimmunoprecipitation;16556730;30.05.02;"The process of receptor dimerization can be either constitutive or ligand dependent. The receptor dimer appears in variant (alternatively spliced) forms: As heterodimer long form (LF) - short form (SF) S1a/S1b and homodimers LF - LF, SF - SF.";"";""
3162;TF-FVIIa-FXa-TFPI complex;;Human;P00742,P13726,P08709,P10646;2159,2152,2155,7035;MI:0017- classical fluorescence spectroscopy;12787023;36.25.16.09;"The authors describe that the FXa-dependent inhibition of TF-FVIIa activity by TFPI leads to formation of the quaternary complex TF-FVIIa-FXa-TFPI.";"";""
3163;VILIP-1-AChR-alpha-4-AChR-beta-2 complex;;Rat;P09483,P12390,P62762;25590,54239,24877;MI:0006- anti bait coimmunoprecipitation;12202488;16.17.01,18.02.10,20.03.01.01,34.03.01,77.03.01.01.01;"The results suggest a rule for VILIP-1 as an AChR-associated protein that modulates the surface expression levels and functional properties of alpha 4-beta 2 AChRs in response to changes in the intracellular levels of calcium.";"";""
3164;HESX1-TLE1 complex;;Human;Q9UBX0,Q04724;8820,7088;MI:0004- affinity chromatography technologies | MI:0007- anti tag coimmunoprecipitation;11731482;11.02.03.04.03,16.03.01,30.05.02.14,47.03.21.03.05,70.10;"HESX1 recruits the TLE1 corepressor to specific promoters during pituitary organogenesis. This complex completely abolishes transcriptional activation mediated by PROP1.";"";""
3166;AXIN-APC-betaCatenin-GSK3B complex;;Human;P25054,O15169,P35222,P49841;324,8312,1499,2932;MI:0019- coimmunoprecipitation;10906131;14.07.03,30.05.02.20;"Interactions:  The RGS domains of Axin and conductin interact directly with the region containing the third to seventh 20-aa repeats of APC. The interaction of APC with Axin is important for regulating the stability of b-catenin. APC promotes a GSK-3b-dependent phosphorylation of b-catenin by interacting with Axin, thereby down-regulating b-catenin. APC binds not to GSK-3b but forms a complex with GSK-3b when Axin is present.";"";""
3167;NCOR-SIN3-HDAC-HESX1 complex;;Human;Q13547,Q92769,Q9UBX0,Q9Y618,Q96ST3,O75182;3065,3066,8820,9612,25942,23309;MI:0007- anti tag coimmunoprecipitation;11731482;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,30.05.02.14,42.10.03,47.03.21.03.05,70.10;"HESX1 recruits the N-Cor-SIN3-HDAC complex to specific promoters during pituitary organogenesis.";"";""
3168;DAXX-AXIN complex;;Human;O15169,Q9UER7;8312,1616;MI:0007- anti tag coimmunoprecipitation;17210684;18.01.07,18.02.01.01.05,18.02.09,32.01.13,40.10.02.03,77.03.01.01.01;"The Daxx-Axin complex formation is enhanced by UV-irradiation.  ";"";""
3169;Daxx-Axin complex;;Mouse;O35625,O35613;12005,13163;MI:0007- anti tag coimmunoprecipitation;17210684;18.01.07,18.02.01.01.05,18.02.09,40.10.02.03,77.03.01.01.01;"The Daxx-Axin complex formation is enhanced by UV-irradiation.";"";""
3170;Daxx-Axin-p53 complex;;Human;O15169,Q9UER7,P04637;8312,1616,7157;MI:0007- anti tag coimmunoprecipitation;17210684;11.02.03.04,32.01.13,40.10.02.03,70.10,77.03.01.01.01;"Axin enhances the interaction between DAXX and p53 in a dose-dependent manner. DAXX does not directly interact with p53, but through a bridge by Axin. DAXX-Axin-p53 complex promotes HIPK2 phosphorylation of p53 at Ser(46).  ";"";""
3171;GluR6a-GluR6b-KA2 complex;;Mouse;P39087,Q61626;14806,14809;MI:0019- coimmunoprecipitation;16102538;20.01.01.01,20.03.01.01,34.03.01,70.02;"The splice variants GluR6a and GluR6b which differ in their C-terminal domains can assemble in vivo within the same KAR complex, together with KA2.";"";""
3172;NUMB-TP53-MDM2 complex;;Human;Q00987,P49757,P04637;4193,8650,7157;MI:0019- coimmunoprecipitation;18172499;16.01,30.05.02.14,30.07;"NUMB enters in a tricomplex with p53 and the E3 ubiquitin ligase MDM2, thereby preventing ubiquitination and degradation of p53. This results in increased p53 protein levels and activity, and in regulation of p53-dependent phenotypes.";"In breast cancers, loss of NUMB expression causes increased activity of the receptor NOTCH. Thus, in these cancers, a single event-loss of NUMB expression determines activation of an oncogene (NOTCH) and attenuation of the p53 tumour suppressor pathway.";""
3173;CIN85 homotetramer complex;;Human;Q96B97;30011;MI:0031- protein cross-linking with a bifunctional reagent;11071869;30.05.01.12;"CIN85 interacted with itself via its coiledcoil region, regardless of EGF stimulation.";"";""
3174;CIN85-BLNK complex;;Human;Q8WV28,Q96B97;29760,30011;MI:0019- coimmunoprecipitation;11071869;30.05.01.12,70.03;"The authors suggest a novel mechanism in regulation of the B cell signaling events in which CIN85 plays a specific role by association with BLNK or c-Cbl.";"";""
3175;CIN85-c-CBL complex;;Human;P22681,Q96B97;867,30011;MI:0019- coimmunoprecipitation;11071869;30.05.01.12,70.03;"The authors suggest a novel mechanism in regulation of the B cell signaling events in which CIN85 plays a specific role by association with BLNK or c-Cbl.";"";""
3176;USP1-UAF1 complex;;Human;O94782,Q8TAF3;7398,57599;MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;18082604;14.07.05,32.01.09,70.10;"USP1-UAF1 is a ternary complex of two cleavage products of USP1 (produced after autocleavage of USP1) and UAF1 (= USP1 associated factor 1, official name: WDR48). The complex is necessary for deubiquitinating Ub-FANCD2, a key protein of the Fanconi anemia DNA repair pathway. ";"";""
3177;GNA14-p115RhoGEF complex;;Human;Q92888,O95837;9138,9630;MI:0114- x-ray crystallography | MI:0019- coimmunoprecipitation;15735747;40.01;"The G-protein alpha subunit a13 regulates cell growth and differentiation.";"";""
3178;Frs2-Shp2 complex, FGF stimulated;;Mouse;Q8C180,P35235;327826,19247;MI:0007- anti tag coimmunoprecipitation;9632781;30.05.01.12.03;"";"";""
3179;Grb2-Shp2 complex, FGF stimulated;;Mouse;Q60631,P35235;14784,19247;MI:0007- anti tag coimmunoprecipitation;9632781;30.05.01.12.03;"On the basis of further experiments the authors conclude that FGF stimulation leads to tyrosine phosphorylation of Shp2 and association with the Grb2-Sos complex.";"";""
3180;Shp2-Sos complex, FGF stimulated;;Mouse;P35235,Q62245;19247,20662;MI:0007- anti tag coimmunoprecipitation;9632781;30.05.01.12.03;"On the basis of further experiments the authors conclude that FGF stimulation leads to tyrosine phosphorylation of Shp2 and association with the Grb2-Sos complex.";"";""
3181;LMO4-CREB complex;;Human;P16220,P61968;1385,8543;MI:0007- anti tag coimmunoprecipitation;16899735;11.02.03.04.01,30.01.09.03,41.05.13,73.03.13;"Most probably homodimerization of LMO4 and interaction with CREB is necessary for full Ca(2+)-dependent transcription activation. This complex plays a key role in patterning thalamocortical connections during development. ";"";""
3182;FHL2 homodimer complex;;Human;Q14192;2274;MI:0018- two hybrid;11046156;11.02.03.04,18.01.07,18.02.09;"FHL2 protein forms homodimer complexes.";"";""
3183;PDGFRA-SHP-2 complex, PDGF stimulated;;Human;P16234,Q06124;5156,5781;MI:0019- coimmunoprecipitation;8943348;30.05.01.12;"The data demonstrate that SHP-2 does not need to be tyrosine phosphorylated in order to bind to the phosphorylated PDGFRA and are consistent with the idea that SHP-2 binds to the PDGFRA directly.";"";""
3184;FHL3 homodimer complex;;Human;Q13643;2275;MI:0018- two hybrid;11046156;11.02.03.04,18.01.07,18.02.09;"FHL3 protein forms homodimer complexes.";"";""
3185;ACT homodimer complex;;Human;Q5TD97;9457;MI:0018- two hybrid;11046156;11.02.03.04,18.01.07,18.02.09;"ACT protein forms homodimer complexes.";"";""
3186;GRB2-SHP-2 complex, PDGF stimulated;;Human;P62993,Q06124;2885,5781;MI:0019- coimmunoprecipitation;8943348;30.05.01.12;"In summary, the data demonstrate that activation of the PDGFRA leads to phosphorylation of SHP-2 at Y580, which appears to trigger the formation of a complex between Grb2 and SHP-2. In addition, SHP-2 binds the activated PDGFRA directly, whereas Grb2 binds indirectly, via SHP-2.";"";""
3187;FHL2-FHL3 complex;;Human;Q14192,Q13643;2274,2275;MI:0018- two hybrid;11046156;11.02.03.04,18.01.07,18.02.09;"";"";""
3188;FHL2-ACT complex;;Human;Q14192,Q5TD97;2274,9457;MI:0018- two hybrid;11046156;11.02.03.04,18.01.07,18.02.09;"";"";""
3189;FHL2-CREB complex;;Human;P16220,Q14192;1385,2274;MI:0007- anti tag coimmunoprecipitation;11046156;11.02.03.04.01,16.03.01,18.01.07,18.02.09;"FHL proteins differentially modulate CRE-dependent transcription in mammalian cells.";"";""
3190;FHL3-CREB complex;;Human;P16220,Q13643;1385,2275;MI:0007- anti tag coimmunoprecipitation;11046156;11.02.03.04.01,16.03.01,18.01.07,18.02.09;"FHL proteins differentially modulate CRE-dependent transcription in mammalian cells.";"";""
3191;ACT-CREB complex;;Human;P16220,Q5TD97;1385,9457;MI:0007- anti tag coimmunoprecipitation;11046156;11.02.03.04.01,16.03.01,18.01.07,18.02.09;"FHL proteins differentially modulate CRE-dependent transcription in mammalian cells.";"";""
3192;G protein complex (Hdac4, Gnb1, Gng2);;Mouse;P62874,P63213,Q6NZM9;14688,14702,208727;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;16221676;11.02.03.04.03,30.01.05.05;"The class II HDAC4 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.";"";""
3193;G protein complex (Hdac5, Gnb1, Gng2);;Mouse;P62874,P63213,Q9Z2V6;14688,14702,15184;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;16221676;11.02.03.04.03,30.01.05.05;"The class II HDAC5 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.";"";""
3194;G protein complex (HDAC5, GNB1, GNG2);;Bovine;P62871,P63212,Q2T9N9;281201,281203,504242;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;16221676;11.02.03.04.03,30.01.05.05;"The class II HDAC5 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.";"";""
3195;G protein complex (Btk, Gng2, Gnb1);;Mouse;P35991,P62874,P63213;12229,14688,14702;MI:0047- far western blotting;7972043;30.01.05.05,43.03.07.02.01;"";"Deficient expression or function of Bruton tyrosine kinase (Btk) causes human X chromosome-linked agammaglobulinemia (XLA) ormurine X chromosome-linked immunodeficiency (XID).";""
3196;FHL4/STX11-ACT complex;;Human;Q5TD97,O75558;9457,8676;MI:0018- two hybrid;11046156;11.02.03.04,18.01.07,18.02.09;"";"";""
3197;SMAD4-SNO-SKI complex;;Human;P12755,P12757,Q13485;6497,6498,4089;MI:0004- affinity chromatography technologies;10485843;11.02.03.04,16.03.01,30.05.01.18.01,70.10;"Ski and Sno associate predominantly with the MH2 domain of SMAD4.  ";"";""
3198;SMAD2-SKI complex;;Human;P12755,Q15796;6497,4087;MI:0007- anti tag coimmunoprecipitation;10485843;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"Smad proteins are the DNA-binding partners of Ski. Ski represses TGF(beta)-induced and SMAD-dependent transcriptional activation. ";"";""
3199;SMAD3-SKI complex;;Human;P12755,P84022;6497,4088;MI:0007- anti tag coimmunoprecipitation;10485843;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"Smad proteins are the DNA-binding partners of Ski. Ski represses TGF(beta)-induced and SMAD-dependent transcriptional activation.  ";"";""
3200;SMAD4-SKI complex;;Human;P12755,Q13485;6497,4089;MI:0004- affinity chromatography technologies;10485843;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"Smad proteins are the DNA-binding partners of Ski. Ski represses TGF(beta)-induced and SMAD-dependent transcriptional activation.   ";"";""
3201;Ship-Shc complex, IL-3 stimulated;;Mouse;Q9ES52,P98083;16331,20416;MI:0019- coimmunoprecipitation;10891441;30.05.01.05;"The authors describe that Shc-SHIP and Shc-Il3rb1 exist as separate complexes. They further propose that the interaction between Shc and the Il3rb1 subunit seems to be transient and of a lower affinity than the association of Shc with SHIP.";"";""
3202;Il3rb1-Shc-Ship complex, IL-3 stimulated;;Mouse;P26955,Q9ES52,P98083;12983,16331,20416;MI:0096- pull down;10891441;30.05.01.05;"";"";""
3203;Shc-Ship-Grb2 complex, IL-3 stimulated;;Mouse;Q60631,Q9ES52,P98083;14784,16331,20416;MI:0007- anti tag coimmunoprecipitation;10891441;30.05.01.05;"The authors conclude that although both Y239 and Y317 of Shc can associate with Grb2, the latter is the principal site for Grb2 binding in IL-3-stimulated IC2 cells. The data reported here indicate that Shc phosphorylation in IL-3-stimulated mast cells depends on binding of the PTB domain to the IL-3 receptor and that Shc pTyr sites subsequently bind SH2 proteins involved in different signaling pathways.";"";""
3204;SMAD2-SKI-NCOR complex;;Human;O75376,P12755,Q15796;9611,6497,4087;MI:0007- anti tag coimmunoprecipitation;10485843;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"Ski recruits the corepressor N-Cor to the SMAD proteins.  ";"";""
3205;SMAD3-SKI-NCOR complex;;Human;O75376,P12755,P84022;9611,6497,4088;MI:0007- anti tag coimmunoprecipitation;10485843;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"Ski recruits the corepressor N-Cor to the SMAD proteins.  ";"";""
3206;SMAD4-SKI-NCOR complex;;Human;O75376,P12755,Q13485;9611,6497,4089;MI:0007- anti tag coimmunoprecipitation;10485843;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"Ski recruits the corepressor N-Cor to the SMAD proteins.  ";"";""
3207;LIN2-LIN7-SAP97-MINT1 complex;;Human;Q02410,O14936,Q12959,O14910;320,8573,1739,8825;MI:0019- coimmunoprecipitation;11865057;14.04,40.01.03,41.05.19,45.03.09,75.03.09;"";"";""
3208;LIN2-LIN7 complex;;Human;O14936,O14910;8573,8825;MI:0096- pull down;11865057;14.04,40.01.03,41.05.19,45.03.09,75.03.09;"It was earlier described that LIN-2/CASK and LIN-7 form a complex and localize to the basolateral surfaces of renal epithelia and MDCK (Madin-Darby canine kidney) cells (PMID:10710551).";"";""
3209;LIN2-SAP97 complex;;Mammalia;O14936,Q12959;8573,1739;MI:0096- pull down;11865057;14.04,40.01.03,41.05.19,45.03.09,75.03.09;"Association of SAP97 with LIN-2/CASK is crucial for lateral localization of SAP97 in MDCK cells.";"";""
3210;Dlg3-SAP97 complex;;Rat;Q62696,Q62936;25252,58948;MI:0019- coimmunoprecipitation;12351654;14.04,40.01.03,41.05.19,77.03.01.01.01;"Both Myc-DLG3 and Myc-mLIN-2 bound SAP97 via its MRE domain (found in a pull down experiment using MDCK cells). Immunoprecipitation in rat brain showed that endogenous DLG3 and SAP97 interact in rat brain.";"";""
3211;Lin2/CASK-SAP97 complex;;Mammalia;O70589,Q811D0;12361,13383;MI:0019- coimmunoprecipitation;12351654;14.04,40.01.03,41.05.19,75.03.09;"Both Myc-DLG3 and Myc-mLIN-2 bound SAP97 via its MRE domain.";"";""
3212;Pax7-HMT complex;;Mouse;Q91X20,P47239,O08550,P61965;23808,18509,75410,140858;MI:0007- anti tag coimmunoprecipitation;18066051;11.02.03.04.01,14.07.09,41.05.15,70.10;"Pax7 associates with the Wdr5-Ash2L-MLL2 histone methyltransferase (HMT) complex. Binding of the Pax7-HMT complex to Myf5 resulted in H3K4 tri-methylation of surrounding chromatin. Thus, Pax7 induces chromatin modifications that stimulate transcriptional activation of target genes to regulate entry into the myogenic developmental programme.";"";""
3213;ULBP1-KLRK1-HCST complex;;Human;Q9UBK5,P26718,Q9BZM6;10870,22914,80329;MI:0004- affinity chromatography technologies;11239445;36.25.16;"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.";"";""
3214;G protein complex (Mcf2l, Gnb1, Gng2);;Rat;P54311,Q45QK6,Q63406;24400,80850,117020;MI:0019- coimmunoprecipitation;10518015;30.01.05.05;"";"";""
3215;G protein complex (Kalrn, Gnb1, Gng2);;Rat;P54311,Q45QK6,P97924;24400,80850,84009;MI:0019- coimmunoprecipitation;10518015;30.01.05.05;"";"";""
3216;G protein complex (CACNA1A, GNB1, GNG2);;Bovine;A5ACB9,P62871,P63212;282648,281201,281203;MI:0047- far western blotting;9238069;30.01.05.05,30.05.02.24;"The direct interaction of the G proteins (beta, gamma) with the Ca-channel alpha 1 subunit  is responsible for the channel inhibition by  G protein-coupled receptors.";"";""
3217;MAML2-RBP-Jkappa-Notch2 complex;;Mammalia;Q7TPU6,Q04721,P31266;270118,4853,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3218;MAML2-RBP-Jkappa-Notch3 complex;;Mouse;Q7TPU6,Q61982,P31266;270118,18131,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3219;MAML2-RBP-Jkappa-Notch4 complex;;Mammalia;Q7TPU6,Q99466,P31266;270118,4855,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3220;MAML3-RBP-Jkappa-Notch1 complex;;Mammalia;Q96JK9,P46531,P31266;55534,4851,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3221;MAML3-RBP-Jkappa-Notch2 complex;;Mammalia;Q96JK9,Q04721,P31266;55534,4853,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3222;MAML3-RBP-Jkappa-Notch3 complex;;Mouse;Q69Z97,Q61982,P31266;433586,18131,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3223;MAML3-RBP-Jkappa-Notch4 complex;;Mammalia;Q96JK9,Q99466,P31266;55534,4855,19664;MI:0019- coimmunoprecipitation;12370315;11.02.03.04,16.03.01,30.05.02.14,70.10;"";"";""
3224;G protein complex (NME2, GNB1, GNGT1);;Bovine;P62871,P02698,Q3T0Q4;281201,281796,615447;MI:0047- far western blotting | MI:0004- affinity chromatography technologies | MI:0019- coimmunoprecipitation;12486123;30.01.05.05;"NDPK B (=NME2) contributes to G protein activation by increasing the high energetic phosphate transfer onto GDP via intermediately phosphorylated His-266 in Gbeta1 subunits.";"";""
3225;NMDA receptor complex (NR2A, NR2B, NR1, PSD-95);;Rat;P31016,P35439,Q00959,Q00960;29495,24408,24409,24410;MI:0019- coimmunoprecipitation;15924861;14.04,20.03.01.01,30.01.05.05.01,30.05.02.24.05,30.07,34.03,70.02,73.03.13,77.03.01.01.01;"The authors analyse the links between NMDAR subtypes, Ras-ERK signaling, and AMPAR trafficking. They find that NR2A and NR2B have antagonistic actions on Ras-ERK activation and AMPAR distribution in mature neurons. NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expression of GluR1 - primarily by regulating GluR1 surface insertion.";"";""
3226;Cd74-Cd44 receptor complex;;Mouse;P15379,P04441;12505,16149;MI:0019- coimmunoprecipitation;18056708;30,40;"Cd74 forms a complex with Cd44 on the B cell surface, and the Macrophage migration inhibitory factor (MIF) protein can serve as a ligand for the Cd74-Cd44 receptor complex. This complex is essential for the MIF-induced signaling cascade that results in B cell survival.";"";""
3227;Pick1-Pkca complex, TPA (tissue plasminogen activator) treated;;Rat;Q9EP80,P05696;84591,24680;MI:0007- anti tag coimmunoprecipitation;11466413;14.04,34.03.01,70.02;"A strong complex of Pick1-Pkca was observed when the cells were treated with TPA to activate PKC-alpha. In contrast to PKC-alpha , the binding of PICK1 to GluR2 was constitutive and did not require TPA treatment.";"";""
3228;Pick1-Glur2 complex;;Rat;P19491,Q9EP80;29627,84591;MI:0007- anti tag coimmunoprecipitation;11466413;14.04,34.03.01,70.02;"In contrast to the formation of the complex Pick1-PKCa, which affords treatment with TPA to activate PKC-alpha, the binding of PICK1 to GluR2 was constitutive and did not require TPA treatment.";"";""
3229;Heterodimer complex (CDK9, IL6ST);;Human;P50750,P40189;1025,3572;MI:0019- coimmunoprecipitation;12386808;30.01.05,70.03;"The pleiotropic activities of the gp130-utilizing cytokines point to an extensive role for Cdk9 as a regulator of immune response, inflammation and cell differentiation.";"";""
3230;Heterodimer complex (Cdk9, Il6st);;Mouse;Q99J95,Q00560;107951,16195;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;12386808;30.01.05,70.03;"The pleiotropic activities of the gp130-utilizing cytokines point to an extensive role for Cdk9 as a regulator of immune response, inflammation and cell differentiation.";"";""
3231;Eps15-stonin2 complex;;Human;P42566,Q8WXE9;2060,85439;MI:0077- nuclear magnetic resonance;18200045;14.04,20.09.07;"Eps15 and stonin2 have both been shown to directly associate with the clathrin adaptor complex AP-2 and to localize to clathrin-coated pits (CCPs).";"";""
3232;Hippocalcin-beta2-adaptin complex;;Rat;P62944,P84076;140670,29177;MI:0019- coimmunoprecipitation;16102532;14.04,16.17.01;"The authors describe that in neurons the hippocalcin-AP2 complex binds TfR in a Ca(2+)-independent manner, whereas the complex only binds to AMPARs, like Glur2 in the presence of Ca(2+).  Hippocalcin binds the beta-2-adaptin subunit of the AP2 adaptor complex.  ";"";"The authors state that beta2-adaptin is part of AP2 complex, described in PMID:12086608."
3233;SMAD2-SMAD4-FAST1-TGIF complex, TGF(beta) induced;;Mammalia;O75593,Q15796,Q13485,Q15583;8928,4087,4089,7050;MI:0007- anti tag coimmunoprecipitation;9389648;11.02.03.04.03,16.03.01,30.05.01.18.01,70.10;"This complex is only present in TGF(beta)-treated cells.";"";"The orthologous human proteins are used."
3234;SMAD2-SMAD4-FAST1-TGIF-HDAC1 complex, TGF(beta) induced;;Mammalia;O75593,Q13547,Q15796,Q13485,Q15583;8928,3065,4087,4089,7050;MI:0007- anti tag coimmunoprecipitation;10199400;10.01.09.05,11.02.03.04.03,16.03.01,30.05.01.18.01,42.10.03,70.10;"This complex is only present in TGF(beta)-treated cells. Interaction of TGIF with HDAC1 is necessary for silencing of TGF(beta) transcriptional responses.";"";"The orthologous human proteins are used."
3235;PTF1 complex (Ptf1a, Tcf12, Rbpj);;Mouse;Q9QX98,P31266,Q61286;19213,19664,21406;MI:0006- anti bait coimmunoprecipitation;18198335;11.02.03.04,16.03.01,41.05.04,41.05.13,47.03.01.01.01.02,47.03.11.09,70.10,77.03.01.01.01.02,77.03.11.09;"Transcriptional activity of PTF1 complex is independent of Notch signaling. The PTF1 transcription factor complex determines neuronal identity by inducing GABAergic-specific genes and suppressing glutamergic-specific genes. ";"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.";""
3240;Nsg1-Glur2-Grip1-Stx13 complex;;Rat;P19491,P97879,P02683,Q9ER00;29627,84016,25247,100226;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;16037816;14.04,20.09.18.09.01,70.02,77.03.01.01.01;"The results indicate that NEEP21-GRIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane. ";"";"Since Stx12 (Stx13) from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3262;SCAMP1-SCAMP2-SCAMP3 complex;;Human;O15126,O15127,O14828;9522,10066,10067;MI:0019- coimmunoprecipitation;9224770;20.01.10,20.09.07.06;"";"";""
3263;HERP1/HEY2-NCOR-SIN3A complex;;Human;Q13547,Q9UBP5,Q9Y618,Q96ST3;3065,23493,9612,25942;MI:0007- anti tag coimmunoprecipitation;11486045;10.01.09.05,11.02.03.04.03,16.03.01,42.10.03,70.10;"HERP1/HEY2 associates with the SIN3A complex. ";"";"The authors state that SIN3A is part of the SIN3A complex, described in PMID:11784859."
3269;RB1-HDAC1-BRG1 complex;;Human;Q13547,P06400,P51532;3065,5925,6597;MI:0007- anti tag coimmunoprecipitation;10778858;10.01.09.05,10.03.01.02,11.02.03.04.03,42.10.03,70.10;"Rb forms a repressor containing histone deacetylase (HDAC) and the hSWI/SNF nucleosome remodeling complex, which inhibits transcription of genes for cyclins E and A and arrests cells in the G1 phase of the cell cycle.";"";""
3270;Delta1 homodimer complex;;Human;O00548;28514;MI:0007- anti tag coimmunoprecipitation;12794186;30.05.02.14;"";"";""
3271;Gamma-secretase-Delta1 complex;;Human;Q96BI3,O00548,Q92542,P49768,Q9NZ42;51107,28514,23385,5663,55851;MI:0071- molecular sieving;12794186;30.05.02.14;"";"";""
3276;GluR1-GluR2 complex;;Rat;P19490,P19491;50592,29627;MI:0019- coimmunoprecipitation;15924137;20.01.01.01,20.03.01.01,34.03.01,36.25.03.04.01,73.03.13,77.03.01.01.01;"The results demonstrate a dominant role of the GluR2 subunit in signaling mediated by CaMKII at AMPARs.";"";""
3277;D2 receptor-Nsf-GluR2 complex;;Rat;P61169,P19491,Q9QUL6;24318,29627,60355;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;15858065;14.04,20.01.01.01,20.03.01.01,30.05.02.24.03,34.03.01,77.03.01.01.01;"The results indicate that D2 receptor interacts with GluR2 indirectly through NSF.";"";""
3284;SMN complex (GEMIN5,2,3,4, SMN);;Human;Q9UHI6,P57678,Q8TEQ6,O14893,Q16637;11218,50628,25929,8487,6606;MI:0019- coimmunoprecipitation | MI:0069- mass spectrometry studies of complexes;11714716;11.04.03.01,11.04.05,14.10,16.03.03,20.01.01,70.03,70.10;"Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly.";"Spinal muscular atrophy";""
3289;Ng2-Grip1-Glur2 complex;;Mouse;Q8VHY0,P23819,Q925T6;121021,14800,74053;MI:0006- anti bait coimmunoprecipitation;12458226;14.04,34.03.01,40.01.03.03,73.03.13,77.03.01.01.01;"The authors propose that GRIP1 acts as a scaffolding molecule clustering NG2 and AMPA receptors in immature glia.";"";""
3296;SMN complex (GEMIN5,4,3), SMN-independent intermediate;;Human;Q9UHI6,P57678,Q8TEQ6;11218,50628,25929;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;17640873;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"The survival of motor neurons (SMN) complex is essential for the biogenesis of small nuclear ribonucleoprotein (snRNP) complexes in eukaryotic cells.  ";"Reduced levels of SMN cause the motor neuron degenerative disease, spinal muscular atrophy.";""
3297;SMN complex (GEMIN6,7, UNRIP), SMN-independent intermediate;;Human;Q8WXD5,Q9H840,Q9Y3F4;79833,79760,11171;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;17640873;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"The survival of motor neurons (SMN) complex is essential for the biogenesis of small nuclear ribonucleoprotein (snRNP) complexes in eukaryotic cells. ";"Reduced levels of SMN cause the motor neuron degenerative disease, spinal muscular atrophy.";""
3298;SMN complex (GEMIN2,5, SMN);;Human;Q8TEQ6,O14893,Q16637;25929,8487,6606;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients;17640873;11.04.03.01,11.04.05,14.10,16.03.03,70.03,70.10;"The survival of motor neurons (SMN) complex is essential for the biogenesis of small nuclear ribonucleoprotein (snRNP) complexes in eukaryotic cells.  ";"Reduced levels of SMN cause the motor neuron degenerative disease, spinal muscular atrophy.";""
3335;Homotetrameric complex NIAP;;Human;Q13075;4671;MI:0019- coimmunoprecipitation;15280366;40.10.02.04,73.03.07.02.03;"The expression of NAIP in macrophages and the structural organization of the NAIP raise the possibility that the protein function may be activated by pathogen-associated molecular patterns concomitant with proinflammatory caspases. The authors propose therefore that a key role of NAIP may therefore be to allow caspase-1 activation while suppressing unintentional activation of caspase-3/7 and -9.";"";""
3439;CCT:PhLP complex;;Bovine;Q58DJ8,Q3T115,P19632;504735,533784,287007;MI:0019- coimmunoprecipitation | MI:0040- electron microscopy;15583139;14.01;"PhLP seems to interact with different isoforms of CCT. Complex models:  Model 1: CCT(gamma and delta) on one side of PhLP and CCT (alpha, epsilon, and zeta) on the other side. Model 2: CCT (delta and eta) on one side. and CCT (zeta, beta, and gamma) on the other side. With the exception of CCT isoforms epsilon and gamma,  no other isoforms could be found in the Uniprot database.";"";""
3457;B23-NPM3 complex;;Mouse;Q61937,Q9CPP0;18148,18150;MI:0018- two hybrid;15596447;12.01;"NPM3 interacts with Nucleophosmin to inhibit ribosome biogenesis.";"";""
3458;B23-NPM3 complex;;Mammalia;Q61937,Q9CPP0;18148,18150;MI:0007- anti tag coimmunoprecipitation;15596447;12.01;"NPM3 interacts with Nucleophosmin to inhibit ribosome biogenesis. ";"";""
3489;Klf5-Pias1 complex;;Mouse;Q9Z0Z7,O88907;12224,56469;MI:0018- two hybrid | MI:0007- anti tag coimmunoprecipitation;17178721;11.02.03.04.01,16.03.01,70.10;"The authors demonstrate that Pias1 is a functional partner of Klf5 and enhances the ability of KLF5 to promote proliferation.";"";""
3492;Bax homooligomeric complex, after apoptotic stimulation;;Human;Q07812;581;MI:0030- cross-linking studies;15757910;40.10.02,70.16;"In unstimulated cells BAX normally exists as monomer. After apoptotic stimulation Bax is oligomerized.";"";""
3522;COG complex; Conserved oligomeric golgi tethering complex;Human;Q8WTW3,Q14746,Q96JB2,Q9H9E3,Q9UP83,Q9Y2V7,P83436,Q96MW5;9382,22796,83548,25839,10466,57511,91949,84342;MI:0019- coimmunoprecipitation;15047703;20.09.07,42.08,70.08;"The COG complex plays important roles in Golgi structure and function.";"";""
3525;Tetrameric COG subcomplex;;Human;Q9UP83,Q9Y2V7,P83436,Q96MW5;10466,57511,91949,84342;MI:0019- coimmunoprecipitation;15047703;20.09.07,42.08,70.03;"The COG complex plays important roles in Golgi structure and function.";"";""
3529;Ternary COG subcomplex;;Human;Q9UP83,Q9Y2V7,P83436;10466,57511,91949;MI:0019- coimmunoprecipitation;15047703;20.09.07,42.08,70.08;"The COG complex plays important roles in Golgi structure and function. COG6 interacts with a binary COG5-COG7 subcomplex.  Similarly, it was shown that COG8 interacts with a ternary COG5-COG6-COG7 subcomplex.";"";""
3530;Binary COG subcomplex;;Human;Q9UP83,P83436;10466,91949;MI:0019- coimmunoprecipitation;15047703;20.09.07,42.08,70.08;"The COG complex plays important roles in Golgi structure and function. COG6 interacts with a binary COG5-COG7 subcomplex.  Similarly, it was shown that COG8 interacts with a ternary COG5-COG6-COG7 subcomplex.";"";""
3532;COG1-COG8 subcomplex;;Human;Q8WTW3,Q96MW5;9382,84342;MI:0018- two hybrid | MI:0007- anti tag coimmunoprecipitation;16020545;20.01.10,20.09.07.07,42.08;"COG1-COG8 subcomplex constitutes a bridge linking COG2-COG3-COG4 subcomplex to COG5-COG6-COG7 subcomplex. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.";"";""
3539;Limd1-p62-Traf6-Prkcz complex;;Mouse;Q9QXD8,Q02956,Q64337,P70196;29806,18762,18412,22034;MI:0006- anti bait coimmunoprecipitation;17092936;41.05.17,45.03.05.07;"The authors discuss the potential role of Limd1 as a positive regulator of Traf6 activity, only during states of osteoclastogenic stress.";"";""
3544;COG2-COG3-COG4 subcomplex;;Human;Q14746,Q96JB2,Q9H9E3;22796,83548,25839;MI:0007- anti tag coimmunoprecipitation;16020545;20.01.10,20.09.07.07,42.08;"For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.";"";""
3545;COG5-COG6-COG7 subcomplex;;Human;Q9UP83,Q9Y2V7,P83436;10466,57511,91949;MI:0007- anti tag coimmunoprecipitation;16020545;20.01.10,20.09.07.07,42.08;"For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.";"";""
3551;COG1-COG8-COG2-COG3-COG4 subcomplex;;Human;Q8WTW3,Q14746,Q96JB2,Q9H9E3,Q96MW5;9382,22796,83548,25839,84342;MI:0007- anti tag coimmunoprecipitation;16020545;20.01.10,20.09.07.07,42.08;"COG1 mediates the interaction between COG1-COG8 and COG2-COG3-COG4. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.";"";""
3552;COG1-COG8-COG5-COG6-COG7 subcomplex;;Human;Q8WTW3,Q9UP83,Q9Y2V7,P83436,Q96MW5;9382,10466,57511,91949,84342;MI:0007- anti tag coimmunoprecipitation;16020545;20.01.10,20.09.07.07,42.08;"COG8 mediates interaction between COG1-COG8 subcomplex and COG5-COG6-COG7 subcomplex. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.";"";""
3553;Traf6-p62-aPKC complex, RANK-L stimulated;;Mouse;Q62074,Q64337,P70196;18759,18412,22034;MI:0006- anti bait coimmunoprecipitation;14960283;43.03.21,73.03.07.02.03;"The results indicate that the activation of the RANK pathway promotes the formation of a TRAF6-p62-aPKC complex required for  NF-kappa-B activation, NFATc1 synthesis, and osteoclast differentiation.";"";""
3556;COG complex; COG1-COG8-COG2-COG3-COG4-COG5-COG6-COG7 complex;Human;Q8WTW3,Q14746,Q96JB2,Q9H9E3,Q9UP83,Q9Y2V7,P83436,Q96MW5;9382,22796,83548,25839,10466,57511,91949,84342;MI:0007- anti tag coimmunoprecipitation;16020545;20.01.10,20.09.07.07,42.08;"COG1 mediates the interaction between COG1-COG8 and COG2-COG3-COG4. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.";"";""
3558;Fgf2-Ck2 complex;;Mouse;P67871,P15655;13001,14173;MI:0019- coimmunoprecipitation;10657989;10.03.01.01.03,14.07.03,70.10;"";"";""
3559;Fgf2-Ck2 complex;;Mouse;P67871,P15655;13001,14173;MI:0004- affinity chromatography technologies;15879597;10.03.01.01.03,14.07.03,70.10;"";"";""
3563;Fgf2-Rsk2 complex;;Mouse;P15655,P18654;14173,110651;MI:0096- pull down | MI:0006- anti bait coimmunoprecipitation;15879597;14.07.03,70.10;"Fgf2-Rsk2 complex phosphorylates histone H3 as well as several other proteins.";"";""
3569;Angiomotin isoform p80-Angiostatin complex;;Mouse;Q8VHG2,P20918;27494,18815;MI:0096- pull down;16043488;34.05,47.03.03.02;"The complex is larger than 175 kDa, indicating that the complex consists of more than one angiostatin (38 kDa) and one p80 angiomotin (80 kDa) molecule.";"";""
3618;GammaH2AFX-NDHII-Ku70-DNA complex;;Human;Q08211,P16104,P12956;1660,3014,2547;MI:0006- anti bait coimmunoprecipitation;15613478;10.01.05.01,32.01.09,70.10;"NDH II directly bound to gammaH2AX, whereas association of Ku70 with gammaH2AX was mediated by chromosomal DNA.";"";""
3634;NR3C2-UBC9-SRC-1 complex;;Human;Q15788,P08235,P63279;8648,4306,7329;MI:0019- coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;17105732;11.02.03.04.01,70.10;"The results support a physiological role of Ubc9 as a transcriptional MR coactivator, beyond the known SUMO E2-conjugating enzyme.";"";""
3677;RIN1-STAM2-HRS complex;;Human;O14964,Q13671,O75886;9146,9610,10254;MI:0019- coimmunoprecipitation;17403676;14.04,70.22;"";"";""
3678;RIN1-STAM2-EGFR complex, EGF stimulated;;Human;P00533,Q13671,O75886;1956,9610,10254;MI:0006- anti bait coimmunoprecipitation;17403676;14.04,20.09.18.09.01,30.05.01.12.01,70.22;"It seems that Rin1 plays dual roles, one facilitating cytoskeletal-dependent cellular movement and a second facilitating vesicle trafficking and receptor degradation.";"";""
3710;CHL2-BMP2 complex;;Human;P12643,Q6WN34;650,25884;MI:0071- molecular sieving;17483092;30.05.01.18,41.05.17,45.03.05.07;"";"";""
3711;CHL2-BMP2-TSG complex;;Human;P12643,Q6WN34,Q9GZX9;650,25884,57045;MI:0071- molecular sieving;17483092;30.05.01.18,41.05.17,45.03.05.07;"";"";""
3712;Smad2-Smad4 complex;;Mouse;Q62432,P97471;17126,17128;MI:0065- isothermal titration calorimetry | MI:0114- x-ray crystallography | MI:0226- ion exchange chromatography;15350224;11.02.03.04,30.05.01.18.01,70.10;"Preferential formation of the R-Smad/Smad4 heterotrimer over the R-Smad homotrimer is largely enthalpy driven, contributed by the unique presence of strong electrostatic interactions within the heterotrimeric interfaces.";"";""
3713;Smad3-Smad4 complex;;Mouse;Q8BUN5,P97471;17127,17128;MI:0065- isothermal titration calorimetry | MI:0114- x-ray crystallography | MI:0226- ion exchange chromatography;15350224;11.02.03.04,30.05.01.18.01,70.10;"Preferential formation of the R-Smad/Smad4 heterotrimer over the R-Smad homotrimer is largely enthalpy driven, contributed by the unique presence of strong electrostatic interactions within the heterotrimeric interfaces.";"";""
3714;Pericentrin-GCP complex;;Human;O95613,Q9BSJ2,Q96CW5;5116,10844,10426;MI:0019- coimmunoprecipitation | MI:0018- two hybrid | MI:0047- far western blotting;15146056;10.03.01,10.03.05.01,70.05;"The authors show that the centrosomal coiled-coil protein pericentrin anchors gamma TuRCs at spindle poles through an interaction with gamma tubulin complex proteins 2 and 3 (GCP2/3).";"";""
3715;Pericentrin-GCP complex;;Mouse;P48725,Q921G8,P58854;18541,74237,259279;MI:0019- coimmunoprecipitation | MI:0018- two hybrid | MI:0047- far western blotting;15146056;10.03.01,10.03.05.01,70.05;"The authors show that the centrosomal coiled-coil protein pericentrin anchors gamma TuRCs at spindle poles through an interaction with gamma tubulin complex proteins 2 and 3 (GCP2/3).";"";""
3729;SKI-SMAD2 hexameric complex;;Human;P12755,Q15796;6497,4087;MI:0065- isothermal titration calorimetry | MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3733;SKI-SMAD3 hexameric complex;;Human;P12755,P84022;6497,4088;MI:0065- isothermal titration calorimetry | MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3739;SKI-SMAD2-SMAD4  pentameric complex;;Human;P12755,Q15796,Q13485;6497,4087,4089;MI:0065- isothermal titration calorimetry | MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3740;SKI-SMAD3-SMAD4  pentameric complex;;Human;P12755,P84022,Q13485;6497,4088,4089;MI:0065- isothermal titration calorimetry | MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3741;Slp5-Rab27A complex;;Mouse;Q9ERI2,Q80T23;11891,236643;MI:0006- anti bait coimmunoprecipitation;12051743;20.09.07;"Slp5-Rab27A complex is formed in liver but not in heart.  ";"Rab27A is involved in Griscelli syndrome (human hemophagocytic syndrome).";""
3749;CREBBP-SMAD2 hexameric complex;;Human;Q92793,Q15796;1387,4087;MI:0065- isothermal titration calorimetry | MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3750;CREBBP-SMAD3 hexameric complex;;Human;Q92793,P84022;1387,4088;MI:0065- isothermal titration calorimetry | MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3753;CREBBP-SMAD2-SMAD4 pentameric complex;;Human;Q92793,Q15796,Q13485;1387,4087,4089;MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3754;CREBBP-SMAD3-SMAD4 pentameric complex;;Human;Q92793,P84022,Q13485;1387,4088,4089;MI:0071- molecular sieving;17283070;11.02.03.04,30.05.01.18.01;"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.";"";""
3828;DRIP78-PHLP complex;;Human;Q6Y2X3,Q13371;85406,5082;MI:0012- bioluminescence resonance energy transfer | MI:0007- anti tag coimmunoprecipitation;17363375;14.04,18.02.05,30.01.05.05;"The authors suggest that the DRiP78·PhLP complex is important in selective formation of different G-beta-gamma pairs.";"";""
3830;ADRB2 homodimer complex;;Human;P07550;154;MI:0012- bioluminescence resonance energy transfer;17363375;30.01.05.05,30.05.02.24;"";"";""
3837;SP1-E2F1 complex;;Mouse;Q61501,O89090;13555,20683;MI:0096- pull down | MI:0006- anti bait coimmunoprecipitation;8657141;11.02.03.04.01;"";"";""
3838;SP1-E2F2 complex;;Mammalia;P56931,P08047;242705,6667;MI:0096- pull down;8657141;11.02.03.04.01;"";"";""
3839;SP1-E2F3 complex;;Mammalia;O35261,P08047;13557,6667;MI:0096- pull down;8657141;11.02.03.04.01;"";"";""
3847;TCL1(trimer)-AKT1 complex;;Human;P31749,P56279;207,8115;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;10983986;18.02.01.01.05;"TCL1 forms trimers which associate with AKT1 and binds to AKT PH domain. TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. It stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival. ";"";""
3848;TCL1(trimer)-AKT2 complex;;Human;P31751,P56279;208,8115;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;10983986;18.02.01.01.05;"TCL1 forms trimers which associate with AKT1 and binds to AKT PH domain. TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. It stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival. ";"";""
3849;TCL1(homotrimer) complex;;Human;P56279;8115;MI:0019- coimmunoprecipitation | MI:0095- proteinchip(r) on a surface-enhanced laser desorption/ionization;10983986;18.02.01.01.05;"TCL1 forms trimers which associate with AKT1 and binds to AKT PH domain. TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. It stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival. ";"";""
3852;Rb-HDAC1 complex;;Mammalia;Q13547,P06400;3065,5925;MI:0006- anti bait coimmunoprecipitation;9491888;10.01.09.05,10.03.01.01.03,11.02.03.04.03,14.07.04,42.10.03,70.10;"The interaction was analyzed in CV-1 cells expressing a mixture of endogenous and transfected proteins. H. sapiens is used as model organism for annotation of the subunits. ";"";""
3853;Rb-HDAC1 complex;;Human;Q13547,P06400;3065,5925;MI:0007- anti tag coimmunoprecipitation;9491888;10.01.09.05,10.03.01.01.03,11.02.03.04.03,14.07.04,42.10.03,70.10;"";"";""
3867;Xin-Cdh2-Ctnnb1-Ctnnd1 complex;;Mouse;P15116,Q02248,P30999,O70373;12558,12387,12388,22437;MI:0006- anti bait coimmunoprecipitation;17925400;34.07,42.04.03,75.03.12.03;"The authors found that the actin binding and bundling activity of mXinalpha was enhanced in the presence of beta-catenin. ";"Xirp1 is involved in cardiac hypertrophy and cardiomyopathy (PMID:17766470).";""
3882;Abcg5-Abcg8 complex;;Mouse;Q99PE8,Q9DBM0;27409,67470;MI:0019- coimmunoprecipitation;14504269;20.01.13,20.03.25,77.03.11.07;"The results indicate that G5 and G8 are obligate heterodimers and are dependent on one another for transport out of the ER and for the excretion of hepatic sterols into bile. None of the other G subfamily members supported movement of G5 or G8 out of the ER in these cells.";"";""
3883;Abcg5-Abcg1 complex;;Mouse;Q64343,Q99PE8;11307,27409;MI:0019- coimmunoprecipitation;14504269;70.07;"Any complex formed between G5 and G1, G2, or G4  was retained in the ER.";"";""
3884;Abcg5-Abcg2 complex;;Mouse;Q7TMS5,Q99PE8;26357,27409;MI:0019- coimmunoprecipitation;14504269;70.07;"Any complex formed between G5 and G1, G2, or G4  was retained in the ER.";"";""
3886;Abcg5-Abcg4 complex;;Mouse;Q91WA9,Q99PE8;192663,27409;MI:0019- coimmunoprecipitation;14504269;70.07;"Any complex formed between G5 and G1, G2, or G4  was retained in the ER.";"";""
3888;Abcg8-Abcg4 complex;;Mouse;Q91WA9,Q9DBM0;192663,67470;MI:0019- coimmunoprecipitation;14504269;70.07;"Any complex formed between G5 and G1, G2, or G4 or between G8 and G4 was retained in the ER.";"";""
3900;GABP(gamma)1-E2F1-DP1 complex;;Human;Q01094,Q8TAK5,Q14186;1869,126626,7027;MI:0412- electrophoretic mobility supershift assay;11884602;10.03.01.01.03,11.02.03.04.01,16.03.01,40.10.02,70.10;"";"";""
3903;Grip-Glur2/3-liprin-alpha complex;;Rat;P19491,P19492,Q91Z80,(P97879,Q9WTW1);29627,29628,140592,(84016,171571);MI:0006- anti bait coimmunoprecipitation;11931740;14.04,41.05.13.01,70.02,77.03.01.01.01;"";"";""
3917;Ternary complex (GATA4, SRF, MYOCD);;Human;P43694,Q8IZQ8,P11831;2626,93649,6722;MI:0019- coimmunoprecipitation;15367672;11.02.03.04;"";"";""
3929;Ternary complex (CCD1, Dvl, Rac);;Mammalia;P31750,Q155Q3,P51141;11651,85458,13542;MI:0019- coimmunoprecipitation;15262978;30.01.05.01.02;"";"";""
3930;CCD1-Axin complex;;Mammalia;O35625,Q155Q3;12005,85458;MI:0019- coimmunoprecipitation;15262978;30.01.05.01.02;"Ccd1 drastically inhibits JNK activation both by Axin and by Dvl.";"";""
3941;RCP-Rab11 complex;;Human;P62491,Q6WKZ4;8766,80223;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;15181150;14.04,18.02.07;"The RCP-Rab11 complex regulates the sorting of transferrin receptors from the degradative to the recycling pathway.";"";""
3942;Beta-catenin-Cadherin-LAR complex;;Rat;Q9Z1Y3,Q9WU82,Q64604;83501,84353,360406;MI:0006- anti bait coimmunoprecipitation;15750591;41.05.13.01,73.03.13,77.03.01.01.01;"The authors suggest that one pool of cadherin-beta-catenin is associated with the GRIP-liprin-alpha complex independently of LAR-RPTP, and another pool of beta-catenin-cadherin is associated with LAR-RPTP independently of GRIP-liprin-alpha.";"";""
3943;MondoA-Mlx complex;;Mouse;O08609,Q3UPW8;21428,208104;MI:0006- anti bait coimmunoprecipitation | MI:0047- far western blotting | MI:0412- electrophoretic mobility supershift assay;11073985;11.02.03.04.01,16.03.01,70.03,70.10;"MondoA-Mlx complexes activate transcription when targeted to the nucleus.";"";""
3952;Mlx-Mad1 complex;;Mouse;O08609,P50538;21428,17119;MI:0412- electrophoretic mobility supershift assay;10593926;11.02.03.04.03,16.03.01,70.10;"";"";""
3959;SMAD3-SMAD4-cSKI, TGF(beta)-dependent;;Human;P12755,P84022,Q13485;6497,4088,4089;MI:0412- electrophoretic mobility supershift assay;10575014;11.02.03.04.03,30.05.01.18.01,70.10;"c-SKI interacts with SMAD in a TGF(beta)-dependent manner.";"";""
3961;SMAD3-cSKI-SIN3A-HDAC1 complex;;Human;Q13547,Q96ST3,P12755,P84022;3065,25942,6497,4088;MI:0007- anti tag coimmunoprecipitation;10575014;10.01.09.05,11.02.03.04.03,14.07.04,16.03.01,42.10.03,70.10;"";"";""
3967;SMURF2-SMAD2 complex, TGF(beta)-dependent;;MINK;Q15796,Q9HAU4;4087,64750;MI:0006- anti bait coimmunoprecipitation;11389444;11.02.03.04,14.07.05,30.05.01.18.01,70.10;"SMURF2 interacts stably with phosphorylated SMAD2 in response to TGF(beta) signaling.";"";"Since SMURF2 and SMAD2 from mink were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
3971;SMURF2-SMAD3 complex, TGF(beta)-dependent;;Mammalia;P84022,Q9HAU4;4088,64750;MI:0006- anti bait coimmunoprecipitation;11389444;11.02.03.04,14.07.05,30.05.01.18.01,70.10;"SMURF2 interacts stably with phosphorylated SMAD3 in response to TGF(beta) signaling.";"";"Since SMURF2 and SMAD3 from mink were not available in the UniProt database at the time of annotation, the orthologous human proteins were used."
3972;SMURF2-SMAD3-SnoN complex, TGF(beta)-dependent;;Human;P12757,P84022,Q9HAU4;6498,4088,64750;MI:0006- anti bait coimmunoprecipitation;11389444;11.02.03.04.03,14.07.05,30.05.01.18.01,70.10;"This complex allows SMURF2 to target SnoN for ubiquitin-mediated degradation. ";"";""
3979;mTORC2 complex (mTOR/FRAP1, LST8, mAVO3/RICTOR, SIN1);;Human;P42345,Q9BVC4,Q9BPZ7,Q6R327;2475,64223,79109,253260;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;17043309;30.01.05.01,40.01,42.04.03;"The authors showed that hSin1, similar to Rictor, is selectively required for the phosphorylation and activation of the TORC2 substrate Akt, but not the TORC1 substrate S6K and that it plays an important role in the regulation of Akt activity and the phosphorylation of Akt substrates in vivo. They mentioned LST8 as a conserved component of the complex but did not show it in the experiments.  ";"";""
3980;mTOR-RAPTOR complex;;Human;P42345,Q9BVC4,Q8N122;2475,64223,57521;MI:0006- anti bait coimmunoprecipitation;15268862;30.01.05.01,40.01;"The raptor-mTOR complex regulates by phosphorylating the ribosomal S6 Kinase (S6K) in a  rapamycin-sensitive manner.  ";"";""
3988;ClpP complex, heptameric;;Human;Q16740;8192;MI:0071- molecular sieving;16115876;16.01,70.16;"ClpP occurs as a stable heptamer in solution. Heptameric hClpP has no proteolytic activity and very low peptidase activity.";"";""
3989;ClpP complex, heptameric;;Rat;O88696;53895;MI:0071- molecular sieving;16115876;16.01,70.16;"ClpP occurs as a stable heptamer in solution. Heptameric hClpP has no proteolytic activity and very low peptidase activity.";"";"Since ClpP from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
3990;ClpXP complex;;Rat;O88696,Q9JHS4;53895,270166;MI:0071- molecular sieving;16115876;14.13,16.01,70.16;"In the presence of ATP, ClpX promotes interaction between two ClpP rings, forming a proteolytic active ClpXP complex.";"";"Since ClpP and ClpX from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
3991;ClpX complex, hexameric;;Human;O76031;10845;MI:0028- cosedimentation in solution;16115876;16.01,70.16;"";"";""
3992;ClpXP complex;;Human;Q16740,O76031;8192,10845;MI:0040- electron microscopy;16115876;14.13,16.01,70.16;"In the presence of ATP, ClpX promotes interaction between two ClpP rings, forming a proteolytic active ClpXP complex: two rings of ClpP heptamers bind to two ClpX hexamers.";"";""
4025;Affixin-actinin(alpha) complex;;Human;P12814,Q9HBI1;87,29780;MI:0019- coimmunoprecipitation | MI:0018- two hybrid;15159419;30.05.02.26,70.04.03;"Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell–substrate interaction.";"";""
4039;PAR4-BACE1 complex;;Human;P56817,Q96IZ0;23621,5074;MI:0006- anti bait coimmunoprecipitation;15671026;14.13;"The C-terminal domain of PAR-4 is necessary for forming a complex with the cytosolic tail of BACE1. PAR-4 may be directly involved in regulating the APP cleavage activity of BACE1.";"This complex is involved in the pathogenesis of Alzheimer disease.";""
4043;NEMO-HIF2(alpha)-ARNT complex;;Human;P27540,Q99814,Q9Y6K9;405,2034,8517;MI:0007- anti tag coimmunoprecipitation;15653678;11.02.03.04,30.01.05.01.04;"During hypoxia HIF(alpha) proteins migrate into the nucleus and heterodimerize with the aryl hydrocarbon nuclear translocator ARNT (also called HIF-1(beta)).";"";""
4055;Axin-Dvl-Gsk complex;;Mouse;O35625,P51141,Q9WV60;12005,13542,56637;MI:0007- anti tag coimmunoprecipitation;10428961;30.05.02.20;"Gsk, Dvl and Axin form a complex, which is probably bridged by Axin in the absence of Wnt-signaling. ";"";""
4056;Axin-Dvl-Gsk-Frat1 complex;;Mouse;O35625,P51141,P70339,Q9WV60;12005,13542,14296,56637;MI:0007- anti tag coimmunoprecipitation;10428961;30.05.02.20;"Wnt may promote the disintegration of the Axin-Dvl-Gsk-Frat1 complex. ";"";""
4062;NRP1-VEGFR2-VEGF(165) complex;;Human;P35968,O14786,P15692;3791,8829,7422;MI:0019- coimmunoprecipitation | MI:0107- surface plasmon resonance;17575273;34.07,41.05.16;"VEGF165 mediates the formation of complexes containing VEGFR2 and NRP1, which enhances the affinity of VEGF165 for VEGFR2 and therefore VEGFR2 signaling. VEGF121 does not promote VEGFR2·NRP1 complex formation.";"";""
4072;Heterotrimeric SKP1-CUL1-ROC1 complex;;Human;Q13616,P62877,P63208;8454,9978,6500;MI:0019- coimmunoprecipitation;15118074;10.01.02,14.07.05,14.13.01.01;"SCFhFBH1 (=SKP1/CUL1/ROC1 - human F-box DNA helicase) can act as helicase and E3 ubiquitin ligase.";"";""
4081;Ku70/Ku86 complex; Ku complex;Human;P13010,P12956;7520,2547;MI:0019- coimmunoprecipitation;10783163;10.01.05.01,16.03.01,32.01.09,70.10;"Ku complex interacts with and stimulates the Werner protein.";"";""
4082;Ku70/Ku86/Werner complex;;Human;Q14191,P13010,P12956;7486,7520,2547;MI:0019- coimmunoprecipitation;10783163;10.01.05.01,16.03.01,32.01.09,70.10;"Ku complex interacts with and stimulates the Werner protein. ";"Werner syndrome (=is the hallmark premature aging disorder in which affected humans appear older than their chronological age).";""
4089;SMAD6-HOXC8 complex;;Human;P31273,O43541;3224,4091;MI:0018- two hybrid | MI:0019- coimmunoprecipitation | MI:0413- electrophoretic mobility shift assay;10722652;11.02.03.04.03,16.03.01;"The Smad6-Hoxc8 complex inhibits interaction of Smad1 with Hoxc-8- and Smad1-induced transcription activity.";"";""
4090;SMAD6-HOXA9 complex;;Human;P31269,O43541;3205,4091;MI:0413- electrophoretic mobility shift assay;10722652;16.03.01;"";"";""
4095;Catulin (alpha) - catenin (beta) complex;;Human;Q9UBT7,P35222;8727,1499;MI:0019- coimmunoprecipitation;14993280;30.05.02,34.07;"";"";""
4096;Catenin (alpha) - catenin (beta) complex;;Human;P35221,P35222;1495,1499;MI:0019- coimmunoprecipitation;14993280;30.05.02,34.07;"";"";""
4149;5'-AMP-activated protein kinase complex (AMPK);;Mammalia;Q09137,Q6PAM0,O54950;78975,108097,19082;MI:0007- anti tag coimmunoprecipitation;17012231;01.06;"";"";""
4151;TSC complex;;Rat;O70239,P18265,Q9Z136,P49816;79257,50686,60445,24855;MI:0019- coimmunoprecipitation;15972957;12.07;"TSC1/TSC2 complex associated with GSK3 and Axin  promotes beta-catenin degradation to inhibit Wnt-stimulated TCF/LEF-dependent transcription.";"";""
4158;HSP90-FKBP38-CAM-Ca(2+) complex;;Human;P62158,Q14318,(P07900,P08238);805,23770,(3320,3326);MI:0019- coimmunoprecipitation | MI:0017- classical fluorescence spectroscopy;17379601;40.10.02.04;"The authors show that the TPR domain of FKBP38 interacts with the C-terminal domain of Hsp90, but only if the FKBP38-CaM-Ca(2+) complex is preformed. The resulting ternary complex is enzymatically inactive, and the association of Bcl-2 and the PPIase site of FKBP38 is prevented.";"";""
4200;DLP1-hFIS1 complex;;Human;O00429,Q9Y3D6;10059,51024;MI:0019- coimmunoprecipitation | MI:0055 fluorescent resonance energy transfer;12861026;42.16;"The authors suggest that hFis1 participates in mitochondrial fission through an interaction that recruits DLP1 from the cytosol.";"";""
4216;GR-hnRNP U complex;;Human;Q00839,P04150;3192,2908;MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;9353307;11.02.03.04;"The glucocorticoid receptor (GR) is a ligand-dependent transcription factor that is able to modulate gene activity by binding to its response element, interacting with other transcription factors (here = GRIP120 = hnRNP U), and contacting several accessory proteins such as coactivators.";"";""
4389;EIF3 core complex (EIF3A, EIF3B, EIF3G, EIF3I);;Human;Q14152,P55884,O75821,Q13347;8661,8662,8666,8668;MI:0096- pull down;14688252;12.04.01;"EIF3b appears to be a central scaffolding subunit.";"";""
4392;EIF3 complex (EIF3A, EIF3B, EIF3G, EIF3I, EIF3C);;Human;Q14152,P55884,Q99613,O75821,Q13347;8661,8662,8663,8666,8668;MI:0096- pull down;14688252;12.04.01;"EIF3b appears to be a central scaffolding subunit. EIF3c is able to associate with the four-subunit eIF3 subcomplex, but does so only weakly under these expression and purification conditions.";"";""
4395;EIF3 complex (EIF3B, EIF3G, EIF3I);;Human;P55884,O75821,Q13347;8662,8666,8668;MI:0096- pull down;14688252;12.04.01;"";"";""
4399;EIF3 complex (EIF3B, EIF3J, EIF3I);;Human;P55884,Q13347,O75822;8662,8668,8669;MI:0096- pull down;14688252;12.04.01;"";"";""
4403;EIF3 complex (EIF3A, EIF3B, EIF3G, EIF3I, EIF3J);;Human;Q14152,P55884,O75821,Q13347,O75822;8661,8662,8666,8668,8669;MI:0096- pull down;14688252;12.04.01;"EIF3b appears to be a central scaffolding subunit. The authors conclude that EIF3J promotes the stable association of EIF3 subcomplexes to the 40S ribosomal subunit.";"";""
4478;CBF-DNA complex;;Human;P23511,P25208,Q13952;4800,4801,4802;MI:0413- electrophoretic mobility shift assay | MI:0096- pull down;15243141;11.02.03.04,16.03.01,70.10;"";"";""
4498;p32-CBF-DNA complex;;Human;Q07021,P23511,P25208,Q13952;708,4800,4801,4802;MI:0096- pull down;15243141;11.02.03.04.03,16.03.01,70.10;"p32 interacts specifically with CBF-B subunit and also associates with CBF-DNA complex.";"";""
4869;beta(1)-AR receptosome (ADRB1-SAP97-AKAP79-PRKAR2A);;Human;P08588,P24588,Q12959,P13861;153,9495,1739,5576;MI:0019- coimmunoprecipitation | MI:0055- fluorescent resonance energy transfer;17170109;14.04,14.07.03,30.05.02.24;"SAP97 siRNA abolished the ability of the beta(1)-AR to co-immunoprecipitate AKAP79 and SAP97. This indicates that SAP97 probably serves as a bridging molecule between the beta1-AR and the AKAP79-PKA complex.";"";""
4976;SVIP-p97/VCP-DERL1 complex;;Human;Q9BUN8,Q8NHG7,P55072;79139,258010,7415;MI:0007- anti tag coimmunoprecipitation;17872946;32.01.07,70.07;"The authors identified SVIP as the first endogenous inhibitor of ERAD (ER-associated degradation) that uses a novel mechanism through inhibiting the assembly of the gp78-p97/VCP-Derlin1 complex. The data suggest that p97/VCP and Derlin1 can form a complex with either gp78 or SVIP. The gp78 complex facilitates ERAD, whereas the SVIP complex inhibits ERAD.";"";""
4977;gp78-p97/VCP-DERL1 complex;;Human;Q9UKV5,Q9BUN8,P55072;267,79139,7415;MI:0007- anti tag coimmunoprecipitation;17872946;14.13.01.01,32.01.07,70.07;"The authors identified SVIP as the first endogenous inhibitor of ERAD (ER-associated degradation) that uses a novel mechanism through inhibiting the assembly of the gp78-p97/VCP-Derlin1 complex. The data suggest that p97/VCP and Derlin1 can form a complex with either gp78 or SVIP. The gp78 complex facilitates ERAD, whereas the SVIP complex inhibits ERAD. ";"";""
4997;p97/VCP-VIMP-DERL1 complex;;Human;Q9BUN8,Q9BQE4,P55072;79139,55829,7415;MI:0019- coimmunoprecipitation;16186509;32.01.07,70.07;"";"";""
4998;p97/VCP-VIMP-DERL2 complex;;Human;Q9GZP9,Q9BQE4,P55072;51009,55829,7415;MI:0019- coimmunoprecipitation;16186509;32.01.07,70.07;"";"";""
4999;p97/VCP-VIMP-DERL1-DERL2-HRD1-SEL1L complex;;Human;Q9BUN8,Q9GZP9,Q9UBV2,Q9BQE4,Q86TM6,P55072;79139,51009,6400,55829,84447,7415;MI:0019- coimmunoprecipitation;16186509;32.01.07,70.07;"Cell lin: U373.";"";""
5000;p47-p97 complex;;Rat;O35987,P46462;83809,116643;MI:0019- coimmunoprecipitation;10811609;14.04,20.09.07.27;"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes in.";"";""
5001;p97-Ufd1-Npl4 complex;;Rat;Q9ES54,Q9ES53,P46462;140639,84478,116643;MI:0096- pull down;11740563;14.13.01.01,32.01.07,70.07;"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes.";"";""
5002;p47-p97 complex;;Rat;O35987,P46462;83809,116643;MI:0019- coimmunoprecipitation;11740563;14.04,20.09.07.27;"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes in cytosol.";"";""
5003;p97/VCP homohexamer complex;;Mouse;Q01853;269523;MI:0114- x-ray crystallography | MI:0040- electron microscopy;12949490;14.13.01.01,20.09.07.07,20.09.07.27,32.01.07;"";"";""
5772;ZO1-(beta)cadherin-(VE)cadherin-VEGFR2 complex;;Human;P33151,P35222,P35968,Q07157;1003,1499,3791,7082;MI:0006- anti bait coimmunoprecipitation;18662404;30.05.01.12,41.05.16,42.06,47.03.03.02;"";"";""
5092;Cdk5-p39-CaMKII(alpha)-(alpha)actinin1 complex;;Rat;Q9Z1P2,P11275,Q03114,O35926;81634,25400,140908,12570;MI:0096- pull down;12223541;10.03.01,30.01.05.01,34.05.01,41.05.13,43.03.13,47.03.01.01.01,77.03.01.01.01;" ";"Cdk5 might be a potential drug target for the treatment of neurodegenerative diseases.";"Since Cdk5r2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5099;RB1(hypophosphorylated)-E2F4 complex;;Human;Q16254,P06400;1874,5925;MI:0006- anti bait coimmunoprecipitation;9380698;10.03.01.01.03,11.02.03.04.03;"Hypo-phosphorylated Rb interacts with E2F4 in the early G1 phase of the cell cyclus. Inactivation of Rb by hyper-phosphorylation in late G1 phase causes release of E2F, allowing transcription of genes important for DNA synthesis.";"";""
5100;CyclinD3-CDK4-CDK6 complex;;Human;P30281,P11802,Q00534;896,1019,1021;MI:0007- anti tag coimmunoprecipitation;8930396;10.03.01.01,10.03.01.01.03,30.01.05.01,41.05.15;"Upon myocyte differentiation subunit composition of the CDK4/6 complex is altered. Interaction with cyclinD1 is reduced but interaction with cyclinD3 and p21 is enhanced thus inhibiting the kinase activity of CDK4/6.";"";""
5101;CyclinD3-CDK4-CDK6-p21 complex;;Human;P30281,P11802,Q00534,P38936;896,1019,1021,1026;MI:0007- anti tag coimmunoprecipitation;8930396;10.03.01.01,10.03.01.01.03,30.01.05.01,41.05.15;"Upon myocyte differentiation subunit composition of the CDK4/6 complex is altered. Interaction with cyclinD1 is reduced but interaction with cyclinD3 and p21 is enhanced thus inhibiting the kinase activity of CDK4/6.";"";""
5107;p34(SEI-1)-CDK4-CyclinD2 complex;;Human;P30279,P11802,Q9UHV2;894,1019,29950;MI:0096- pull down;15065884;10.01.03,30.01.05.01;"p34(SEI1) binds to the CDK4-CyclinD2 complex.";"";""
5115;Trip(Br1)-Dp1-E2F1 complex;;Mouse;Q61501,Q9JL10,Q08639;13555,55942,21781;MI:0006- anti bait coimmunoprecipitation;11331592;11.02.03.04.01;"Trip-Br proteins interact with Dp1 thus stimulating the E2F1-Dp1 transcriptional activity.";"";""
5116;Trip(Br2)-Dp1-E2F1 complex;;Mouse;Q61501,Q9JJG5,Q08639;13555,58172,21781;MI:0006- anti bait coimmunoprecipitation;11331592;11.02.03.04.01;"";"";""
5117;pRb2/p130-multimolecular complex (DNMT1, E2F4, SuV39H1, HDAC1, RBL2);;Human;P26358,Q16254,Q13547,Q08999,O43463;1786,1874,3065,5934,6839;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;12789259;11.02.03.01;"";"";""
5118;pRb2/p130-multimolecular complex (RB2, E2F4, HDAC1, SUV39H1, P300);;Human;Q16254,Q09472,Q13547,Q08999,O43463;1874,2033,3065,5934,6839;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;12789259;11.02.03.01;"";"";""
5119;p19-Cdk4 complex;;Mouse;P30285,Q60773;12567,12581;MI:0096- pull down;7739547;10.03.01,18.01.07,18.02.01.02.05,30.01.05.01;"";"";""
5120;p19-Cdk6 complex;;Mouse;Q64261,Q60773;12571,12581;MI:0096- pull down;7739547;10.03.01,18.01.07,18.02.01.02.05,30.01.05.01;"";"";""
5127;p18-Cdk4 complex;;Mouse;P30285,Q60772;12567,12580;MI:0096- pull down;7739547;10.03.01,18.01.07,18.02.01.02.05,30.01.05.01;"";"";""
5128;p18-Cdk6 complex;;Mouse;Q64261,Q60772;12571,12580;MI:0096- pull down;7739547;10.03.01,18.01.07,18.02.01.02.05,30.01.05.01;"";"";""
5142;DCS complex (Ptbp1, Ptbp2, Hnrph1, Hnrpf);;Mouse;Q9Z2X1,O35737,P17225,Q91Z31;98758,59013,19205,56195;MI:0226- ion exchange chromatography | MI:0019- coimmunoprecipitation | MI:0004- affinity chromatography technologies;11003644;11.04.03.01.10,16.03.03,70.10;"";"";""
5143;E2F1-Rb complex;;Human;Q01094,P06400;1869,5925;MI:0412- electrophoretic mobility supershift assay | MI:0006- anti bait coimmunoprecipitation;1531040;10.03.01.01.01,11.02.03.04;"Rb forms a complex with E2F1 in the G1 phase of the cell cycle.";"";""
5144;E2F1-p107-cyclinA complex;;Human;P20248,Q01094,P28749;890,1869,5933;MI:0412- electrophoretic mobility supershift assay | MI:0006- anti bait coimmunoprecipitation;1531040;10.03.01.01.05,11.02.03.04;"p107 forms a complex with E2F1 and cyclin A in the S phase of the cell cycle.";"";""
5145;p19-Cdk4-cyclinD2 complex;;Mouse;P30280,P30285,Q60773;12444,12567,12581;MI:0006- anti bait coimmunoprecipitation;7739547;10.03.01,30.01.05.01;"p19 binds to preassembled cyclinD-CDK complex in vitro and inhibits their activity without replacing Cyclin D. However, affinity for p19 to the uncomplexed CDK4 is higher.";"";""
5146;RB1-TFAP2A complex;;Human;P06400,P05549;5925,7020;MI:0019- coimmunoprecipitation;9632747;11.02.03.04.01;"";"";""
5151;Nsf-Stx1a-Napa complex;;Rat;P54921,Q9QUL6,P32851;140673,60355,116470;MI:0019- coimmunoprecipitation;1315316;20.09.07.27,20.09.16.09.05,77.03.11.07;"";"";""
5152;Nsf-Stx1a-NAPG complex;;Rat;Q99747,Q9QUL6,P32851;8774,60355,116470;MI:0019- coimmunoprecipitation;1315316;20.09.07.27,20.09.16.09.05,77.03.11.07;"";"";"Since Napg from rat was not available in the UniProt database at the time of annotation, the orthologous human protein was used."
5153;CTFC-TAF1 complex;;Human;P49711,Q01105;10664,6418;MI:0029- cosedimentation through density gradients | MI:0004- affinity chromatography technologies;14759373;11.02.03.04;"";"";""
5154;CTCF-nucleophosmin complex;;Human;P49711,P06748;10664,4869;MI:0004- affinity chromatography technologies | MI:0029- cosedimentation through density gradients | MI:0006- anti bait coimmunoprecipitation;14759373;11.02.03.04,70.10;"CTCF and nucleophosmin work together as insularors blocking enhancer activity.";"";""
5158;SMARCA2/BRM-BAF57-MECP2 complex;;Human;P51608,P51531,Q969G3;4204,6595,6605;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;15696166;11.02.03.04.03;"";"";""
5159;E2F4-p107-cyclinE complex;;Human;P24864,Q16254,P28749;898,1874,5933;MI:0412- electrophoretic mobility supershift assay;12096339;10.03.01.01.03,70.10;"In proliferating MCF-7 cells the complex contains mostly cyclin A. After overexpression of cyclin E most of the complexes contain cyclin E. ";"";""
5160;E2F4-p130 complex;;Human;Q16254,Q08999;1874,5934;MI:0412- electrophoretic mobility supershift assay;12096339;10.03.01.01.03,70.10;"After tamoxifen treatment p107 is replaced by p130. ";"";""
5162;ELK1-SRF-ELK3 complex;;Human;P19419,P41970,P11831;2002,2004,6722;MI:0413- electrophoretic mobility shift assay;7540136;11.02.03.04;"";"";""
5165;AP1G1-PACS1-FURIN complex;;Human;O43747,P09958,Q6VY07;164,5045,55690;MI:0096- pull down;11331585;14.04,20.09.07;"The data suggest that PACS-1 functions in a connector capacity by linking acidic cluster motifs to adaptor complexes and their associated vesicle-generating machinery.";"";""
5166;C3G-Crkl-Shp2 complex;;Rat;Q5U2U2,P41499,Q9QYV3;287942,25622,63881;MI:0006- anti bait coimmunoprecipitation;11466412;30.05.01.12;"In untreated cells C3G is tyrosine phosphorylated constitutively and formes a stable complex with CrkL and Shp2. ";"";""
5167;C3G-Crkl-Shp2-Cbl-Egfr complex;;Rat;P22682,Q5U2U2,Q9QX70,P41499,Q9QYV3;12402,287942,24329,25622,63881;MI:0006- anti bait coimmunoprecipitation;11466412;30.05.01.12;"After EGF treatment, C3G is dephosphorylated and a protein complex that includes C3G/CrkL/Shp2/Cbl/Egfr is formed transiently. ";"";"Since Cbl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5168;C3G-Crkl-Shp2-Gab2-TrkA complex;;Rat;Q5U2U2,Q9EQH1,P35739,P41499,Q9QYV3;287942,84477,59109,25622,63881;MI:0006- anti bait coimmunoprecipitation;11466412;30.05.01.12;"After NGF treatment of the cell, C3G remains tyrosine-phosphorylated and the C3G-CrkL-Shp2 complex becomes stably associated with Gab2 and TrkA. ";"";"Since Cbl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5171;SH3KBP1-CBLB-EGFR complex;;Human;Q13191,P00533,Q96B97;868,1956,30011;MI:0007- anti tag coimmunoprecipitation;12177062;20.09.18.09.01.01,30.05.01.12;"Growth factor stimulation led to a complex formation between endogenous SH3KBP1, Cbl-b and EGF or PDGF receptors in several cell lines. The results suggested that SH3KBP1 binding to Cbl-b is important for EGF receptor internalization, although it has no effect on Cbl-b-induced receptor ubiquitination. ";"";""
5172;Sh3kbp1-Cblb-Egfr complex;;Mouse;Q3TTA7,Q01279,Q8R550;208650,13649,58194;MI:0007- anti tag coimmunoprecipitation;12177062;20.09.18.09.01.01,30.05.01.12;"Growth factor stimulation led to a complex formation between endogenous Sh3kbp1, Cbl-b and EGF or PDGF receptors in several cell lines. The results suggested that Sh3kbp1 binding to Cbl-b is important for EGF receptor internalization, although it has no effect on Cbl-b-induced receptor ubiquitination. ";"";""
5173;Sh3kbp1-Cblb-Pdgfrb complex;;Mouse;Q3TTA7,P05622,Q8R550;208650,18596,58194;MI:0007- anti tag coimmunoprecipitation;12177062;20.09.18.09.01.01,30.05.01.12;"Growth factor stimulation led to a complex formation between endogenous Sh3kbp1, Cbl-b and EGF or PDGF receptors in several cell lines. The results suggested that Sh3kbp1 binding to Cbl-b is important for  receptor internalization, although it has no effect on Cbl-b-induced receptor ubiquitination.";"";""
5174;Smarcb1/Ini1-Smarca2-Mecp2 complex;;Mouse;Q9Z2D6,Q99KH6,Q9Z0H3;17257,67155,20587;MI:0047- far western blotting;15696166;11.02.03.04.03;"";"";""
5175;SWI/SNF-related complex;;Mouse;P70288,Q9Z2D6,Q60520,Q3UX55,Q9Z0H3,P97496,O54941;15182,17257,20466,67155,20587,20588,57376;MI:0047- far western blotting;15696166;11.02.03.04.03;"";"";""
5176;MGC1-DNA-PKcs-Ku complex;;Human;Q14676,P78527,P13010,P12956;9656,5591,7520,2547;MI:0096- pull down | MI:0006- anti bait coimmunoprecipitation;15377652;10.01.05.01,10.03.01.03,32.01.09,70.10;"MDC1 directly interacts with the DNA-PKc-Ku complex and this interaction is required for efficient DNA-PK autophosphorylation and DNA damage repair.";"";""
5177;Polycystin-1 multiprotein complex (ACTN1, CDH1, SRC, JUP, VCL, CTNNB1, PXN, BCAR1, PKD1, PTK2, TLN1);;Human;P12814,P56945,P12830,P35222,P14923,P98161,Q05397,P49023,P12931,Q9Y490,P18206;87,9564,999,1499,3728,5310,5747,5829,6714,7094,7414;MI:0029- cosedimentation through density gradients;11113628;34.07,45.03.09,47.03.07.01,75.03.09;"The results suggest that polycystin-1 complexes are present in focal adhesions in subconfluent cells  and in both focal adhesions and cell–cell adherens complexes in confluent cells.";"PKD1 is involved in autosomal dominant polycystic kidney disease (ADPKD).";""
5178;JAK2-PAFR-TYK2 complex;;Mammalia;O60674,P25105,P29597;3717,5724,7297;MI:0007- anti tag coimmunoprecipitation;14500680;30.01.05.01.01;"";"";""
5179;NCOA6-DNA-PK-Ku-PARP1 complex;;Human;Q14686,P09874,P78527,P13010,P12956;23054,142,5591,7520,2547;MI:0096- pull down;12519782;10.01.05.01,70.10;"TRBP (NCOA6) stimulates DNA-PK kinase activity in the absence of DNA.";"";""
5182;DNA-PK-Ku complex; DNA-PK-Ku70-Ku80 complex;Human;P78527,P13010,P12956;5591,7520,2547;MI:0412- electrophoretic mobility supershift assay;9442054;10.01.05.01,14.07.03,16.03.01,18.01.01,18.02.01.01,70.10;"For assembly of the DNA-PK-Ku70-Ku80 complex presence of DNA is necessary.";"";""
5183;DNA-PK-Ku-eIF2-NF90-NF45 complex;;Human;P05198,P20042,P41091,Q12905,Q12906,P78527,P13010,P12956;1965,8894,1968,3608,3609,5591,7520,2547;MI:0412- electrophoretic mobility supershift assay | MI:0006- anti bait coimmunoprecipitation;9442054;10.01.05.01,14.07.03,16.03.01,18.01.01,18.02.01.01,70.10;"NF90, in complex with NF45, interacts with DNA-PKcs and Ku and promotes formation of a complex on DNA.";"";""
5184;SWI/SNF chromatin-remodeling complex;;Human;Q13547,P51608,Q96ST3,P51531,Q969G3;3065,4204,25942,6595,6605;MI:0402- chromatin immunoprecipitation assays;15696166;11.02.03.04.03;"";"";""
5185;SWI/SNF chromatin-remodeling complex (Mecp2, Smarc);;Mouse;P70288,Q9Z2D6,Q60520,Q3UX55,Q9Z0H3,O54941;15182,17257,20466,67155,20587,57376;MI:0029- cosedimentation through density gradients;15696166;11.02.03.04.03;"";"";""
5189;YWHAQ-CALM1-CABIN1 complex;;Human;Q9Y6J0,P62158,P27348;23523,805,10971;MI:0004- affinity chromatography technologies;15902271;30.07;"";"";""
5190;TIAM1-EFNB1-EPHA2 complex;;Human;P98172,P29317,Q13009;1947,1969,7074;MI:0006- anti bait coimmunoprecipitation;14988728;40.01.03.03,41.05.13;"";"";""
5191;Ezh2 methyltransferase complex, cytosolic;;Mammalia;O75530,Q61188,Q15022;8726,14056,23512;MI:0019- coimmunoprecipitation;15882624;14.07.09,70.03;"";"";""
5192;Tiam1-Efnb1-Epha2 complex;;Mouse;P52795,Q03145,Q60610;13641,13836,21844;MI:0006- anti bait coimmunoprecipitation;14988728;40.01.03.03,41.05.13,77.03.01.01.01;"Tiam1 physiologically interacts with ephrin-B1 and EphA2 in the brain of an E14 mouse embryo.";"";""
5193;TNF-alpha/NF-kappa B signaling complex (CHUK, KPNA3, NFKB2, NFKBIB, REL, IKBKG,  NFKB1, NFKBIE, RELB,  NFKBIA, RELA, TNIP2);;Human;O15111,Q9Y6K9,O00505,P19838,Q00653,P25963,Q15653,O00221,Q04864,Q04206,Q01201,Q8NFZ5;1147,8517,3839,4790,4791,4792,4793,4794,5966,5970,5971,79155;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5194;TNF-alpha/NF-kappa B signaling complex (SEC16A, CHUK, IKBKB, NFKB2, REL, IKBKG, MAP3K14, RELA, FBXW7, USP2);;Human;O15111,Q969H0,O14920,Q9Y6K9,Q99558,Q00653,Q04864,Q04206,O15027,O75604;1147,55294,3551,8517,9020,4791,5966,5970,9919,9099;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5195;PTIP-HMT complex;;Human;Q9UBL3,Q9C005,Q8NEZ4,Q14686,Q9BTK6,Q6ZW49,Q15291,O15550,Q9UMN6,P61964;9070,84661,58508,23054,79447,22976,5929,7403,9757,11091;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving;17500065;10.01.09.05,11.02.03.04,14.07.09,16.03.01,42.10.03,70.10;"In cells without DNA damage PTIP associates with proteins involved in regulation of gene expression.";"";""
5196;TNF-alpha/NF-kappa B signaling complex (CHUK, BTRC, NFKB2, PPP6C, REL, CUL1, IKBKE, SAPS2, SAPS1, ANKRD28, RELA, SKP1);;Human;O15084,Q9Y297,O15111,Q13616,Q14164,Q00653,O00743,Q04864,Q04206,Q9UPN7,O75170,P63208;23243,8945,1147,8454,9641,4791,5537,5966,5970,22870,9701,6500;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5197;PTIP-DNA damage response complex;;Human;P54132,P49959,O60934,Q6ZW49,Q92878,Q12888;641,4361,4683,22976,10111,7158;MI:0007- anti tag coimmunoprecipitation | MI:0071- molecular sieving;17500065;10.01.05.01,16.03.01,32.01.09,70.10;"In cells treated with DNA damage agents, PTIP associates with proteins involved in DNA damage response and DNA repair.";"";""
5198;CBP-RARA-RXRA-DNA complex, ligand stimulated;;Human;Q92793,P10276,P19793;1387,5914,6256;MI:0413- electrophoretic mobility shift assay;8616895;11.02.03.04.01,30.01.11,70.10;"The authors suggest that CBP/p300 serves as an integrator of multiple signal transduction pathways within the nucleus.";"";""
5199;Kinase maturation complex 1;;Human;Q16543,P07900,P08238,P34932,Q13163,Q99759,Q7KZI7,Q9NUG6,Q9UHV9,Q6Q0C0,P31946,P62258,P61981,Q04917,P27348,P63104;11140,3320,3326,3308,5607,4215,2011,81572,5202,84231,7529,7531,7532,7533,10971,7534;MI:0676- tandem affinity purification;14743216;30.01.05.01;"";"";""
5727;TBP-TAF complex;;Human;Q15573,Q53T94,Q15572,P20226;9015,9014,9013,6908;MI:0004- affinity chromatography technologies;7801123;11.02.03.01,16.03.01;"";"";""
5206;Pentraxin complex;;Rat;P47971,P97738,O35764,Q62703;266777,288475,81005,29218;MI:0029- cosedimentation through density gradients | MI:0019- coimmunoprecipitation;10748068;34.03.01;"NP1 and NP2 are secreted, exist as higher order multimers (probably pentamers), and interact with taipoxin and taipoxin-associated calcium-binding protein 49 (TCBP49).  NPR is expressed on the cell membrane and does not bind taipoxin or TCBP49 by itself, but it can form heteropentamers with NP1 and NP2 that can be released from cell membranes.";"";""
5209;Ubiquilin-proteasome complex;;Human;P25786,P25787,P60900,Q05086,Q9UMX0,Q9UHD9;5682,5683,5687,7337,29979,29978;MI:0019- coimmunoprecipitation;10983987;14.13.01.01;"";"";""
5210;TANK-TRAF2-TRAF3 complex;;Human;Q92844,Q12933,Q13114;10010,7186,7187;MI:0676- tandem affinity purification;14743216;30.07;"";"";""
5211;RAF1-PPP2-PIN1 complex;;Human;Q13526,P62714,P30153,P63151,P04049;5300,5516,5518,5520,5894;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;15664191;30.05.01.18;"The Raf-1 kinase is an important signaling molecule, functioning in the Ras pathway to transmit mitogenic, differentiative, and oncogenic signals to the downstream kinases MEK and ERK.";"";""
5212;Kinase maturation complex 2;;Human;Q9H6S1,Q16543,P07900,P08238,Q92844,Q9UHD2,A7MCY6,Q12933;64343,11140,3320,3326,10010,29110,9755,7186;MI:0676- tandem affinity purification;14743216;30.01.05.01;"";"";""
5213;Pex26-Pex6-Pex1 complex;;Human;O43933,Q7Z412,Q13608;5189,55670,5190;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;12717447;42.19,70.19;"The results indicate that Pex26 anchors Pex6 and Pex1 through Pex26-Pex6 and Pex6-Pex1 interactions. ";"The complex is involved in peroxisome biogenesis disorders (PBDs), such as Zellweger syndrome and neonatal adrenoleukodystrophy.";""
5215;CS-MAP3K7IP1-MAP3K7IP2 complex;;Human;O75390,Q15750,Q9NYJ8;1431,10454,23118;MI:0676- tandem affinity purification;14743216;30.01.05.01;"";"";""
5216;Casein kinase II (beta-dimer, alpha-dimer);;Bovine;P68399,P67868;282419,539235;MI:0019- coimmunoprecipitation;7768894;14.07.03,30.05.02.20;"";"";""
5217;Calreticulin oligomer complex;;Human;P27797;811;MI:0047- far western blotting | MI:0019- coimmunoprecipitation;15383281;32.01.05;"";"";"The protein complex consists of several  identical subunits (oligomerization)."
5218;Casein kinase II (beta-dimer, alpha, alpha');;Bovine;P68399,P20427,P67868;282419,282420,539235;MI:0019- coimmunoprecipitation;7768894;14.07.03,30.05.02.20;"";"";""
5219;Casein kinase II (beta-dimer, alpha'-dimer);;Bovine;P20427,P67868;282420,539235;MI:0019- coimmunoprecipitation;7768894;14.07.03,30.05.02.20;"";"";""
5220;CHUK-IQGAP2-AKAP8L-RELA-TNIP2 complex;;Human;Q9ULX6,O15111,Q13576,Q04206,Q8NFZ5;26993,1147,10788,5970,79155;MI:0676- tandem affinity purification;14743216;30.01;"";"";""
5222;p14-Mp1-MEK1 complex;;Human;Q02750,Q9Y2Q5,Q9UHA4;5604,28956,8649;MI:0007- anti tag coimmunoprecipitation;11266467;30.01.05.01.03;"";"";""
5223;Casein kinase II (beta-dimer, alpha'-dimer);;Human;P19784,P67870;1459,1460;MI:0018- two hybrid;7768894;14.07.03,30.05.02.20;"";"";""
5224;Casein kinase II (beta-dimer, alpha, alpha');;Human;P68400,P19784,P67870;1457,1459,1460;MI:0018- two hybrid;7768894;14.07.03,30.05.02.20;"";"";""
5225;Casein kinase II (beta-dimer, alpha-dimer);;Human;P68400,P67870;1457,1460;MI:0018- two hybrid;7768894;14.07.03,30.05.02.20;"";"";""
5226;p14-Mp1-ERK2 complex;;Human;Q9Y2Q5,P28482,Q9UHA4;28956,5594,8649;MI:0007- anti tag coimmunoprecipitation;11266467;30.01.05.01.03;"";"";""
5227;p14-Mp1-Erk1/2 complex;;Mouse;O88653,Q9JHS3,(P63085,Q63844);56692,83409,(26413,26417);MI:0029- cosedimentation through density gradients;11266467;30.01.05.01.03,70.02;"";"";""
5228;REL-MAP3K8-RELA-TNIP2-PAPOLA complex;;Human;P41279,P51003,Q04864,Q04206,Q8NFZ5;1326,10914,5966,5970,79155;MI:0676- tandem affinity purification;14743216;30.01.05.01.04;"";"";""
5229;RPA complex; replication complex;Human;P27694,P15927,P35244;6117,6118,6119;MI:0091- chromatography technologies | MI:0029- cosedimentation through density gradients;2833742;10.01.03,16.03.01;"RPA facilitates unwinding of dsDNA.";"";""
5230;CHUK-NFKB2-REL-IKBKG-SPAG9-NFKB1-NFKBIE-COPB2-TNIP1-NFKBIA-RELA-TNIP2 complex;;Human;O15111,P35606,Q9Y6K9,P19838,Q00653,P25963,O00221,Q04864,Q04206,O60271,Q15025,Q8NFZ5;1147,9276,8517,4790,4791,4792,4794,5966,5970,9043,10318,79155;MI:0676- tandem affinity purification;14743216;30.01.05.01.04;"";"";""
5231;53BP1-containing complex; 53BP1-Ku70-Ku80-RPA1-RPA2 complex;Human;P27694,P15927,Q12888,P13010,P12956;6117,6118,7158,7520,2547;MI:0007- anti tag coimmunoprecipitation;15856006;10.01.05.01,16.03.01,32.01.09;"53BP1 is involved in DNA damage-induced RPA2 phosphorylation.";"";""
5232;TNF-alpha/Nf-kappa B signaling complex (RPL6, RPL30, RPS13, CHUK, DDX3X, NFKB2, NFKBIB, REL, IKBKG, NFKB1, MAP3K8, RELB, GLG1, NFKBIA, RELA, TNIP2,  GTF2I);;Human;O15111,O00571,Q92896,P78347,Q9Y6K9,P41279,P19838,Q00653,P25963,Q15653,Q04864,Q04206,Q01201,P62888,Q02878,P62277,Q8NFZ5;1147,1654,2734,2969,8517,1326,4790,4791,4792,4793,5966,5970,5971,6156,6128,6207,79155;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5233;TNF-alpha/NF-kappa B signaling complex 5;;Human;O15446,O15111,Q13616,Q9UKB1,O14920,Q9Y6K9,Q13576,P52292,P42704,P23508,P46199,P19838,Q00653,Q15653,Q16342,O95602,Q9H9Y6,Q9Y2S0,Q9GZS1,P52434,P62875,Q9UJF2,Q04864,Q04206,P63208;10849,1147,8454,23291,3551,8517,10788,3838,10128,4163,4528,4790,4791,4793,5134,25885,84172,51082,64425,5437,5441,9462,5966,5970,6500;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5234;IKBKB-CDC37-KIAA1967-HSP90AB1-HSP90AA1 complex;;Human;Q16543,P07900,P08238,O14920,Q8N163;11140,3320,3326,3551,57805;MI:0676- tandem affinity purification;14743216;30.01.05.01.04;"";"";""
5235;WRN-Ku70-Ku80-PARP1 complex;;Human;P09874,Q14191,P13010,P12956;142,7486,7520,2547;MI:0007- anti tag coimmunoprecipitation | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;14734561;16.03.01,32.01.09,70.10;"PARP1 regulates the exonucleolytic activity of WRN. ";"";""
5237;c-Myc-Max-Arf complex;;Mouse;Q64364,P28574,P01108;12578,17187,17869;MI:0019- coimmunoprecipitation;15361884;11.02.03.04,70.10;"";"";""
5239;CAP(C)-CAP(E) complex; SMC2-SMC4 complex;Human;O95347,Q9NTJ3;10592,10051;MI:0006- anti bait coimmunoprecipitation;9789013;10.03.01.01.11,10.03.04.03,70.10;"CAP(C)-CAP(E) complex is required for mitotic chromosome condensation.";"";""
5241;SMC1-SMC3 complex;;Human;Q14683,Q9UQE7;8243,9126;MI:0006- anti bait coimmunoprecipitation;9789013;10.03.01.01.11,70.10;"SMC1-SMC3 complex is required for metaphase progression in mitotic cells.";"";""
5243;XRCC1-LIG3-PNK-TDP1 complex;;Human;P49916,Q96T60,Q9NUW8,P18887;3980,11284,55775,7515;MI:0006- anti bait coimmunoprecipitation;15744309;10.01.05.01;" ";"TDP1 is involved in Spinocerebellar ataxia with axonal neuropathy (SCAN1).";""
5244;Dolichol-phosphate mannose (DPM) synthase;;Human;O60762,O94777,Q9P2X0;8813,8818,54344;MI:0004- affinity chromatography technologies;10835346;14.07.02,70.07;"The results indicate that DPM2 stabilizes DPM3 and DPM3 stabilizes DPM1.";"";""
5248;Iqgap1-Cdc42-Ctnnb1-Cdh2 complex;;Rat;Q8CFN2,Q9Z1Y3,Q9WU82,Q9JKF1;64465,83501,84353,29875;MI:0019- coimmunoprecipitation;15389538;42.06.04,70.06.04;"";"";"Since Iqgap1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5249;Iqgap1-Cdh1-Ctnnb1-Cdh2 complex;;Rat;Q9R0T4,Q9Z1Y3,Q9WU82,Q9JKF1;83502,83501,84353,29875;MI:0019- coimmunoprecipitation;15389538;42.06.04,70.06.04;"";"";"Since Iqgap1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5250;Iqgap1-Actb-Vim complex;;Rat;P60711,Q9JKF1,P31000;81822,29875,81818;MI:0019- coimmunoprecipitation;15389538;42.06.04,70.06.04;"";"";"Since Iqgap1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5251;Ku-ORC complex;;Human;Q13416,Q9UBD5,O43929,Q9Y5N6,P13010,P12956;4999,23595,5000,23594,7520,2547;MI:0006- anti bait coimmunoprecipitation | MI:0402- chromatin immunoprecipitation assays;15910003;10.01.03.03,16.03.01,16.19.03,70.10.03;"Ku associates specifically with DNA replication origins in vivo in a cell cycle dependent manner, its association being maximal in late G1 phase and decreasing as cells enter S phase (PMID:11694575). ";"";""
5252;Htt-Dctn1-Hap1 complex;;Mouse;O08788,O35668,P42859;13191,15114,15194;MI:0006- anti bait coimmunoprecipitation;15242649;20.09.07,20.09.14,70.04.05;"The authors demonstrate that htt is a processivity factor that increases the transport efficiency of BDNF-containing vesicles along MTs. The alteration of the huntingtin/HAP1/p150(Glued) complex correlates with reduced association of motor proteins with microtubules.";"";""
5253;MNK1-eIF4F complex;;Human;P60842,P06730,Q9BUB5,(Q04637,P78344);1973,1977,8569,(1981,1982);MI:0006- anti bait coimmunoprecipitation;9878069;12.04.01,16.03.03;"Mnk1 is associated with the eIF4F complex. ";"";""
5260;TCF4-CTNNB1-SUMO1-EP300-HADAC6 complex;;Human;P35222,Q09472,Q9UBN7,P63165,P15884;1499,2033,10013,7341,6925;MI:0225- chromatin immunoprecipitation array;15782138;11.02.03.01;"";"";""
5261;TCF4-CTNNB1-EP300 complex;;Human;P35222,Q09472,P15884;1499,2033,6925;MI:0225- chromatin immunoprecipitation array;15782138;11.02.03.01;"";"";""
5262;TCF4-CTNNB1 complex;;Human;P35222,P15884;1499,6925;MI:0225- chromatin immunoprecipitation array;15782138;11.02.03.01;"";"";""
5264;TCF4-CTNNB1-CREBBP complex;;Human;Q92793,P35222,P15884;1387,1499,6925;MI:0225- chromatin immunoprecipitation array;15782138;11.02.03.01;"";"";""
5266;TNF-alpha/NF-kappa B signaling complex 6;;Human;Q16543,O15111,P22087,P07900,P08238,O14920,Q9Y6K9,Q99558,P62888,P36578,Q02878,P62917,P62280,P62277;11140,1147,2091,3320,3326,3551,8517,9020,6156,6124,6128,6132,6205,6207;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5267;VHL-VDU1-TCEB1-TCEB2 complex;;Human;Q15369,Q15370,Q8TEY7,P40337;6921,6923,23032,7428;MI:0007- anti tag coimmunoprecipitation;11739384;14.13.01.01;"Only in the presence of VHL, VDU1 could be precipitated along with VHL, Elongin B and Elongin C.";"";""
5268;TNF-alpha/NF-kappa B signaling complex 7;;Human;Q16543,Q13451,P07900,P08238,O43318,Q15750,Q9NYJ8,Q8N5C8;11140,2289,3320,3326,6885,10454,23118,257397;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5269;TNF-alpha/NF-kappa B signaling complex 8;;Human;Q16543,Q13451,P07900,P08238,Q14164,Q86UP2;11140,2289,3320,3326,9641,3895;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5270;VHL-TCEB1-TCEB2 complex;;Human;Q15369,Q15370,P40337;6921,6923,7428;MI:0007- anti tag coimmunoprecipitation;11739384;14.13.01.01;"";"";""
5271;Kif3-cadherin-catenin complex;;Mouse;P15116,Q02248,P30999,Q61771,P70188;12558,12387,12388,16569,16579;MI:0019- coimmunoprecipitation;15834408;47.03.01.01.01;"";"";""
5273;VHL-TBP1-HIF1A complex;;Human;Q16665,P17980,P40337;3091,5702,7428;MI:0007- anti tag coimmunoprecipitation;14556007;14.13.01.01,32.01.01;"TBP-1 associates with the beta-domain of VHL and complexes with VHL and Hif1-alpha in vivo. The ability of VHL to degrade Hif1-alpha depends in part on its interaction with TBP-1 and suggests a new mechanism for Hif1-alpha stabilization in some VHL-deficient tumors.";"";""
5274;Cell-cell junction complex (ARHGAP10-CTNNA1);;Human;A1A4S6,P35221;79658,1495;MI:0018- two hybrid;16184169;42.06;"ARHGAP10 is a new component of cell-cell junctions that controls alpha-catenin recruitment and has a key role during L. monocytogenes uptake.";"";""
5276;HIF1A-OS9-EGLN1 complex;;Human;Q9GZT9,Q16665,Q13438;54583,3091,10956;MI:0019- coimmunoprecipitation;15721254;11.02.03.04,32.01.01;"The results indicate that OS-9 and PHD2 bind to different regions of HIF-1-alpha, and therefore may bind simultaneously. The results show enhanced binding of PHD2 to V5-OS-9  in the presence of HIF-1-alpha.";"";""
5277;HIF1A-OS9-EGLN3 complex;;Human;Q9H6Z9,Q16665,Q13438;112399,3091,10956;MI:0096- pull down;15721254;11.02.03.04,32.01.01;"Similar to its effect on PHD2, OS-9 stimulates the binding of PHD3 to HIF-1-alpha and cooperates with PHD3 to inhibit HIF-1 transcriptional activity.";"";""
5280;RAB9-TIP47-MPRI complex;;Human;P11717,O60664,P51151;3482,10226,9367;MI:0004- affinity chromatography technologies;11359012;14.04,20.09.07;"Rab9 bound to immobilized CI-MPR only in the presence of TIP47 in a concentration-dependent manner. Thus TIP47 formed a ternary complex linking the CI-MPR and Rab9.";"";""
5281;Cell-cell junction complex (CDH1-CTNNB1);;Human;P12830,P35222;999,1499;MI:0019- coimmunoprecipitation;16184169;30.05.02.28,42.06;"";"";""
5282;CAS-SRC-FAK complex;;Human;P56945,Q05397,P12931;9564,5747,6714;MI:0019- coimmunoprecipitation;9148935;30.05.01.12;"";"";""
5283;tRNA splicing endonuclease;;Human;Q92989,Q8WW01,Q8NCE0,Q9BSV6,Q7Z6J9;10978,116461,80746,79042,283989;MI:0004- affinity chromatography technologies;15109492;11.04.02,11.04.03,70.10;"";"";""
5284;RNA endonuclease (SEN2deltaEx8, SEN54, CLP1);;Human;Q92989,Q8NCE0,Q7Z6J9;10978,80746,283989;MI:0004- affinity chromatography technologies;15109492;11.04;"TSEN2 is an alternatively spliced gene. SEN2deltaEx8 is the variant lacking exon 8. The complex formed with variant SEN2deltaEx8 does not properly cleave pre-tRNAs, although it does retain endonucleolytic activity. It is likely that the SEN2deltaEx8-containing complex is not a tRNA splicing endonuclease but is responsible for processing as yet unknown RNA substrates.";"";""
5285;TNF-alpha/NF-kappa B signaling complex 9;;Human;Q16543,O15111,Q13451,P08238,Q15653;11140,1147,2289,3326,4793;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5286;TNF-alpha/NF-kappa B signaling complex 10;;Human;Q676U5,Q8IX12,Q16543,O15111,P07900,P08238,Q9Y6K9,Q15653,Q9UHD2,P40222;55054,55749,11140,1147,3320,3326,8517,4793,29110,200081;MI:0676- tandem affinity purification;14743216;30.01.05.01.04,40.02.03.01;"";"";""
5287;CDK4-CCND1 complex;;Human;P24385,P11802;595,1019;MI:0019- coimmunoprecipitation;15735718;10.03.01.01.03;"";"";""
5288;P53-BARD1-Ku70 complex;;Human;Q99728,P04637,P12956;580,7157,2547;MI:0019- coimmunoprecipitation;15782130;40.10.02;"";"";""
5291;Cd3e-Nck1-Mink1 complex;;Mouse;P22646,Q9JM52,Q8BMV0;12501,50932,17973;MI:0019- coimmunoprecipitation;15608642;30.01.05.01;"";"";""
5292;Ets2-Ini1-Smarce1-Smarca4 complex;;Mouse;P15037,O35845,Q9Z0H3,O54941;23872,20586,20587,57376;MI:0019- coimmunoprecipitation;12637547;11.02.03.04.03;"";"";""
5293;ETS2-SMARCA4-INI1 complex;;Human;P15036,P51532,Q12824;2114,6597,6598;MI:0019- coimmunoprecipitation;12637547;11.02.03.04.03,70.10;"Brg-1 and Ini1 could be detected in complex with ets-2 after tetracycline removal, but not in cells maintained in tetracycline.";"";""
5295;Cd247 homodimer complex;;Mouse;P24161;12503;MI:0019- coimmunoprecipitation;9218590;14.04,70.02;"";"";""
5296;Cd3e homodimer complex;;Mouse;P22646;12501;MI:0019- coimmunoprecipitation;9218590;14.04,70.02;"";"";""
5301;Striatin-SG2NA-zinedin-caveolin1 complex;;Rat;P41350,P70483,P58405,P58404;25404,29149,114520,97387;MI:0006- anti bait coimmunoprecipitation | MI:0096- pull down;11707266;20.09.07,30.01.09.03,43.03.13,73.03.13,77.03.01.01.01;"Caveolin-1 may directly regulate the function of the proteins of the striatin family, by concentrating them within caveolin-enriched domains.";"";"Since Strn4 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5302;Rab3a-Rims2-Rapgef4 complex;;Mouse;P63011,Q9EQZ6,Q9EQZ7;19339,56508,116838;MI:0096- pull down;11056535;20.09.07.27,20.09.16.09.03;"Rab3A-Rim2-cAMP-GEFII complex was formed in vitro when Rab3A was in the GTP-activated form. The authors showed that cAMP-GEFII is a direct target of cAMP in regulated exocytosis and is responsible for cAMP-dependent, PKA-independent exocytosis.";"";""
5308;Rb-NeuroD1-Ngfi-B complex;;Mouse;Q60867,P12813,Q64701;18012,15370,19650;MI:0006- anti bait coimmunoprecipitation | MI:0007- anti tag coimmunoprecipitation;15701640;11.02.03.04,16.03.01;"Rb provides a bridge to bring together NGFI-B and NeuroD1 within a trimeric complex. ";"";""
5309;Cd3g-Cd3e complex;;Mouse;P22646,P11942;12501,12502;MI:0019- coimmunoprecipitation;9218590;14.04,70.02;"";"";""
5310;Cd3d-Cd3g-Cd3e-Cd247 complex;;Mouse;P24161,P04235,P22646,P11942;12503,12500,12501,12502;MI:0019- coimmunoprecipitation;9218590;30.05.02,43.03.07.02.01.02,70.02;"";"";""
5311;Cd3g-Cd3e-Cd247-Canx complex;;Mouse;P35564,P24161,P22646,P11942;12330,12503,12501,12502;MI:0019- coimmunoprecipitation;9218590;30.05.02,43.03.07.02.01.02,70.02;"";"";""
5315;Munc13-1-Rim2-Rab3a complex;;Rat;P63012,Q9JIS1,Q62768;25531,116839,64829;MI:0071- molecular sieving;16052212;20.01.26,20.09.16.09.05;"The results show that the N-terminal sequence of alpha-RIMs has a modular design that places Rab3A and Munc13-1 into close proximity, but not into competition.";"";""
5317;LATS1-HTRA2-BIRC4 complex;;Human;O43464,O95835,P98170;27429,9113,331;MI:0019- coimmunoprecipitation;16007220;40.10;"WARTS forms a complex with XIAP while interacting with Omi and is potentially involved in the cell death through the inhibition of XIAP.";"";""
5318;DDEF1-CTTN-PXN complex;;Human;Q14247,Q9ULH1,P49023;2017,50807,5829;MI:0006- anti bait coimmunoprecipitation;15719014;42.04;"This co-precipitation was only detected in highly invasive cells, such as MDA-MB-231 and 4T1/luc, but was undetectable in weak or noninvasive cells, such as MDA-MB-468 and MCF7, as well as in normal mammary epithelial cells. The authors describe that AMAP1 bridges cortactin and paxillin in highly invasive cells. ";"";""
5319;CDH1-CKS1B complex;;Human;P12830,P61024;999,1163;MI:0019- coimmunoprecipitation;15014502;10.03.01.01;"";"";""
5320;CDH1-SKP2 complex;;Human;P12830,Q13309;999,6502;MI:0019- coimmunoprecipitation;15014502;10.03.01.01;"";"";""
5321;Cebpa-Smarca2 complex;;Mouse;P53566,O35846;12606,67155;MI:0019- coimmunoprecipitation;15716955;10.03.01,77.03.11.07;"The cEBP-alpha-Brm protein complex was detected in liver extracts from old isochronic parabionts but not from young isochronic parabionts.";"";""
5330;Lef1-Tle1 complex;;Mouse;P27782,Q62440;16842,21885;MI:0067- light scattering;15768032;11.02.03.04,16.03.01;"In the absence of nuclear beta-catenin, Tcf/Lefs act as transcriptional repressors by binding to Groucho/TLE proteins.";"";""
5331;YY1-MDM2-p53 complex;;Human;Q00987,P04637,P25490;4193,7157,7528;MI:0029- cosedimentation through density gradients;15210108;14.07.05,14.13.01.01;"YY1 is a potential cofactor for MDM2 in the regulation of p53 homeostasis. The physical interaction of YY1 with MDM2 appears to be important for efficient MDM2-p53 interaction in vivo, which in turn is necessary for p53 ubiquitination.";"";""
5333;Lef1-Tle1-Ctnnb1 complex;;Mouse;Q02248,P27782,Q62440;12387,16842,21885;MI:0004- affinity chromatography technologies | MI:0027- cosedimentation;15768032;11.02.03.04,16.03.01;"In the absence of nuclear beta-catenin, Tcf/Lefs act as transcriptional repressors by binding to Groucho/TLE proteins.";"";""
5337;ELMO1-DOCK1 complex;;Human;Q14185,Q92556;1793,9844;MI:0007- anti tag coimmunoprecipitation;12134158;16.01,30.01.05.05,34.05.01;"Dock-ELMO complex functions as an unconventional two-part exchange factor for Rac.";"";""
5341;ELMO1-DOCK2 complex;;Human;Q92608,Q92556;1794,9844;MI:0007- anti tag coimmunoprecipitation;12134158;16.01,30.01.05.05,34.05.01;"Dock-ELMO complex functions as an unconventional two-part exchange factor for Rac.";"";""
5342;ELMO1-DOCK1-RAC1 complex;;Human;Q14185,Q92556,P63000;1793,9844,5879;MI:0007- anti tag coimmunoprecipitation;12134158;16.01,30.01.05.05,34.05.01;"Dock-ELMO complex functions as an unconventional two-part exchange factor for Rac.";"";""
5343;ELMO1-DOCK1-CRKII complex;;Human;P46108,Q14185,Q92556;1398,1793,9844;MI:0007- anti tag coimmunoprecipitation;16025104;16.01,30.01.05.05,34.05.01;"";"";""
5344;Endocytic coat complex (11 subunits);;Rat;O08838,P17426,P62944,O08839,P11442,P21575,Q5JC29,O35964,O35179,Q05140,Q62910;60668,11771,140670,117028,54241,140694,313474,81922,116743,65178,85238;MI:0096- pull down;9694653;20.09.18.09.01;"Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2.";"";"Since Ap2a1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5345;Endocytic coat complex (7 subunits);;Rat;O08838,P17426,P62944,O08839,P11442,P21575,Q62910;60668,11771,140670,117028,54241,140694,85238;MI:0096- pull down;9694653;20.09.18.09.01;"Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2.";"";"Since Ap2a1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used."
5348;Pik3r5-Pik3cg complex;;Mouse;Q9JHG7,Q5SW28;30955,320207;MI:0019- coimmunoprecipitation;15797027;18.02.01;"";"";""
5358;GTP-Rho-Rhpn1-Ropn1 complex;;Mouse;Q3TN61,Q61085,Q9ESG2;11848,14787,76378;MI:0096- pull down;10591629;34.05,75.01.01;"";"";""
5360;AGO2-FXR1-TNF(alpha)ARE-RNP complex;;Human;Q9UKV8,P51114;27161,8087;MI:0030- cross-linking studies | MI:0004- affinity chromatography technologies | MI:0006- anti bait coimmunoprecipitation;17382880;12.07,16.03.03,70.03;"AGO2 functions as translational activator under serum-starved conditions.";"";""
5361;Cell division cycle complex (CDC27, CDC16, ANAPC7);;Human;Q9UJX3,Q13042,P30260;51434,8881,996;MI:0019- coimmunoprecipitation;15916961;10.03.01.01;"";"";""
5363;Actin-ribonucleoprotein complex (POLR2A, GTF2F1, HNRNPU);;Human;P35269,Q00839,P24928;2962,3192,5430;MI:0019- coimmunoprecipitation;15711563;11.02.03.01;"";"";""
5365;Ripk2-Nod2 complex;;Mouse;Q8K3Z0,P58801;257632,192656;MI:0019- coimmunoprecipitation;15620648;30.07;"Nod2 binding to R2 and Rip2 expression are necessary for Nod2 to Induce ubiquitinylation of Nemo protein.";"";""
5366;Calm1-Ryr1 complex;;Rat;P62161,Q9R1G1;24244,114207;MI:0040- electron microscopy;11694536;36.25.09.05;"";"";""
5367;THRB-RXRB complex;;Human;P28702,P10828;6257,7068;MI:0096- pull down;9346901;30.01.09.08;"";"";""
5368;Nfkb1-Rela complex;;Mouse;P25799,Q04207;18033,19697;MI:0019- coimmunoprecipitation;9738011;11.02.03.04;"";"";""
5369;ATM homodimer complex;;Human;Q13315;472;MI:0029- cosedimentation through density gradients;15790808;10.01.05.01;"";"";""
5370;ERAP1-ERAP2 complex;;Human;Q9NZ08,Q6P179;51752,64167;MI:0019- coimmunoprecipitation;15908954;36.25.16.03.05;"";"";""
5371;Grancalcin-sorcin complex;;Human;P28676,P30626;25801,6717;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;12804766;16.17.01,45.03.11;"";"";""
5372;SRI homodimer complex;;Human;P30626;6717;MI:0018- two hybrid;12804766;16.01;"";"";""
5373;Chromatin remodeling complex (TACC2, TACC3, PCAF);;Human;Q92831,O95359,Q9Y6A5;8850,10579,10460;MI:0019- coimmunoprecipitation;14767476;10.01.09.05;"";"";""
5375;EGR-EP300 complex;;Human;P18146,Q09472;1958,2033;MI:0019- coimmunoprecipitation;15225550;11.02.03.01;"The results show that the interactions between p300/CBP and Egr1 can lead to complex feedback loops and to inhibition of Egr1 activities under specific conditions.";"";""
5376;Rock1-Pfn2 complex;;Rat;Q9EPC6,Q63644;81531,81762;MI:0019- coimmunoprecipitation;15834419;14.10;"";"";""
5377;RNA-induced silencing complex, RISC; TRBP containing complex (DICER, TRBP, AGO2);Human;Q9UPY3,Q9UKV8,Q15633;23405,27161,6895;MI:0071- molecular sieving | MI:0096- pull down;17507929;11.02.03.04.07,11.04,16.03.03;"The authors describe this complex as minimal Dicer-TRBP-AGO2 complex.";"";""
5378;TRBP containing complex (DICER, TRBP, AGO2, RPL7A, EIF6, MOV10);;Human;Q9UPY3,Q9UKV8,P56537,Q9HCE1,P62424,Q15633;23405,27161,3692,4343,6130,6895;MI:0071- molecular sieving | MI:0096- pull down;17507929;11.02.03.04.07,11.04,16.03.03;"The authors show that depletion of eIF6 in human cells specifically abrogates miRNA-mediated regulation of target protein and mRNA levels.";"";""
5379;Kcna2-Kcnab2 complex;;Rat;P63142,P62483;25468,29738;MI:0019- coimmunoprecipitation | MI:0027- cosedimentation;8608002;20.01.01.01,20.03.01;"";"";""
5380;TRBP containing complex (DICER, RPL7A, EIF6, MOV10 and subunits of the 60S ribosomal particle);;Human;Q9UHA3,Q9UPY3,P56537,Q9HCE1,P62906,P62913,P30050,P26373,P50914,P61313,Q02543,P84098,P46778,P61353,P46779,P62888,P62910,P49207,P18077,Q9Y3U8,P61513,P18124,P62424,P05386,P05387;51187,23405,3692,4343,4736,6135,6136,6137,9045,6138,6142,6143,6144,6155,6158,6156,6161,6164,6165,25873,6168,6129,6130,6176,6181;MI:0071- molecular sieving | MI:0096- pull down;17507929;11.02.03.04.07,12.07,16.03.03;"In mass spectrometric sequencing analyses the authors showed that in addition to RISC subunits they obtained protein sequences corresponding to nearly all subunits of the large (60S) ribosomal particle. The ability of eIF6 to inhibit joining of the 60S and 40S subunits of the ribosome and, thus, to prevent formation of a translationally competent complex, raises the possibility that eIF6 may repress translation by blocking initiation or ribosome recycling.";"";""
5381;RNA-induced silencing complex, RISC; TRBP containing complex (DICER, TRBP, AGO2);Human;Q9UPY3,Q9UKV8,Q15633;23405,27161,6895;MI:0096- pull down | MI:0071- molecular sieving;16271387;11.02.03.04.07,11.04,16.03.03,70.03;"The authors demonstrated that this complex can cleave target RNA using precursor microRNA (pre-miRNA) hairpin as the source of siRNA.";"";""
5382;ARNT-HIF1A complex;;Human;P27540,Q16665;405,3091;MI:0019- coimmunoprecipitation;8663540;11.02.03.04.01,70.10;"";"";""
5383;TRIB3-DDIT3 complex;;Human;P35638,Q96RU7;1649,57761;MI:0019- coimmunoprecipitation;15775988;11.02.03.04;"";"";""
5384;RAG1-RAG2 tetramer complex;;Human;P15918,P55895;5896,5897;MI:0004- affinity chromatography technologies;10373515;10.01.05.03;"";"";""
5385;GAIT complex;;Human;P07814,P04406,P40429,O60506;2058,2597,23521,10492;MI:0004- affinity chromatography technologies;15479637;12.07;"";"";""
5386;MLL1-WDR5 complex;;Human;Q9UBL3,Q8IXM2,Q6PI98,Q9HCK8,O75461,P51610,P34932,Q7Z3B3,Q9Y4W2,Q96EZ8,O43451,Q03164,Q9H7Z6,Q8IZL8,Q9BVI0,Q8WWY3,Q15291,Q99496,Q9Y265,Q9H4L4,P21675,O00268,P49848,Q15545,Q16594,Q9NXF1,P61964;9070,124944,125476,57680,1876,3054,3308,284058,81887,10445,8972,4297,84148,27043,51230,26121,5929,6045,8607,26168,6872,6874,6878,6879,6880,54881,11091;MI:0226- ion exchange chromatography | MI:0007- anti tag coimmunoprecipitation;15960975;10.01.09.05,11.02.03.04.01,14.07.09,70.10;"The MLL1-WDR5 complex has a robust MLL1-mediated histone methyltransferase activity that can effect mono-, di-, and trimethylation of H3 K4 and a MOF-mediated histone acetyltransferase activity that is specific for H4 K16. Both activities are required for optimal transcription activation on a chromatin template in vitro and on an endogenous MLL1 target gene, Hox a9, in vivo. ";"The MLL1 subunit is the product of a protooncogene that was first detected through chromosomal translocations directly associated with aggressive lymphoid and myeloid acute leukemias, especially among infants. ";"The apparent size of the MOF-containing MLL1-WDR5 complex is around 1.5 MDa."
5388;SERPINA1-ELA2 complex;;Human;P08246,P01009;1991,5265;MI:0107- surface plasmon resonance;15131125;14.07.11;"";"";""
5389;SERPINA3-CTSG complex;;Human;P08311,P01011;1511,12;MI:0107- surface plasmon resonance;15131125;14.07.11;"";"";""
5391;SERPINA1-CTSG complex;;Human;P08311,P01009;1511,5265;MI:0107- surface plasmon resonance;15131125;14.07.11;"";"";""
5400;BRCC complex;;Human;P38398,P51587,P46736,Q9NXR7,Q06609;672,675,79184,9577,5888;MI:0004- affinity chromatography technologies;14636569;10.01.05.01,10.03.01.03,14.07.05,32.01.09,70.10;"BRCC may not play a direct role in DNA repair, but through its E3 ubiquitin ligase activity BRCC can regulate factors involved in DNA repair. BRE and BRCC36 are regulatory subunits modulating the ligase activity of the BRCC complex.";"BRCA1 or BRCA2 genes and their deleterious alleles are involved in breast cancer and ovarian cancer.";""
5401;PLEKHM2-KIF5B complex; SKIP-kinesin complex;Human;P33176,Q8IWE5;3799,23207;MI:0096- pull down;15905402;34.05;"During Salmonella typhimurium infection SKIP acts as an essential mediator of SifA (a S. thyphimurium protein, required for the formation of Salmonella-induced filaments). A dynamic process of kinesin recruitment in Salmonella-infected cells is mediated by the secretion of unidentified SPI-2 TTSS effectors and is down-regulated by the SifA-mediated recruitment of SKIP on membranes. The authors suggest that S. typhimurium is able to fine-tune the SCV-associated kinesin motor activity by regulating the secretion of its own effector proteins. ";"";""
5402;Cdk5-Cdk5r1-Pctk1 complex;;Mouse;P49615,P61809,Q04735;12568,12569,18555;MI:0096- pull down;12084709;18.02.01.01.05;"The authors show that Pctaire1 can be phosphorylated by the Cdk5/p25 complex, and serine 95 is the major phosphorylation site. In brain and muscle of Cdk5 null mice, Pctaire1 activity is significantly reduced.";"";""
5404;Myod1-Tcf3 complex;;Mouse;P10085,P15806;17927,21423;MI:0413- electrophoretic mobility shift assay;15719023;11.02.03.04,16.03.01,41.05.15;"";"";""
5405;Myod1 homodimer complex;;Mouse;P10085;17927;MI:0053- fluorescence polarization spectroscopy;9184158;11.02.03.04.01,16.03.01;"";"";""
5406;Myod1-Tcf3 complex;;Mouse;P10085,P15806;17927,21423;MI:0053- fluorescence polarization spectroscopy;9184158;16.03.01,41.05.15;"";"";""
5407;NGF-TrkA complex;;Human;P01138,P04629;4803,4914;MI:0114- x-ray crystallography;10490030;30.05.01.12,41.05.13,47.03.01;"";"";""
5408;Neurotrophin-3-p75 complex;;Human;P08138,P20783;4804,4908;MI:0114- x-ray crystallography;18596692;30.05.01.12,41.05.13,47.03.01;"";"";""
5409;TIAM1-GRIN1 complex;;Human;Q05586,Q13009;2902,7074;MI:0019- coimmunoprecipitation;15721239;40.01,43.03.13;"";"";""
5411;EDG1-HTR1D complex;;Human;P21453,P28221;1901,3352;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5412;HTR1D  homodimer complex;;Human;P28221;3352;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5414;HTR1A-HTR1D complex;;Human;P08908,P28221;3350,3352;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5415;HTR1B homodimer complex;;Human;P28222;3351;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5416;HTR1A-HTR1B complex;;Human;P08908,P28222;3350,3351;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5417;HTR1D-HTR1B complex;;Human;P28222,P28221;3351,3352;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5418;GABBR2-HTR1A complex;;Human;O75899,P08908;9568,3350;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5419;HTR1A-GPR26 complex;;Human;Q8NDV2,P08908;2849,3350;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5420;HTR1A-EDG3 complex;;Human;Q99500,P08908;1903,3350;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5421;HTR1A homodimer complex;;Human;P08908;3350;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5422;HTR1A-EDG1 complex;;Human;P21453,P08908;1901,3350;MI:0019- coimmunoprecipitation;11854302;16.01;"";"";""
5423;HSP70-BAG5-PARK2 complex;;Human;Q9UL15,O60260,(P08107,P34932);9529,5071,(3303,3308);MI:0096- pull down | MI:0019- coimmunoprecipitation;15603737;14.01,18.02.01;"The authors show that within this complex, BAG5 inhibits both parkin E3 ubiquitin ligase activity and Hsp70-mediated refolding of misfolded proteins.";"";""
5424;NGF-p75 complex;;Human;P01138,P08138;4803,4804;MI:0114- x-ray crystallography;15131306;30.05.01.12,41.05.13,47.03.01;"The complex is composed of an NGF homodimer asymmetrically bound to a single p75.";"";""
5426;ANCO1-HDAC3  complex;;Human;Q6UB99,O15379;29123,8841;MI:0019- coimmunoprecipitation | MI:0096- pull down | MI:0018- two hybrid;15184363;11.02.03.04.03;"";"";""
5432;Sororin-cohesin complex;;Human;Q96FF9,Q29RF7,Q9NTI5,O60216,Q14683,Q9UQE7;113130,23244,23047,5885,8243,9126;MI:0004- affinity chromatography technologies | MI:0007- anti tag coimmunoprecipitation;15837422;10.03.01.01,10.03.04.05,70.10;"Sororin interacts with the cohesin complex. It regulates the ability of the cohesin complex to mediate sister chromatid cohesion.";"";""
5435;CycD1-Cdk4 complex;;Mouse;P25322,P30285;12443,12567;MI:0071- molecular sieving | MI:0007- anti tag coimmunoprecipitation;12588994;10.03.01;"";"";""
5436;Cyclin D1-associated protein complex;;Mouse;P25322,P30285,P39689,P17879;12443,12567,12575,15511;MI:0007- anti tag coimmunoprecipitation;12588994;10.03.01.01.01;"Hsc70 functions in the maturation of cyclin D1, thereby facilitating the assembly of an active CyclinD1-CDK4 holoenzyme. ";"";""
5439;Eya1/3-Dach1/2-Six1 complex;;Mouse;Q62231,(Q9QYB2,Q925Q8),(P97767,P97480);20471,(13134,93837),(14048,14050);MI:0402- chromatin immunoprecipitation assays;14628042;11.02.03.04,16.03.01,47.03,70.10;"";"";""
5441;NRG1-IKZF4 complex;;Human;Q9H2S9,Q02297;64375,3084;MI:0019- coimmunoprecipitation;15494726;11.02.03.04;"The Nrg-ICD-Eos complex induces endogenous PSD-95 expression in vivo through a signaling pathway that is mostly independent of gamma-secretase regulation. This upregulation of PSD-95 expression by the Nrg-ICD-Eos complex provides a molecular basis for activity-dependent synaptic plasticity.";"";""
5442;EPOR receptor complex;;Human;P19235;2057;MI:0114- x-ray crystallography;8662530;16.01;"";"";""
5444;CRKII-C3G complex;;Human;P46108,Q13905;1398,2889;MI:0006- anti bait coimmunoprecipitation;9564038;30.01.05.05;"";"";""
5446;EPO-EPOR complex;;Human;P01588,P19235;2056,2057;MI:0114- x-ray crystallography;9774108;30.05.02;"";"";""
5447;Grin2a-Lrp8 complex;;Mouse;P35436,Q924X6;14811,16975;MI:0019- coimmunoprecipitation;16102539;34.03.01;"";"";""
5448;Grin2b-Lrp8 complex;;Mouse;Q01097,Q924X6;14812,16975;MI:0019- coimmunoprecipitation;16102539;34.03.01;"";"";""
5449;Splicing-associated factors complex;-20/24 complex;Human;P35659,Q9Y5S9,Q15287,Q8IYB3,Q86V81;7913,9939,10921,10250,10189;MI:0019- coimmunoprecipitation;11118221;11.04.03.01,16.03.03,70.10;"";"";""
5450;Mediator complex;;Human;Q15648,Q9BTT4,Q9P086,Q9UHV7,Q71F56,O60244,Q96RN5,Q9Y2X0,Q9NVC6,Q9BUE0,Q9H944,Q13503,Q15528,Q9ULK4,O75448,Q71SY5,O95402,Q6P2C8,Q9NX70,Q96HR3,Q9Y3C7,Q9NPJ6,O75586,O43513,Q96G25,A0JLT2,O60313;5469,84246,400569,9969,23389,9282,51586,10025,9440,54797,9477,9412,6837,9439,9862,81857,9441,9442,55588,90390,51003,29079,10001,9443,112950,219541,4976;MI:0004- affinity chromatography technologies;14576168;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10;"";"";""
5451;MED18-MED20-MED29 mediator subcomplex;;Human;Q9BUE0,Q9H944,Q9NX70;54797,9477,55588;MI:0004- affinity chromatography technologies;14576168;11.02.03.04.01,16.01,18.01.07,18.02.09,70.10;"";"";""
5452;Foxo4-Srf-Myocd complex;;Mouse;Q9WVH3,Q8VIM5,Q9JM73;54601,214384,20807;MI:0007- anti tag coimmunoprecipitation;16054032;11.02.03.04,45.03.12.02;"The authors conclude that signal-dependent interaction of Foxo4 with myocardin couples extracellular signals with the transcriptional program for SMC differentiation.";"";""
5459;Axin2-Ctnnb1-Apc complex;;Mouse;Q61315,O88566,Q02248;11789,12006,12387;MI:0007- anti tag coimmunoprecipitation;9554852;30.05.02.20;"The authors suggest that the assembly of a multiprotein complex by conductin controls the stability of b-catenin.";"";""
5460;p50-p65 NF(kappa)B complex;;Human;P19838,Q04206;4790,5970;MI:0018- two hybrid;9556555;11.02.03.04.01,30.01.05.01.04;"";"";""
5461;p50-p65 NF(kappa)B-SRC1 complex;;Human;Q15788,P19838,Q04206;8648,4790,5970;MI:0018- two hybrid;9556555;11.02.03.04.01,30.01.05.01.04;"SRC-1 potentiates NF(kappa)B transactivation.";"";""
5464;I(kappa)B(alpha)-NF(kappa)Bp50-NF(kappa)Bp65 complex;;Human;P19838,P25963,Q04206;4790,4792,5970;MI:0019- coimmunoprecipitation;9738011;30.01.05.01.04,30.07,70.03;"I(kappa)B(alpha) inhibits DNA binding activity of NF(kappa)B heterodimer.";"";""
5465;IKB(epsilon)-RELA-cREL complex;;Human;O00221,Q04864,Q04206;4794,5966,5970;MI:0006- anti bait coimmunoprecipitation;9135156;11.02.03.04,30.01.05.01.04,70.03;"IKB(epsilon) is able to inhibit NF(kappa)B-directed transactivation via cytoplasmic retention of rel proteins. ";"";""
5466;IKB(beta)-RELA-cREL complex;;Human;Q15653,Q04864,Q04206;4793,5966,5970;MI:0006- anti bait coimmunoprecipitation;9135156;11.02.03.04,30.01.05.01.04,70.03;"";"";""
5467;IKB(alpha)-RELA-cREL complex;;Human;P25963,Q04864,Q04206;4792,5966,5970;MI:0006- anti bait coimmunoprecipitation;9135156;11.02.03.04,30.01.05.01.04,30.07,70.03;"";"";""
5473;FAS-FADD-CASP8 complex;;Human;Q14790,Q13158,P25445;841,8772,355;MI:0019- coimmunoprecipitation;15383280;40.10.02;"";"";""
5475;MURR1-NF(kappa)Bp65-IKBA complex;;Human;Q8N668,P25963,Q04206;150684,4792,5970;MI:0006- anti bait coimmunoprecipitation;14685242;30.01.05.01.04;"Murr1, a gene product known previously for its involvement in copper regulation, inhibits HIV-1 growth in unstimulated CD4+ T cells. This inhibition was mediated in part through its ability to inhibit basal and cytokine-stimulated nuclear factor NF(kappa)B activity.";"";""
5492;IKBA-NF(kappa)Bp65-NF(kappa)Bp50 complex;;Human;P19838,P25963,Q04206;4790,4792,5970;MI:0019- coimmunoprecipitation;12972430;30.01.05.01.04,30.07,70.03;"";"";""
5493;Tmsb4x-Lims1-Ilk complex;;Mouse;O55222,Q99JW4,P20065;16202,110829,19241;MI:0007- anti tag coimmunoprecipitation;15565145;34.05.01,36.25.03.01.05,36.25.09.04,75.03.12.03;"The authors showed that the LIM domain protein PINCH and ILK, both of which are necessary for cell migration and survival, formed a complex with thymosin beta4 that resulted in phosphorylation of the survival kinase Akt. Treatment of adult mice with thymosin beta4 after coronary ligation resulted in increased phosphorylation of Akt in the heart, enhanced early myocyte survival and improved cardiac function.";"";""
5495;TFIIH transcription factor complex (ERCC2, ERCC3, GTF2H1, CDK7, CCNH, GTF2H2);;Human;P51946,P50613,P18074,P19447,P32780,Q13888;902,1022,2068,2071,2965,2966;MI:0019- coimmunoprecipitation;12820975;01.04,10.01.05.01,10.03,11.02.03.01,11.02.03.04,18.01.01,18.02.01,70.10;"";"Xeroderma pigmentosum (XP)- Trichothiodystrophy (TTD)- Mutations in the XPD gene result in xeroderma pigmentosum (XP) and trichothiodystrophy (TTD), the phenotypes of which are often intricate.";""
5497;Thyroglobulin folding complex (Tg, Hspa5, Pdi, Erp29, Grp94);;Rat;P52555,P06761,P20717,P06882,Q0R337;117030,25617,29511,24826,362862;MI:0019- coimmunoprecipitation | MI:0029- cosedimentation through density gradients | MI:0051- fluorescence technologies;11884402;14.01;"";"";""
5498;ILK-PARVB-ARHGEF6 complex;;Human;Q15052,Q13418,Q9HBI1;9459,3611,29780;MI:0007- anti tag coimmunoprecipitation;15897874;30.01.05.05.01,42.04.03;"The results suggest that activation of alpha-PIX is dependent on ILK binding to beta-parvin, an event that depends upon ILK activity.";"";""
5499;PARVB-ARHGEF6 complex;;Human;Q15052,Q9HBI1;9459,29780;MI:0007- anti tag coimmunoprecipitation;15897874;42.04.03;"The complex between beta-parvin and alpha-PIX is constitutively formed and is not regulated by either the presence or absence of ILK or its kinase activity. This suggests that ILK may modulate the activity of alpha-PIX indirectly through its binding to and phosphorylation of beta-parvin.";"";""
5500;Thyroglobulin folding complex (Tg, Pdi, Erp29);;Rat;P52555,P20717,P06882;117030,29511,24826;MI:0029- cosedimentation through density gradients;11884402;14.01;"";"";""
5501;Thyroglobulin folding complex (Tg, Hspa5, Erp29, Grp94);;Rat;P52555,P06761,P06882,Q0R337;117030,25617,24826,362862;MI:0019- coimmunoprecipitation;11884402;14.01;"";"";""
5502;EED-EZH-YY1 polycomb complex;;Human;O75530,Q15910,P25490;8726,2146,7528;MI:0006- anti bait coimmunoprecipitation;11158321;11.02.03.04.03,11.02.03.04.07,16.03.01,70.10;"";"";""
5511;Tctex1-channel complex;;Rat;Q02294,Q63100,Q9Z336;257648,29564,83462;MI:0019- coimmunoprecipitation;15768038;20.01.01.01,20.03.01.01;"";"";""
5513;Polycomb repressive complex; hPc2-RING1-BMI1-HPH1 complex;Human;P35226,O00257,P78364,Q06587;648,8535,1911,6015;MI:0006- anti bait coimmunoprecipitation;9199346;11.02.03.04.03,11.02.03.04.07,70.10;"";"";""
5518;BMI1-HPH1-HPH2 complex;;Human;P35226,P78364,Q8IXK0;648,1911,1912;MI:0006- anti bait coimmunoprecipitation | MI:0029- cosedimentation through density gradients;9121482;11.02.03.04.03,11.02.03.04.07,16.03.01,70.10;"";"";""
5521;EED-EZH polycomb complex;;Human;O75530,Q15910;8726,2146;MI:0006- anti bait coimmunoprecipitation | MI:0018- two hybrid;9584199;11.02.03.04.03,11.02.03.04.07,16.03.01,70.10;"";"";""
5524;Bmi1-Mel18-Mph1-M33 polycomb repressor complex;;Mouse;P25916,P30658,P23798,Q64028;12151,12416,22658,13619;MI:0007- anti tag coimmunoprecipitation;9009205;11.02.03.04.03,11.02.03.04.07,70.10;"";"";""
5526;CALM1-FKBP38-BCL2 complex;;Human;P10415,P62158,Q14318;596,805,23770;MI:0019- coimmunoprecipitation;15990872;16.17.01,18.02.01,40.10.02.04;"";"";""
5528;Homodimeric complex Adrb2;;Rat;P10608;24176;MI:0047- far western blotting;15592462;16.01.01;"";"";""
5529;TRAF2-cIAP1/BIRC2 complex;;Human;Q13490,Q12933;329,7186;MI:0019- coimmunoprecipitation;15861135;14.07.05,40.10.02;"";"";""
5530;Homodimeric complex LTBR;;Human;P36941;4055;MI:0018- two hybrid;9371602;16.01.01,30.07;"The viral HCV (hepatitis) core protein can associate with the dimeric or oligomeric form of LT-bR,  and this protein-protein interaction has a modulatory effect  on the signaling pathway of LT-bR in certain cell types.";"";""
5531;Tumor necrosis factor receptor 1 signaling complex;;Human;Q13490,P19438,Q15628,Q12933;329,7132,8717,7186;MI:0019- coimmunoprecipitation;8943045;16.01.01,30.05.02,40.10.02;"";"";""
5532;p35-Cdk5 complex;;Rat;Q03114,P61810;140908,116671;MI:0006- anti bait coimmunoprecipitation;8090221;30.01.05.01.06,73.03.13;"p35 activates the Cdk5 kinase.";"";""
5533;p35-Cdk5 complex;;Bovine;Q02399,Q28199;281066,282173;MI:0006- anti bait coimmunoprecipitation;8090221;30.01.05.01.06,73.03.13,77.03.01.01.01;"p35 activates the Cdk5 kinase.";"";""
5534;PLCB1-PARD3-PARD6A complex;;Human;Q8TEW0,Q9NPB6,Q9NQ66;56288,50855,23236;MI:0019- coimmunoprecipitation;15782111;11.02.03.04,30.01.05.05.03,30.01.09,40.01.03,41.05.19;"The results suggest that the interaction of PLC-beta with cell polarity Par proteins may serve as a nexus to transduce extracellular signals to transcriptional regulation through G-protein-mediated signaling pathway in cell polarity and cell asymmetric division.";"";""
5535;PLCB3-PARD3-PARD6A complex;;Human;Q8TEW0,Q9NPB6,Q01970;56288,50855,5331;MI:0019- coimmunoprecipitation;15782111;11.02.03.04,30.01.05.05.03,30.01.09,40.01.03,41.05.19;"The results suggest that the interaction of PLC-beta with cell polarity Par proteins may serve as a nexus to transduce extracellular signals to transcriptional regulation through G-protein-mediated signaling pathway in cell polarity and cell asymmetric division.";"";""
5540;TRAF2-TRADD complex;;Human;Q15628,Q12933;8717,7186;MI:0019- coimmunoprecipitation;12796506;40.10.02;"TRADD and TRAF2 form a ternary complex  with the viral protein NS5A.";"";""
5541;Ternary complex (TRAF2, FADD, TRADD);;Human;Q13158,Q15628,Q12933;8772,8717,7186;MI:0019- coimmunoprecipitation;12796506;40.10.02;"";"";""
5542;CCNB2-CDC2 complex;;Human;O95067,P06493;9133,983;MI:0019- coimmunoprecipitation;8070405;10.03;"";"";""
5543;CCNB1-CDC2 complex;;Human;P14635,P06493;891,983;MI:0019- coimmunoprecipitation;8070405;10.03;"";"";""
5544;CDC2-PCNA-CCNB1-GADD45A complex;;Human;P14635,P06493,P24522,P12004;891,983,1647,5111;MI:0096- pull down | MI:0019- coimmunoprecipitation;12124778;10.03;"";"";""
5545;CDC2-PCNA-CCNB1-GADD45B complex;;Human;P14635,P06493,O75293,P12004;891,983,4616,5111;MI:0096- pull down | MI:0019- coimmunoprecipitation;12124778;10.03;"";"";""
5546;CDC2-PCNA-CCNB1-GADD45G complex;;Human;P14635,P06493,O95257,P12004;891,983,10912,5111;MI:0096- pull down | MI:0019- coimmunoprecipitation;12124778;10.03;"";"";""
5547;Cdc2-Ccnb1 complex;;Mouse;P24860,P11440;268697,12534;MI:0019- coimmunoprecipitation | MI:0096- pull down;12124778;10.03;"";"";""
5548;IL-12 heterodimer complex;;Human;P29459,P29460;3592,3593;MI:0019- coimmunoprecipitation;7527811;43.03.07.02.01.02;"The authors demonstrated that when p40 is associated with a p35 subunit, the heterodimer acts as an agonist mediating biologic activity, and when p40 associates with another p40, the homodimer behaves as an antagonist in vitro. ";"";""
5549;IL-12 subunit p40 homodimer complex;;Human;P29460;3593;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;7527811;43.03.07.02.01.02;"The authors demonstrated that when p40 is associated with a p35 subunit, the heterodimer acts as an agonist mediating biologic activity, and when p40 associates with another p40, the homodimer behaves as an antagonist in vitro. ";"";""
5550;CDC2-CCNB1-CCNF complex;;Human;P14635,P41002,P06493;891,899,983;MI:0019- coimmunoprecipitation;10716937;10.03;"Cdc2, cyclin B1 and cyclin F form  a complex that exhibits histone  H1 kinase activity.";"";""
5551;CDC2-CCNB1-PTCH1 complex;;Human;P14635,P06493,Q13635;891,983,5727;MI:0019- coimmunoprecipitation;11331587;10.03;"";"";""
5556;CDK2-CCNA2 complex;;Human;P20248,P24941;890,1017;MI:0019- coimmunoprecipitation;8475101;10.03;"";"";""
5557;CDC2-CCNA2 complex;;Human;P20248,P06493;890,983;MI:0019- coimmunoprecipitation;8423786;10.03;"";"";""
5558;PAR6-CDC42 complex;;Human;P60953,Q9BYG5;998,84612;MI:0114- x-ray crystallography;12606577;;"";"";""
5559;CDC2-CCNA2-CDK2 complex;;Human;P20248,P06493,P24941;890,983,1017;MI:0019- coimmunoprecipitation;16009130;10.03;"";"";""
5560;CDK2-CCNE1 complex;;Human;P24864,P24941;898,1017;MI:0019- coimmunoprecipitation;8560263;10.03;"";"";""
5564;LMO4-gp130 complex;;Human;P40189,P23458,P61968,Q06124,O14543;3572,3716,8543,5781,9021;MI:0007- anti tag coimmunoprecipitation;15677447;11.02.03.04.01,30.05.01.05;"LMO4 associates with the gp130 complex and IL-6 may enhance its association. ";"";""
5566;Isl1-Jak1-Stat3 complex;;Mouse;P61372,P52332,P42227;16392,16451,20848;MI:0007- anti tag coimmunoprecipitation;15659653;30.01.05.01.01,47.03.01,73.03.13;"Isl1 may function as an adaptor protein that brings Jak1 and Stat3 in proximity and thereby facilitates Stat3 phosphorylation by Jak1.";"";""
5573;Stat1-alpha-dimer-CBP DNA-protein complex;;Human;Q92793,P42224;1387,6772;MI:0096- pull down | MI:0413- electrophoretic mobility shift assay;8986769;11.02.03.04,70.10;"The results demonstrate that both phosphorylated homodimeric and unphosphorylated monomeric Stat1-alpha can interact with CBP/p300, and their interactions occur at two different regions of both Stat1-alpha and CBP/p300.";"";""
5574;Vps29-Vps35-Vps26a complex;;Mouse;P40336,Q9QZ88,Q9EQH3;30930,56433,65114;MI:0096- pull down | MI:0007- anti tag coimmunoprecipitation;15965486;14.04,20.09.07.07;"The results show that this complex formation is essential for correct localization of mVps29 to endosomal compartments.";"";""
5575;SHP-NR5A2 complex;;Human;Q15466,O00482;8431,2494;MI:0096- pull down | MI:0018- two hybrid;11030331;11.02.03.04.03;"";"";""
5576;Pigr-Vps35-Vps26a-Vps29 complex;;Rat;P15083,Q6AY86,Q9QZ88,Q3TJ43;25046,361846,56433,65114;MI:0006- anti bait coimmunoprecipitation;15247922;14.04,20.09.07.07,70.22,77.03.11.07;"The authors showed that the mammalian Vps35-Vps29-Vps26 retromer subcomplex is involved in pIgR-pIgA transcytosis.";"";""
5577;Ephb1-Sdc2 complex;;Rat;P09759,P34900;24338,25615;MI:0019- coimmunoprecipitation;11580899;43.03.13,73.03.13;"";"";""
5578;Sdc2-Ephb2 complex;;Mouse;P54763,P43407;13844,15529;MI:0019- coimmunoprecipitation;11580899;43.03.13,73.03.13;"";"";""
5579;CNTF-CNTFR-gp130-LIFR complex;;Human;P26441,P26992,P40189,P42702;1270,1271,3572,3977;MI:0030- cross-linking studies;8385113;30.05.01.05,47.03.01;"";"";""
5582;LIFR-LIF-gp130 complex;;Human;P40189,P15018,P42702;3572,3976,3977;MI:0030- cross-linking studies;8385113;30.05.01.05,47.03.01;"";"";""
5583;Per1-Cry1-Cry2-Nono-Wdr5 complex;;Rat;Q32Q86,Q923I8,Q5FVM4,Q8CHI5,Q498M4;299691,170917,317259,287422,362093;MI:0071- molecular sieving;15860628;11.02.03.04.03,34.11.11;"The results suggest that NONO probably operates antagonistically to PER proteins in mammalian cells, and that it is essential to normal circadian rhythmicity in mammals and in Drosophila.";"";""
5584;Per1-Nono-Wdr5 complex;;Rat;Q5FVM4,Q8CHI5,Q498M4;317259,287422,362093;MI:0007- anti tag coimmunoprecipitation;15860628;11.02.03.04.03,34.11.11;"The results suggest that NONO probably operates antagonistically to PER proteins in mammalian cells, and that it is essential to normal circadian rhythmicity in mammals and in Drosophila.";"";""
5585;Per2-Nono-Wdr5 complex;;Rat;Q5FVM4,Q9Z301,Q498M4;317259,63840,362093;MI:0007- anti tag coimmunoprecipitation;15860628;11.02.03.04.03,34.11.11;"The results suggest that NONO probably operates antagonistically to PER proteins in mammalian cells, and that it is essential to normal circadian rhythmicity in mammals and in Drosophila.";"";""
5589;LINC complex, S-phase;;Human;Q96GY3,Q52LA3,Q6MZP7,Q5TKA1,P10244,Q09028,P28749;55957,91750,132660,286826,4605,5928,5933;MI:0006- anti bait coimmunoprecipitation;17671431;10.03.01.01.09,11.02.03.04.01,70.10;"During S-phase B-MYB and p107 become incorporated into the LINC complex. ";"";""
5590;Zip-Prkcz-Kcnab2 complex;;Rat;P62483,P09217,O08623;29738,25522,113894;MI:0006- anti bait coimmunoprecipitation;10477520;18.02.10,34.03,77.03.01.01.01.02;"The results suggest that ZIP acts as a link that targets the activity of PKC-zeta  to Kv-beta 2. ZIP1 and ZIP2, two alternatively spliced protein products, possess distinct activities in stimulating PKC-zeta  phosphorylation of Kv-beta 2. Their ability to interact with each other to form homo- and heteromultimeric complexes provides an explanation for the synergistic stimulatory activity seen only in the presence of both ZIP1 and ZIP2.";"";""
5593;LINC core complex;;Human;Q96GY3,Q52LA3,Q6MZP7,Q5TKA1,Q09028;55957,91750,132660,286826,5928;MI:0029- cosedimentation through density gradients | MI:0007- anti tag coimmunoprecipitation;17671431;10.03.01.01.09,11.02.03.04.01,70.10;"LINC selectively binds to the promoters of G2/M genes whose products are required for mitosis and plays an important role in their cell cycle dependent activation. ";"";""
5596;LINC complex, quiescent cells;;Human;Q16254,Q96GY3,Q52LA3,Q6MZP7,Q5TKA1,Q09028,Q08999;1874,55957,91750,132660,286826,5928,5934;MI:0006- anti bait coimmunoprecipitation;17671431;10.03.01.01.09,11.02.03.04.01,70.10;"In quiescent cells LINC selectively interacts with p130 and E2F4. This association is lost during S-phase. ";"";""
5597;Zip3-Prkcz-Gabrr3 complex;;Rat;P50573,P09217,O08623;192258,25522,113894;MI:0096- pull down;12431995;18.02.07,34.03,77.03.01.01.01;"The authors analysed the splice variant Zip3. Zip3 was able to form homo- and heterodimers and bound to PKC-zeta  and Kv-beta 2. Furthermore, Zip3 interacted with GABAC receptor rho  subunits using a different binding site, allowing simultaneous binding of rho  subunits and PKC-zeta  in vitro. These results suggest a possible formation of a PKC-zeta /ZIP3/GABAC receptor containing macromolecular complex.";"";""
5604;Emerin complex 1;;Human;P60709,Q15417,P50402,Q8WWI1,P35579,Q12965,Q9BRV8,Q13813;60,1266,2010,4008,4627,4643,80143,6709;MI:0004- affinity chromatography technologies;17620012;70.10;"";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5606;Emerin-actin-NMI-(alphaII)spectrin complex;;Human;P60709,P50402,Q13287,Q13813;60,2010,9111,6709;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;70.10;"";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5607;Emerin-actin-NMI complex;;Human;P60709,P50402,Q13287;60,2010,9111;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;70.10;"";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5608;Emerin architectural complex;;Human;P60709,P50402,P02545,P20700,Q13287,Q13813;60,2010,4000,4001,9111,6709;MI:0004- affinity chromatography technologies | MI:0071- molecular sieving | MI:0226- ion exchange chromatography;17620012;42.10,70.10;"";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5609;Emerin regulatory complex;;Human;P60709,O75531,P50402,Q13547,O15379,Q02539,P68431,Q8WWI1,P28749;60,8815,2010,3065,8841,3024,8350,4008,5933;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;10.01.09.05,11.02.03.04,42.10.03,70.10;"";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5610;Alpha-GDI-Hsp90 chaperone complex, ATP dependent;;Rat;P60905,P50398,P82995,P63018;79130,25183,299331,24468;MI:0019- coimmunoprecipitation;12426384;20.09.07.29,20.09.16.09.05,70.02,70.09;"While the major pool comprising the cytosolic form of alpha-GDI in the brain is largely found in a complex with Rab3A (PMID:11152757), the authors found that a minor pool of membrane-associated alpha-GDI forms a complex with chaperones present on the synaptic vesicle membrane. The results suggest a novel role for Hsp90 in regulation of the client molecule alpha-GDI in Rab3A function leading to vesicle targeting and fusion at the synapse.";"";""
5611;Emerin complex 24;;Human;Q9H503,Q07021,P50402,Q02539,P68431,Q00839,P02545,P20700,P49736,P33991,Q14566,Q13287,P06400,Q08999,Q9H0E3;140836,708,2010,3024,8350,3192,4000,4001,4171,4173,4175,9111,5925,5934,79595;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;10.01.03,11.04,70.10;"Complexes are named on the basis of their S300 elution fraction number. Subunits 9-15 were identified via LCMS/MS analysis. ";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5612;Alpha-GDI-Rab3a complex, cytosolic;;Rat;P50398,P63012;25183,25531;MI:0019- coimmunoprecipitation;12426384;20.09.07.27,20.09.07.29,20.09.16.09.05,70.03;"While the major pool comprising the cytosolic form of alpha-GDI in the brain is largely found in a complex with Rab3A (PMID:11152757), the authors found that a minor pool of membrane-associated alpha-GDI forms a complex with chaperones present on the synaptic vesicle membrane.";"";""
5613;Emerin complex 25;;Human;P60709,O75531,Q9P287,Q16543,P50402,Q13283,P61978,P20700,Q9Y333,O95777,Q9H0E3,P62314,P05455,P31946,P62258,O95218;60,8815,56647,11140,2010,10146,3190,4001,57819,51691,79595,6632,6741,7529,7531,9406;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;11.04,30.01,70.10;"Complexes are named on the basis of their S300 elution fraction number. Subunits 5-16 were identified via LCMS/MS analysis. ";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5614;Emerin complex 32;;Human;P60709,Q9H503,Q14839,Q9C005,P50402,Q13547,O15379,P68431,P20700,Q9NPJ6,Q13287,P28749,Q08999,Q9UKL0,O00422,Q12824,Q92922,Q8TAQ2,Q13813,Q9BZK7,Q9BQ87,Q13263;60,140836,1108,84661,2010,3065,8841,8350,4001,29079,9111,5933,5934,23186,10284,6598,6599,6601,6709,79718,90665,10155;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;10.01.09.05,42.10.03,70.10;"Complexes are named on the basis of their S300 elution fraction number. Subunits 9-22 were identified via LCMS/MS analysis. ";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5615;Emerin complex 52;;Human;P60709,Q9BZZ5,Q07021,P12277,O00148,P50402,P51858,Q02539,P61978,P14866,Q00839,Q12906,P46940,Q9Y2U8,P20700,O95777,Q13287,Q53EL6,Q08999,P62314,P10827,P62258,P27348;60,8539,708,1152,10212,2010,3068,3024,3190,3191,3192,3609,8826,23592,4001,51691,9111,27250,5934,6632,7067,7531,10971;MI:0004- affinity chromatography technologies | MI:0226- ion exchange chromatography | MI:0071- molecular sieving;17620012;11.04,30.01,70.10;"Complexes are named on the basis of their S300 elution fraction number. Subunits 8-23 were identified via LCMS/MS analysis. ";"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).";""
5616;Hsp110-Hsc70-Hsp25 complex;;Mouse;P63017,P14602,Q61699;15481,15507,15505;MI:0091- chromatography technologies;10631312;14.01;"Mutational analysis indicate that Hsp25 and Hsp70 can interact with Hsp110 at different sites and that the association of Hsp110 with Hsp25 requires the peptide-binding domain of Hsp110.";"";""
5622;HSP90-CIP1-FKBPL complex;;Human;P38936,Q9UIM3,P07900;1026,63943,3320;MI:0071- molecular sieving | MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;15664193;14.01,32.01.09;"The results show that the ability of WISp39 to stabilize p21 is dependent on its ability to bind and recruit Hsp90.";"";""
5623;Ask1-HSP90-AKT1 complex;;Bovine;Q01314,O35099,(Q76LV2,Q76LV1);280991,26408,(281832,767874);MI:0019- coimmunoprecipitation;15782121;40.10.02;"The data suggest that Hsp90 may serve as a scaffold to hold Akt-ASK1 in close proximity.";"";"Since bovine Map3k5 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. "
5624;Sema3E-PlexinD1 complex;;Mammalia;Q68HV1,P70275;67784,20349;MI:0007- anti tag coimmunoprecipitation;18054858;30.05.02,40.01.03.03,43.03.13,47.03.01.01.01,47.03.03.02,70.02,77.03.01;"Sema3E-PlexinD1 signaling plays an important role in initial development of descending axon tracts in the forebrain. ";"";"Mouse is used as reference organism."
5626;Sema3E-PlexinD1-Nrp1 complex;;Mammalia;P97333,Q68HV1,P70275;18186,67784,20349;MI:0007- anti tag coimmunoprecipitation;18054858;30.05.02,40.01.03.03,43.03.13,47.03.01.01.01,47.03.03.02,70.02,77.03.01;"Sema3E-PlexinD1 signaling plays an important role in the initial development of descending axon tracts in the forebrain. Together with Npn1 the repulsive signaling of Sem3E-PlexinD1 is converted to attraction.  ";"";"Mouse is used as reference organism."
5627;Cdh23-Myo1c complex;;Mouse;Q99PF4,Q9WTI7;22295,17913;MI:0019- coimmunoprecipitation;15057245;20.03.01.01,77.03.02.01;"CDH23 and myosin-1c cooperate to regulate the activity of mechanically gated ion channels in hair cells.";"";""
5628;Ask1-Traf6 complex, LPS induced;;Mouse;O35099,P70196;26408,22034;MI:0006- anti bait coimmunoprecipitation;15864310;36.25.16;"ASK1 formed a complex with TRAF6 in response to LPS (lipopolysaccharide), and this complex formation and subsequent ASK1 activation required LPS-induced production of reactive oxygen species (ROS).";"";""
5629;Sema3E-PlexinD1 complex;;Mammalia;Q68HV1,P70275;67784,20349;MI:0007- anti tag coimmunoprecipitation;15550623;30.05.02,40.01.03.03,43.03.13,47.03.01.01.01,47.03.03.02,70.02,77.03.01;"Sema3E-PlexinD1 signaling does not require neuropilins, which were previously presumed to be obligate Sema3 coreceptors.";"";"Mouse is used as reference organism."
5641;PSD95-FYN-NR2A complex;;Human;P78352,P06241,Q12879;1742,2534,2903;MI:0006- anti bait coimmunoprecipitation;9892651;30.01.05.01.05,70.02;"NR2A was coimmunoprecipitated with Fyn only in the presence of PSD-95. So it was shown that PSD-95 induced formation of a ternary complex of NR2A, PSD-95, and Fyn.";"";""
5642;Securin-separase complex;;Human;Q14674,O95997;9700,9232;MI:0027- cosedimentation | MI:0071- molecular sieving;15880121;10.03.04;"";"";""
5643;ESPL1-CDC2 complex;;Human;P06493,Q14674;983,9700;MI:0019- coimmunoprecipitation;15989971;10.03.04;"";"";""
5644;Sharpin homo-oligomer complex;;Rat;Q9EQL9;81859;MI:0019- coimmunoprecipitation;11178875;14.10;"The potential role of the multimerization of Sharpin is to provide a link between Shank and as yet undentified binding patner(s) of Sharpin.";"";"Oligomer"
5645;Sharpin-Shank1 complex;;Rat;Q9WV48,Q9EQL9;78957,81859;MI:0019- coimmunoprecipitation;11178875;30.01,77.03.01.01.01;"";"";""
5646;FARP2-NRP1-PlexinA1 complex;;Human;O94887,O14786,Q9UIW2;9855,8829,5361;MI:0019- coimmunoprecipitation;16286926;30.05.02,47.03.01;"Interaction of FARP2 with PlexinA1 is substantially reduced in the absence of neuropilin1.";"";""
5647;FARP2-NRP1-PlexinA2 complex;;Human;O94887,O14786,O75051;9855,8829,5362;MI:0019- coimmunoprecipitation;16286926;30.05.02,47.03.01;"";"";""
5648;FARP2-NRP1-PlexinA3 complex;;Human;O94887,O14786,P51805;9855,8829,55558;MI:0019- coimmunoprecipitation;16286926;30.05.02,47.03.01;"";"";""
5649;FARP2-NRP1-PlexinA4 complex;;Human;O94887,O14786,Q9HCM2;9855,8829,91584;MI:0019- coimmunoprecipitation;16286926;30.05.02,47.03.01;"";"";""
5654;SEMA4A-PlexinD1 complex;;Human;Q9Y4D7,Q9H3S1;23129,64218;MI:0030- cross-linking studies;17318185;30.05.02,40.01.03.03,41.05.16,45.03.11,47.03.03.02;"SEMA4A-PlexinD1 signaling negatively regulates angiogenesis.";"";""
5655;Ternary complex (LRRC7, CAMK2a, ACTN4);;Human;O43707,Q9UQM7,Q96NW7;81,815,57554;MI:0397- two hybrid array | MI:0019- coimmunoprecipitation;11160423;34.07;"";"";""
5656;CEBPE-E2F1-RB1 complex;;Human;Q15744,Q01094,P06400;1053,1869,5925;MI:0019- coimmunoprecipitation;12947005;43.03.07.02.02;"";"";""
5659;SEMA3C-PlexinD1-Nrp1 complex;;Mammalia;O14786,Q9Y4D7,Q99985;8829,23129,10512;MI:0428- imaging techniques;15239958;30.05.02,40.01.03.03,41.05.16,45.03.12.03,47.03.03.02;"";"";"Human is used as reference organism."
5660;PlexinC1-SEMA7A complex;;Mammalia;O60486,O75326;10154,8482;MI:0428- imaging techniques;10520995;30.05.02,40.01.03.03;"";"";"Human is used as reference organism."
5661;PlexinC1-SEMA7A complex;;Mammalia;O43157,Q92854;5364,10507;MI:0428- imaging techniques;10520995;30.05.02,40.01.03.03;"";"";"Human is used as reference organism."
5663;TRIM27-RB1 complex;;Human;P06400,P14373;5925,5987;MI:0096- pull down | MI:0019- coimmunoprecipitation;15837424;11.02.03.04;"";"";""
5668;PlexinA1-Nrp1 complex;;Mammalia;O14786,Q9UIW2;8829,5361;MI:0007- anti tag coimmunoprecipitation;10520995;30.05.02,40.01.03.03,47.03.01;"";"";"The orthologous human proteins are used."
5669;PlexinA3-Nrp1 complex;;Mammalia;O14786,P51805;8829,55558;MI:0007- anti tag coimmunoprecipitation;10520995;30.05.02,40.01.03.03,47.03.01;"";"";"Human is used as reference organism"
5670;PlexinB1-Nrp1 complex;;Mammalia;O14786,O43157;8829,5364;MI:0007- anti tag coimmunoprecipitation;10520995;30.05.02,40.01.03.03,47.03.01;"";"";"Human is used as reference organism."
5673;PlexinA1-Nrp2 complex;;Mammalia;O60462,Q9UIW2;8828,5361;MI:0007- anti tag coimmunoprecipitation;10520995;30.05.02,40.01.03.03,47.03.01;"";"";"The orthologous human/mouse proteins are used."
5728;VEGFR2-STAT3 complex, VEGF induced;;Bovine;Q28197,P61635;407170,508541;MI:0006- anti bait coimmunoprecipitation;12824281;11.02.03.04.01,30.05.01.12,41.05.16;"VEGF promotes STAT3-VEGFR2 complex formation in BREC cells, but not in BAEC cells.";"";""
5682;Retn homotrimer  complex;;Mouse;Q99P87;57264;MI:0071- molecular sieving;15155948;01.05.25,01.08.02;"";"";""
5683;hRAD51C-hXRCC3 complex;;Human;Q06609,O43543;5888,7516;MI:0019- coimmunoprecipitation;15123651;10.01.05.01;"";"";""
5684;Membrane protein complex (DERL1, SELS, VCP);;Human;Q9BUN8,Q9BQE4,P55072;79139,55829,7415;MI:0019- coimmunoprecipitation | MI:0051- fluorescence technologies;15215856;16.01.01;"";"";""
5685;Membrane protein complex (VCP, UFD1L, SEC61B);;Human;P60468,Q92890,P55072;10952,7353,7415;MI:0019- coimmunoprecipitation;15215856;16.01.01;"";"";""
5689;SEMA6D-PlexinA1-NRP1 complex;;Human;O14786,Q9UIW2,Q8NFY4;8829,5361,80031;MI:0428- imaging techniques;14977921;30.05.02,40.01.03.03,45.03.12.03,47.03.01,75.03.12.03;"";"";""
5691;TALL1 homo-oligomer complex;;Human;Q9Y275;10673;MI:0071- molecular sieving | MI:0114- x-ray crystallography;14749821;43.03.07.02.01.01;"";"";"Oligomer"
5693;Tip5-Dnmt-Hdac1 complex;;Mouse;Q91YE5,P13864,O88509,O09106;116848,13433,13436,433759;MI:0096- pull down;16085498;11.02.03.04,14.07.04,16.03.01;"";"";""
5694;Nucleolar remodeling complex (NoRC complex);;Human;Q9UIF9,O60264;11176,8467;MI:0019- coimmunoprecipitation;16085498;10.01.09.05,11.02.01,42.10.03;"";"";""
5695;TIP5-DNMT-HDAC1 complex;;Human;Q9UIF9,P26358,Q9UBC3,Q13547;11176,1786,1789,3065;MI:0096- pull down;16085498;11.02.03.04,14.07.04,16.03.01;"";"";""
5696;VEGFA(165)-KDR-NRP1 complex;;Human;P35968,O14786,P15692;3791,8829,7422;MI:0006- anti bait coimmunoprecipitation;11948691;30.05.01.12,41.05.16,45.03.11,47.03.03.02;"Binding of the isoform VEGF(165) to NRP1 is essential for the association of NRP1 and KDR. In contrast, isoform VEGF(121) does no support the complex formation.";"";""
5697;VEGFA(165)-KDR-NRP1 complex;;Pig;Q9N0K7,O14786,P49151;0,8829,397157;MI:0006- anti bait coimmunoprecipitation;11948691;30.05.01,41.05.16,45.03.11,47.03.03.02;"Binding of the isoform VEGF(165) to NRP1 is essential for the association of NRP1 and KDR. In contrast, isoform VEGF(121) does not support the complex formation.";"";"Since NRP1 from pig was not available in the UniProt database at the time of annotation, the orthologous human protein was used."
5698;VEGFA(165)-VEGFR2-NRP1 complex;;Human;P35968,O14786,P15692;3791,8829,7422;MI:0006- anti bait coimmunoprecipitation;18628209;30.05.01.12,41.05.16,45.03.11,47.03.03.02;"VEGFR2 and NRP1 associate upon stimulation with VEGF(165). Phosphorylation of VEGFR2 is required for this association.";"";""
5701;NRP1-VEGF(165/121) complex;;Human;O14786,P15692;8829,7422;MI:0107- surface plasmon resonance;17575273;41.05.16,47.03.03.02;"In contrast to former publications (PMID:10991952), both isoforms of VEGFA, VEGF(165) and VEGF(121), bind to NRP1, but only VEGF165 is sufficient to promote complex formation between VEGFR2 and NRP1.";"";""
5702;VEGF-KDR-NRP2 complex;;Pig;Q9N0K7,Q5RLQ5,P49151;0,0,397157;MI:0031- protein cross-linking with a bifunctional reagent;11278319;30.05.01,41.05.16,45.03.11,47.03.03.02;"";"";""
5705;CyclinA2-Cdk2 complex;;Mouse;P51943,P97377;12428,12566;MI:0019- coimmunoprecipitation;9371520;10.03,32.01.09;"";"";""
5706;CyclinB1-Cdc2 complex;;Mouse;P24860,P11440;268697,12534;MI:0019- coimmunoprecipitation;9371520;10.03,32.01.09;"";"";""
5710;PRMT2 homo-oligomer complex;;Human;P55345;3275;MI:0096- pull down;12039952;18.02.07;"";"";"Oligomer"
5724;CIN85-SH3GL3-CBL complex;;Human;P22681,Q99963,Q96B97;867,6457,30011;MI:0006- anti bait coimmunoprecipitation;11894096;20.09.07.25,20.09.18.09.01,30.05.01.12;"";"";""
5725;Mdm2-P53 complex;;Mouse;P51480,P23804,Q9CXW4,P02340;12578,17246,67025,22059;MI:0019- coimmunoprecipitation;15989966;10.03,40.01,40.10;"";"";""
5729;VEGF-VEGFR2 complex;;Bovine;Q28197,P15691;407170,281572;MI:0006- anti bait coimmunoprecipitation;12824281;30.05.01.12,41.05.16,45.03.11;"";"";""
5730;IKBKG homotrimer complex;;Human;Q9Y6K9;8517;MI:0018- two hybrid | MI:0030- cross-linking studies;12435599;18.02.01;"";"";""
5731;NRP1-VEGFC complex, heparin dependent;;Human;O14786,P49767;8829,7424;MI:0004- affinity chromatography technologies;16816121;20.09.18.09.01.01,30.05.01.12,41.05.16,70.09;"";"";""
5732;NRP2-VEGFC complex;;Human;O60462,P49767;8828,7424;MI:0004- affinity chromatography technologies | MI:0428- imaging techniques;16816121;20.09.18.09.01.01,30.05.01.12,41.05.16,70.09;"VEGFC colocalizes with NRP2 in endocytotic vesicles.";"";""
5733;NRP2-VEGFD complex, heparin dependent;;Human;O43915,O60462;2277,8828;MI:0004- affinity chromatography technologies | MI:0428- imaging techniques;16816121;20.09.18.09.01.01,30.05.01.12,41.05.16,70.09;"VEGFD colocalizes with NRP2 in endocytotic vesicles.";"";""
5734;NRP1-VEGFD complex, heparin dependent;;Human;O43915,O14786;2277,8829;MI:0004- affinity chromatography technologies;16816121;20.09.18.09.01.01,30.05.01.12,41.05.16,70.09;"";"";""
5735;TGF-beta receptor-SMAD3 complex;;Human;P84022,P36897,P37173;4088,7046,7048;MI:0019- coimmunoprecipitation;8774881;30.05.01.18.01,40.02.03.05;"";"";""
5736;Pre-initiation complex (PIC);;Human;P60709,P24928,P20226;60,5430,6908;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;15502823;11.02.03.01.01,16.03;"Actin is required for the initiation of transcription (for the formation of pre-initiation complexes).";"";""
5737;Multicomponent signaling complex, anti-CD40 stimulated (Birc2, Birc3, Cd40, Ikbkg, Map2k4, Map2k7, Map3k1, Traf2, Ube2n);;Mouse;Q62210,O08863,P27512,O88522,P47809,Q8CE90,P53349,P39429,P61089;11797,11796,21939,16151,26398,26400,26401,22030,93765;MI:0006- anti bait coimmunoprecipitation;18635759;30.01.05.01.03,36.25.16.03.01,43.03.07.02.01.01,73.03.07.02.01.01;"With anti-CD40 as the immunoprecipitating antibody the complex included trace amounts of the MEKK1 substrates MKK4 and MKK7, furthermore it was shown that the amounts of most complex components declined between 10 and 30 min after stimulation.  The results indicate that MAPK signaling, at least by CD40 and other TNFRs, follows a two-stage mechanism based on assembly of a multiprotein complex at the receptor that primes MAP3Ks for activation, but in which kinase activation is delayed until the complex is released to the cytoplasm.";"";""
5740;NRP2-VEGFR3 complex;;Human;P35916,O60462;2324,8828;MI:0004- affinity chromatography technologies;16816121;20.09.18.09.01.01,30.05.01.12,41.05.16,70.09;"";"";""
5742;Multicomponent signaling complex, anti-CD40 stimulated,(Birc2, Birc3, Cd40, Ikbkg, Map3k1, Traf2, Ube2n);;Mouse;Q62210,O08863,P27512,O88522,P53349,P39429,P61089;11797,11796,21939,16151,26401,22030,93765;MI:0006- anti bait coimmunoprecipitation;18635759;30.01.05.01.03,36.25.16.03.01,43.03.07.02.01.01,73.03.07.02.01.01;"With anti-MEKK1 as the immunoprecipitating antibody  it was shown that the apparent dissociation of the complex was not seen like in the anti-CD40 immunoprecipitated complexes,  where the amounts of most complex components declined between 10 and 30 min after stimulation.  The results indicate that MAPK signaling, at least by CD40 and other TNFRs, follows a two-stage mechanism based on assembly of a multiprotein complex at the receptor that primes MAP3Ks for activation, but in which kinase activation is delayed until the complex is released to the cytoplasm.";"";""
5743;Membrane-associated multicomponent signaling complex, anti-CD40 stimulated (Cd40, Ikbkg, Map3k1, Traf2, Ube2n);;Mouse;P27512,O88522,P53349,P39429,P61089;21939,16151,26401,22030,93765;MI:0006- anti bait coimmunoprecipitation;18635759;30.01.05.01.03,36.25.16.03.01,43.03.07.02.01.01,70.02,73.03.07.02.01.01;"The complex isolated with either CD40, IKK-gamma, or MEKK1-specific antibodies was present in the membrane-containing fraction at 10 min after stimulation but was barely detected after 30 min.";"";""
5744;Cytosolic multicomponent signaling complex, anti-CD40 stimulated, (Ikbkg, Map3k1, Traf2, Ube2n);;Mouse;O88522,P53349,P39429,P61089;16151,26401,22030,93765;MI:0006- anti bait coimmunoprecipitation;18635759;30.01.05.01.03,36.25.16.03.01,43.03.07.02.01.01,70.03,73.03.07.02.01.01;"This complex containing TRAF2, MEKK1, IKK-gamma, and Ubc13, but not CD40, was detected in the soluble cytosol fraction within 10 min, and most of its components were relatively stably associated for up to 60 min after CD40 engagement.";"";""
5745;PlexinA1-NRP1 complex;;Human;O14786,Q9UIW2;8829,5361;MI:0007- anti tag coimmunoprecipitation;10520994;30.05.02,40.01.03.03,47.03.01;"";"";""
5746;PlexinA1-NRP1-SEMA3A complex;;Human;O14786,Q9UIW2,Q14563;8829,5361,10371;MI:0007- anti tag coimmunoprecipitation;10520994;30.05.02,40.01.03.03,47.03.01;"Plexin A increases Neuropilin 1 affinity for SEMA3A. ";"";""
5747;2AR-mGluR2 complex;;Human;P08913,P42262;150,2891;MI:0006- anti bait coimmunoprecipitation;18297054;30.05.02.24,73.03.13,77.03.01.01.01;"The results are consistent with the hypothesis that the 2AR-mGluR2 complex integrates serotonin and glutamate signaling to regulate the sensory gating functions of the cortex, a process that is disrupted in psychosis.";"2AR-mGluR2 complex is involved in psychosis.";""
5748;2AR-mGluR2 complex;;Human;P08913,P42262;150,2891;MI:0007- anti tag coimmunoprecipitation | MI:0012- bioluminescence resonance energy transfer | MI:0055- fluorescent resonance energy transfer;18297054;30.05.02.24;"The results are consistent with the hypothesis that the 2AR-mGluR2 complex integrates serotonin and glutamate signalling to regulate the sensory gating functions of the cortex, a process that is disrupted in psychosis.";"2AR-mGluR2 complex is involved in psychosis.";""
5749;MRIT complex;;Human;Q07817,Q14790,O15519;598,841,8837;MI:0019- coimmunoprecipitation | MI:0047- far western blotting | MI:0018- two hybrid;9326610;40.10.02.02.02;"";"";""
5755;SUMO1-SUA1-UBA2 complex;;Human;Q9UBE0,P63165,Q9UBT2;10055,7341,10054;MI:0047- far western blotting;9920803;14.07.05,14.07.07;"Sua1p and hUba2p form a complex, and the complexed hUba2p binds SUMO-1.";"";""
5756;SUA1-UBA2 complex;;Human;Q9UBE0,Q9UBT2;10055,10054;MI:0047- far western blotting;9920803;18.02;"";"";""
5758;PLXNA2-RANBPM complex;;Human;O75051,Q96S59;5362,10048;MI:0007- anti tag coimmunoprecipitation;16672672;20.09.07.07,30.05.02,40.01.03.03;"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.";"";""
5759;PLXNA3-RANBPM complex;;Human;P51805,Q96S59;55558,10048;MI:0007- anti tag coimmunoprecipitation;16672672;20.09.07.07,30.05.02,40.01.03.03;"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.";"";""
5760;PLXNA4-RANBPM complex;;Human;Q9HCM2,Q96S59;91584,10048;MI:0007- anti tag coimmunoprecipitation;16672672;20.09.07.07,30.05.02,40.01.03.03;"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.";"";""
5762;CRMP-MICAL-PlexinA1 complex, induced by SEMA3A;;Human;Q14194,Q8TDZ2,Q9UIW2;1400,64780,5361;MI:0007- anti tag coimmunoprecipitation;18305261;30.05.02,40.01.03.03,47.03.01;"MIDCAL1 forms a SEMA3A-modulated complex with CRMP and PlexA proteins.";"";""
5770;RUNX1-CBF-beta-DNA complex;;Human;Q13951,Q01196;865,861;MI:0114- x-ray crystallography;11276260;11.02.03.04,16.03.01;"The heterodimeric complex between AML1 and CBF beta has an essential role in the ontogeny of definitive hematopoiesis and is the most frequent target for chromosomal rearrangements in human acute leukemias.";"The complex is involved in acute leukemias.";""
5791;PlexinA1-PlexinB1 complex;;Mouse;P70206,Q8CJH3;18844,235611;MI:0018- two hybrid | MI:0007- anti tag coimmunoprecipitation;12559962;30.05.01.12,41.05.16;"";"";""
5798;Death induced signaling complex II (FADD, CASP8, CFLAR), cytosolic, CD95L induced;;Human;Q14790,O15519,Q13158;841,8837,8772;MI:0006- anti bait coimmunoprecipitation;18635548;40.10.02.03.01;"In contrast to the caspase activation at the CD95 DISC reported to occur within seconds after stimulation, caspase activation in the cytosol took place hours after stimulation. This complex was found in all investigated cell lines:  SKW6.4, BJAB, Raji, HUT78 and J16. ";"";""
5799;Death induced signaling complex DISC (FAS, FADD, CASP8, CFLAR), membrane-associated, CD95L induced;;Human;Q14790,O15519,Q13158,P25445;841,8837,8772,355;MI:0006- anti bait coimmunoprecipitation;18635548;40.10.02.03.01;"The CD95 DISC is formed within seconds after CD95 stimulation, followed by caspase-8 activation at the DISC complex.";"";""
5800;Death-inducing signaling complex DISC (type I cells associated), stimulated;;Human;Q14790,Q13158,P25445;841,8772,355;MI:0006- anti bait coimmunoprecipitation;9501089;40.10.02.03,70.02;"The authors compared the formation of the DISC between typeI (SKW6.5, H9) and type II  (JUrkat, CEM) cells. In type I cells, induction of apoptosis was accompanied by activation of large amounts of caspase-8 by the death-inducing signaling complex (DISC), whereas in type II cells DISC formation was strongly reduced and activation of caspase-8 and caspase-3 occurred following the loss of mitochondrial transmembrane potential.";"";""
5805;PGAM5-KEAP1-NRF2 complex;;Human;Q14145,Q16236,Q96HS1;9817,4780,192111;MI:0006- anti bait coimmunoprecipitation;18387606;11.02.03.04,32.01.01,70.16.01;"The authors describe that PGAM5, by anchoring the Keap1-Nrf2 complex to outer membrane of mitochondria, may facilitate coordination between mitochondrial function and regulation of Nrf2-dependent anti-oxidant gene expression.    ";"";""
5806;Keap1-Nrf2-Cul3 complex;;Mouse;Q9JLV5,Q9Z2X8,Q60795;26554,50868,18024;MI:0029- cosedimentation through density gradients;17903176;14.13.01.01,32.01.01,70.03,77.03.11.07;"The authors propose that Cul3 regulates the Nrf2 turnover through forming the Keap1-Nrf2-Cul3 complex.";"";""
5807;Keap1-Nrf2 complex;;Mammalia;Q9Z2X8,Q60795;50868,18024;MI:0006- anti bait coimmunoprecipitation;17903176;14.13.01.01,32.01.01,70.03;"The authors described that the electrophilic stress does not disrupt the association of Keap1 and Nrf2, but rather it represses Keap1-mediated ubiquitination of Nrf2.";"";""
5808;DISC complex;;Mammalia;Q14790,Q8IUB6,Q13158;841,355,8772;MI:0019- coimmunoprecipitation;19347032;40.10.02.03.01;"This complex formation was induced by 5-FU.";"";""
5809;GABAA receptor ;;Human;P14867,P47870,P18507;2554,2561,2566;MI:0401- biochemical;11992121;20.01.01.07.09,20.03.01.01;"";"Epilepsy, juvenile mioclonic.";""
5811;p53-BCL2 complex;;Mammalia;P10415,P04637;596,7157;MI:0019- coimmunoprecipitation;12667443;40.10.02.03,70.16;"";"";""
5812;p53-BCL2 complex;;Mammalia;Q07817,P04637;598,7157;MI:0019- coimmunoprecipitation;12667443;40.10.02.03,70.16;"";"";""
5813;tBID-BAK1 complex;;Mouse;O08734,P70444;12018,12122;MI:0019- coimmunoprecipitation;12667443;40.10.02.03,70.16;"";"";""
5814;Tp53-BAK1 complex;;Mouse;O08734,P02340;12018,22059;MI:0019- coimmunoprecipitation;12667443;40.10.02.03,70.16;"";"";""
5815;Quaternary complex (Dvl, Gsk3b, Frat1, Axin1);;Mouse;O35625,P51141,P70339,Q9WV60;12005,13542,14296,56637;MI:0019- coimmunoprecipitation | MI:0096- pull down;10428961;30.05.02.20;"Dvl and GSK bind to different portions of Frat1.";"";""
5816;Apoptosome-procaspase 9 complex;;Human;O14727,P55211,P99999;317,842,54205;MI:0226- ion exchange chromatography;10692394;40.10.02.03,70.03;"";"";""
5817;tBID-BCL2 complex;;Mammalia;P10415,P55957;596,637;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;11583631;40.10.02.04,70.16.01;"";"";""
5818;BIM-BCL2 complex;;Mammalia;P10415,O43521;596,10018;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;11583631;40.10.02.04,70.16.01;"";"";""
5819;BIM-BCL2xL complex;;Mammalia;Q07817,O43521;598,10018;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;11583631;40.10.02.04,70.16.01;"";"";""
5820;tBID-BCL2xL complex;;Mammalia;Q07817,P55957;598,637;MI:0030- cross-linking studies | MI:0019- coimmunoprecipitation;11583631;40.10.02.04,70.16.01;"";"";""
5821;BAD-BCL2xL complex;;Mouse;Q61337,Q64373;12015,12048;MI:0030- cross-linking studies;12242151;40.10.02.04,70.16.01;"";"";""
5822;MCL1-NOXA complex;;Mammalia;Q07820,Q13794;4170,5366;MI:0096- pull down;16697956;40.10.02.04,70.16.01;"";"";""
5823;MCL1-BAK1 complex;;Human;Q16611,Q07820;578,4170;MI:0019- coimmunoprecipitation;15077116;40.10.02.04,70.16.01;"";"";""
5827;IKBKG tetramer complex;;Human;Q9Y6K9;8517;MI:0030- cross-linking studies;12612076;30.01.05.01.04;"Cross link agent EGS appears to cross-link preferentially the IKK-gamma subunits in the IKK-alpha-IKK-beta-IKK-gamma holocomplex.";"";""
5828;IKBKG-IKBKB  complex;;Human;O14920,Q9Y6K9;3551,8517;MI:0007- anti tag coimmunoprecipitation;12612076;30.01.05.01.04;"The tetrameric oligomerization is not required for binding of IKK-gamma to IKK-alpha or IKK-beta.";"";""
5829;IKBKG-CHUK complex;;Human;O15111,Q9Y6K9;1147,8517;MI:0007- anti tag coimmunoprecipitation;12612076;30.01.05.01.04;"The tetrameric oligomerization is not required for binding of IKK-gamma to IKK-alpha or IKK-beta.";"";""
5830;DJ-1-SNCA complex, high molecular weight complex;;Human;Q99497,P37840;11315,6622;MI:0006- anti bait coimmunoprecipitation | MI:0071- molecular sieving;15935068;77.03.01.01.01;"";"";""
5877;MAP2K1-BRAF-RAF1-YWHAE-KSR1 complex;;Human;P15056,Q8IVT5,Q02750,P04049,P62258;673,8844,5604,5894,7531;MI:0676- tandem affinity purification;17979178;30.01.05;"";"";""
5832;PINK1-MIRO2-Milton complex;;Human;Q9BXM7,Q8IXI1,Q9UPV9;65018,89941,22906;MI:0007- anti tag coimmunoprecipitation;19152501;20.09.07,70.16.01;"This complex is involved in anterograde axonal transport of mitochondria.";"";""
5836;MIRO2-Milton complex;;Human;Q8IXI1,Q9UPV9;89941,22906;MI:0007- anti tag coimmunoprecipitation;19152501;20.09.07,70.16.01;"This complex is involved in anterograde axonal transport of mitochondria.";"";""
5837;PPD complex;Parkin-PINK1-DJ1 complex;Human;O60260,Q99497,Q9BXM7;5071,11315,65018;MI:0019- coimmunoprecipitation | MI:0071- molecular sieving;19229105;14.13.01.01,70.03,77.03.01.01.01;"PPD complex plays an important role in degradation of un- or misfolded Parkin substrates, like Parkin itself or Synphilin-1. Usually the PPD complex is found in the cytoplasm, but a small ammount was also detected in the mitochondrial fraction.";"";""
5838;Heterotrimeric complex (Rnd1, Rras, Plxnb1);;Mammalia;Q8CJH3,Q8BLR7,P10833;235611,223881,20130;MI:0019- coimmunoprecipitation;15297673;16.01.01,18.02.01.01.01,30.05,34.07;"";"";""
5843;AIF-CYPA-DNA complex;;Human;O95831,P62937;9131,5478;MI:0096- pull down | MI:0019- coimmunoprecipitation;14716299;40.10.02.03,70.10;"After apoptotic stimulus, AIF translocates to the nucleus, interacts with DNA and tethers CypA to chromatin.";"";""
5844;I-kappa-B kinase (IKK) complex;;Human;O15111,O14920,Q9Y6K9;1147,3551,8517;MI:0007- anti tag coimmunoprecipitation;10893415;30.01.05.01.04;"The authors conclude that while IKK gamma is a stoichiometric component of the IKK complex, obligatory for NF-kappa B signaling, IKAP is not associated with IKKs and plays no specific role in cytokine-induced NF-kappa B activation.";"";""
5849;HSP90-CDC37-LRRK2 complex;;Human;Q16543,P08238,Q5S007;11140,3326,120892;MI:0676- tandem affinity purification;16321986;30.01.05.01;"HSP90 and CDC37 do not serve as substrate for LRRK2 kinase but associates as chaperones participating in maintenance of proper folding of the kinase.";"";""
5859;FAS-FADD-CASP8-CASP10 complex;;Human;Q92851,Q14790,Q13158,P25445;843,841,8772,355;MI:0055- fluorescent resonance energy transfer | MI:0006- anti bait coimmunoprecipitation;11717445;40.10.02;"Stimulation of Fas was induced by anti-Fas or by FasL. The FRET-results suggest that caspase-8 and -10 can be recruited likely within 50 Å, which would constitute the same Fas signaling complex. Caspase-10 is recruited into the Fas signaling complex and becomes activated like caspase-8 with slightly faster kinetics under these conditions. FRET signals showed pairs of of caspase-8 and -10 DEDs (death effector domains) with themselves and with each other, indicating a natural propensity of these domains to cause homotypic and heterotypic complexes.";"";""
5860;FAS-FADD-CASP8 complex;;Human;Q14790,Q13158,P25445;841,8772,355;MI:0055- fluorescent resonance energy transfer;11717445;40.10.02;"Stimulation of Fas was induced by anti-Fas or by FasL.  FRET signals showed pairs of of caspase-8 and -10 DEDs (death effector domains) with themselves and with each other, indicating a natural propensity of these domains to cause homotypic and heterotypic complexes.";"";""
5861;FAS-FADD-CASP10 complex;;Human;Q92851,Q13158,P25445;843,8772,355;MI:0055- fluorescent resonance energy transfer;11717445;40.10.02;"Stimulation of Fas was induced by anti-Fas or by FasL.  FRET signals showed pairs of of caspase-8 and -10 DEDs (death effector domains) with themselves and with each other, indicating a natural propensity of these domains to cause homotypic and heterotypic complexes.";"";""
5862;CAV1-VDAC1-ESR1 complex;;Human;Q03135,P03372,P21796;857,2099,7416;MI:0006- anti bait coimmunoprecipitation | MI:0663- confocal microscopy;19595769;20.03.01.01,70.02,73.03.13,77.03.01.01.01;"";"Disease: CAV1-VDAC1-ESR1 complex is involved in Alzheimer's disease.";""
5870;FE65-TSHZ3-HDAC1 complex;;Human;O00213,Q13547,Q63HK5;322,3065,57616;MI:0007- anti tag coimmunoprecipitation;19343227;11.02.03.04.03,70.10;"CASP4 appears to be one target for the repressor complex centering on FE65.";"Disease: TSHZ3 is involved in Alzheimer disease.";""
5871;Gamma-secretase complex (Aph1a, Psen1, Psenen, Ncstn);;Mouse;Q8BVF7,P57716,P49769,Q9CQR7;226548,59287,19164,66340;MI:0019- coimmunoprecipitation;17911105;14.07.11,30.01.05.03,30.05.02.14,70.02;"The results demonstrated that having one of each of the four subunits is sufficient for gamma-secretase complexes to bind and cleave substrates.";"Gamma-secretase complex is involved in Alzheimer disease.";""
5872;BRAF-MAP2K1-MAP2K2-YWHAE complex;;Human;P15056,Q02750,P36507,P62258;673,5604,5605,7531;MI:0676- tandem affinity purification;17979178;30.01.05;"";"";""
5873;RAF1-MAP2K1-YWHAE complex;;Human;Q02750,P04049,P62258;5604,5894,7531;MI:0676- tandem affinity purification;17979178;30.01.05;"";"";""
5876;PPP2R1A-PPP2R1B-PPP2CA-PPME1-EIF4A1 complex;;Human;P60842,Q9Y570,P67775,P30153,P30154;1973,51400,5515,5518,5519;MI:0676- tandem affinity purification;15761952;14.07.03,18.02.01.02.05;"";"";""
5879;Ksr1-PP2A holoenzyme complex (Ppp2r1a, Ppp2r2b, Ppp2ca), PDGF stimulated;;Mouse;Q61097,P63330,Q76MZ3,Q6ZWR4;16706,19052,51792,72930;MI:0006- anti bait coimmunoprecipitation;12932319;14.07.03,30.01.05.01.03,70.02;"The authors showed that the protein phosphatase PP2A is a component of the KSR1 scaffolding complex and demonstrated that PP2A activity is required for the stimulus-induced dephosphorylation of S392.  The binding of the regulatory B subunit (Ppp2r2b) was dramatically increased by PDGF treatment. The data indicate that the PP2A core enzyme is a constitutive component of the KSR1 complex, whereas the regulatory B subunit interaction is induced by Ras pathway activation.";"";""
5880;Ksr1-PP2A core enzyme complex (Ppp2r1a, Ppp2ca), untreated;;Mouse;Q61097,P63330,Q76MZ3;16706,19052,51792;MI:0006- anti bait coimmunoprecipitation;12932319;14.07.03,30.01.05.01.03;"The data indicate that the PP2A core enzyme is a constitutive component of the KSR1 complex, whereas the regulatory B (Ppp2r2b) subunit interaction is induced by Ras pathway activation.";"";""
5881;Ksr1-PP2A core enzyme complex (Ppp2r1a, Ppp2ca), untreated;;Mouse;Q61097,P63330,Q76MZ3;16706,19052,51792;MI:0006- anti bait coimmunoprecipitation;12932319;14.07.03,30.01.05.01.03,70.03,77.03.01.01.01;"The A and C core subunits were readily detected in the KSR1 immunoprecipitates from brain lysates, but much lower levels of the B subunit were observed. The data indicate that the PP2A core enzyme is a constitutive component of the KSR1 complex, whereas the regulatory B (Ppp2r2b) subunit interaction is induced by Ras pathway activation.";"";""
5882;Raf1-PP2A holoenzyme complex (Ppp2r1a, Ppp2r2b, Ppp2ca), PDGF stimulated;;Mouse;P63330,Q76MZ3,Q6ZWR4,Q99N57;19052,51792,72930,110157;MI:0096- pull down;12932319;14.07.03,30.01.05.01.03,70.02;"Studies indicate that PP2A contributes to Raf-1 activation by dephosphorylating S259 (PMID: 11782426) The examination of the PP2A/Raf-1 interaction by immunoblot analysis revealed that, like KSR1, the association of the dimeric core subunits (A and C) was constitutive, whereas binding of the regulatory B subunit was significantly induced by growth factor treatment.";"";""
5883;Raf1-PP2A core enzyme complex (Ppp2r1a, Ppp2ca), untreated;;Mouse;P63330,Q76MZ3,Q99N57;19052,51792,110157;MI:0096- pull down;12932319;14.07.03,30.01.05.01.03,70.03;"The examination of the PP2A/Raf-1 interaction by immunoblot analysis revealed that, like KSR1, the association of the dimeric core subunits (A and C) was constitutive, whereas binding of the regulatory B subunit was significantly induced by growth factor treatment.";"";""
5886;Ksr1 complex (Ksr1, Mek, 14-3-3), unstimulated;;Mouse;Q61097,(P31938,Q63932),(O70456,Q9CQV8,P62259,P61982,P68510,P68254,P63101);16706,(26395,26396),(55948,54401,22627,22628,22629,22630,22631);MI:0007- anti tag coimmunoprecipitation;11741534;14.07.03,30.01.05.01.03,70.03;"The amount of 14-3-3 bound to WT KSR1 did not change in response to EGF treatment, consistent with previous findings that the interaction with both Ser-297 and Ser-392 must be disrupted to reduce 14-3-3 dimer binding to KSR1. Even though MAPK was not observed in KSR1 immunoprecipitates from untreated cells, low levels of MAPK were detected in S392A and S297A/S392A mutant samples. The constitutive interaction between KSR1 and MEK is not affected by mutation of the serine sites.";"";""
5909;Ksr1 complex (Ksr1, Mek, 14-3-3, Mapk), EGF stimulated;;Mouse;Q61097,P63085,(P31938,Q63932),(O70456,Q9CQV8,P62259,P61982,P68510,P68254,P63101);16706,26413,(26395,26396),(55948,54401,22627,22628,22629,22630,22631);MI:0007- anti tag coimmunoprecipitation;11741534;14.07.03,30.01.05.01.03,70.02;"The amount of 14-3-3 bound to WT KSR1 did not change in response to EGF treatment, consistent with previous findings that the interaction with both Ser-297 and Ser-392 must be disrupted to reduce 14-3-3 dimer binding to KSR1. Even though MAPK was not observed in KSR1 immunoprecipitates from untreated cells, low levels of MAPK were detected in S392A and S297A/S392A mutant samples. The constitutive interaction between KSR1 and MEK is not affected by mutation of the serine sites.";"";""
5899;Lebercilin complex (Lca5, Ncl, Npm1, Ywhae, HSPA1A/B, Dctn1, Dctn2);;Pig;O08788,Q99KJ8,Q80ST9,P09405,Q61937,P62259,(P34930,Q6S4N2);13191,69654,75782,17975,18148,22627,(0,396648);MI:0006- anti bait coimmunoprecipitation;17546029;70.04.05,77.03.02.02;"The results showed that lebercilin is a ciliary and microtubule-associated protein.";"Lca5 is involved in Leber congenital amaurosis.";"Since Lca5, Ncl, Npm1, Ywhae, Dctn2 and Dctn1 from pig were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
5910;Ksr1-CK2 complex;;Mouse;Q60737,O54833,P67871,Q61097;12995,13000,13001,16706;MI:0006- anti bait coimmunoprecipitation;17174095;14.07.03,30.01.05.01.03,70.02,77.03.01.01.01;"The authors showed that binding of the CK2 subunits to Ksr1 was found to be constitutive and did not change with growth-factor treatment. The results identify CK2 as a novel component of the KSR1 scaffolding complex that facilitates ERK cascade signaling by functioning as a Raf family N-Region kinase.";"";""
5915;Ksr1-Brap (IMP) complex;;Rat;Q99MP8,Q61097;72399,16706;MI:0006- anti bait coimmunoprecipitation;14724641;30.01.05.01.03;"";"";"Since Ksr1 and Brap from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used."
5918;KSR1 homooligomer complex;;Human;Q8IVT5;8844;MI:0007- anti tag coimmunoprecipitation;18332145;30.01.05.01.03;"The authors found that KSR1 homo-oligomerization is required to couple distinct KSR·MEK and KSR·B-Raf complexes to allow MEK activation. IMP (the Ras effector and ubiquitin-protein isopeptide ligase family member) association blocks KSR1 homo-oligomerization.";"";""
5919;BRAF-RAF1-14-3-3 complex;;Human;P15056,P04049,(P31947,P31946,P62258,P61981,Q04917,P27348,P63104);673,5894,(2810,7529,7531,7532,7533,10971,7534);MI:0007- anti tag coimmunoprecipitation;18332145;30.01.05.01.03;"Expression of IMP (Ras effector and ubiquitin-protein isopeptide ligase family member)  blocked BRAF-RAF1 complex formation. Although 14-3-3 association has been implicated as a prerequisite for B-Raf·c-Raf complex formation, IMP impaired Raf hetero-oligomerization without affecting the relative amounts of 14-3-3 coprecipitating with B-Raf.";"";""
5920;KSR1-RAF1-MEK complex;;Human;Q8IVT5,P04049,(Q02750,P36507);8844,5894,(5604,5605);MI:0007- anti tag coimmunoprecipitation;18332145;30.01.05.01.03;"IMP (Ras effector and ubiquitin-protein isopeptide ligase family member)  significantly inhibited the association of c-Raf with KSR1. This is in stark contrast to the insensitivity of KSR1·B-Raf complexes to IMP expression.";"";""
5921;KSR1-BRAF-MEK complex;;Human;P15056,Q8IVT5,(Q02750,P36507);673,8844,(5604,5605);MI:0007- anti tag coimmunoprecipitation;18332145;30.01.05.01.03;"IMP (Ras effector and ubiquitin-protein isopeptide ligase family member)  significantly inhibited the association of c-Raf with KSR1. This is in stark contrast to the insensitivity of KSR1·B-Raf complexes to IMP expression.";"";""
5922;RAF1-RAS complex, EGF induced;;Human;P04049,(P01112,P01116,P01111);5894,(3265,3845,4893);MI:0006- anti bait coimmunoprecipitation;16364920;30.01.05,70.02;"The authors showed that whereas EGF induces complex formation between RAS and C-RAF, and (G12V)RAS binds directly to C-RAF, a RAS:C-RAF complex is not induced by the impaired activity mutants of B-RAF or by (V600E)B-RAF.";"";""
5923;RAF1-BRAF complex, RAS stimulated;;Human;P15056,P04049;673,5894;MI:0007- anti tag coimmunoprecipitation;16364920;30.01.05;"The authors found that C-RAF binds to B-RAF only under activating conditions, whereas mutant B-RAF binds to C-RAF constitutively. Additionally they showed that wild-type B-RAF can also activate C-RAF, but that C-RAF does not activate B-RAF.";"";""
5924;RAF1-CNK1 complex, RAS stimulated;;Human;Q969H4,P04049;10256,5894;MI:0007- anti tag coimmunoprecipitation;15845549;30.01.05;"The authors described that the interaction between the wild-type proteins of Raf and CNK was detectable but weak. Further they showed that coexpression of activated RasV12 enhanced the association between the two proteins, indicating that Raf-1 preactivated by RasV12 undergoes a conformational change that improves its binding to CNK1.";"";""
5925;BRAF-CNK1 complex, not RAS stimulated;;Human;P15056,Q969H4;673,10256;MI:0007- anti tag coimmunoprecipitation;15845549;30.01.05;"The authors showed that in contrast to Raf-1, B-Raf bound to CNK1 without the coexpression of activated Ras.";"";""
5926;CNK1 homodimer complex;;Human;Q969H4;10256;MI:0007- anti tag coimmunoprecipitation;15845549;30.01.05;"The authors showed that coexpression of activators of the MAP kinase pathway such as RasV12 or the constitutively active MEK mutant MEK-Glu-217/Glu-221  strongly induced dimerization of the CNK proteins. ";"";""
5928;CNK1-SRC-RAF1 complex;;Human;Q969H4,P04049,P12931;10256,5894,6714;MI:0007- anti tag coimmunoprecipitation;15845549;30.01.05;"The results indicated that CNK1 regulates the Src-dependent activation of Raf-1 only under optimized conditions. Too low or too high amounts of CNK1 prevented the formation of the trimeric complex and promoted dimerization between CNK1 and Src or Raf-1, thereby preventing activation of Raf-1 by Src. The authors describe that CNK1 acts as a scaffold protein that assembles and coordinates two kinases of a single signaling pathway.";"";""
5936;Ksr1-CK2-MEK-14-3-3 complex, PDGF treated;;Mouse;Q60737,O54833,P67871,Q61097,(P31938,Q63932),(Q9CQV8,P62259,P61982,P68510,P68254,P63101);12995,13000,13001,16706,(26395,26396),(54401,22627,22628,22629,22630,22631);MI:0007- anti tag coimmunoprecipitation;17174095;14.07.03,30.01.05.01.03,70.02,77.03.01.01.01;"The authors showed that mutation of lysine 360 and arginine 363 to either alanine residues (KR/AA) or to glutamine and glycine residues KR/QG (as found in the C-Raf C1 domain) abolished CK2 binding but had no effect on the association of MEK and 14-3-3, proteins that bind to sites outside the C1 domain.";"";""
5937;B-Ksr1-MEK-MAPK-14-3-3 complex;;Mouse;Q61097,P63085,(P31938,Q63932),(Q9CQV8,P62259,P61982,P68510,P68254,P63101);16706,26413,(26395,26396),(54401,22627,22628,22629,22630,22631);MI:0006- anti bait coimmunoprecipitation;10891492;30.01.05.01.03,41.05.13,73.03.13,77.03.01.01.01;"Experiments done in RASV12 activated 293 cells and in lysates of mouse brain.";"";"B-Ksr1, (corresponding to isoform 2 in Swiss-Prot: Q61097) is a splice variant that is highly expressed in brain-derived tissues."
5946;Ksr1-Mek-Braf complex, EGF induced;;Mouse;P28028,Q61097,(P31938,Q63932);109880,16706,(26395,26396);MI:0007- anti tag coimmunoprecipitation;19541618;30.01.05.01.03;"The authors conclude that ternary interactions between KSR1, MEK, and B-Raf facilitate signal transmission from B-Raf to MEK.";"";""
5947;Ksr1-Mek-Braf-Erk complex, EGF induced;;Mouse;P28028,Q61097,(P31938,Q63932),(P63085,Q63844);109880,16706,(26395,26396),(26413,26417);MI:0007- anti tag coimmunoprecipitation;19541618;30.01.05.01.03;"The authors found that the docking of activated ERK to the KSR1 complex accelerates the phosphorylation of these sites in response to growth factor treatment. As a functional consequence, phosphorylation of B-Raf and KSR1 on the S/TP sites disrupts the B-Raf/KSR1 interaction and promotes the release of KSR1 from the plasma membrane. Thus, the docking of activated ERK downregulates KSR1's scaffold activity and its ability to potentiate signal transmission from B-Raf to MEK.  ";"";""
5948;p18-p14-Mp1 complex;;Mouse;Q9CQ22,O88653,Q9JHS3;0,0,0;MI:0676- tandem affinity purification;19177150;20.09.13,30.01.05.01.03,42.22,70.22;"Experiments were done in mouse embryonic fibroblasts (MEFs). The authors showed that p18 specifically binds to the p14-MP1 complex, a scaffold for MEK1. Further results indicated that p18 serves as a functional component of the MEK-ERK pathway by anchoring the p14-MP1-MEK complex to late endosomes.";"";""
5951;Mp1-p14 scaffolding complex;;Mammalia;Q9UHA4,Q9JHS3;0,0;MI:0114- x-ray crystallography;15016825;30.01.05.01.03,70.22;"The authors describe that an intact and correctly localized MP1-p14 complex is required for MAPK signaling.";"";""
5952;Mp1-p14 scaffolding complex;;Mouse;O88653,Q9JHS3;0,0;MI:0114- x-ray crystallography | MI:0004- affinity chromatography technologies | MI:0071- molecular sieving;15263099;30.01.05.01.03,70.22;"The authors describe that p14/MP1 acts as a MAPK-scaffolding complex anchored to late endosomes.";"";""
5960;p65-p50 Nf(kappa)B complex, Il-1-beta induced;;Mouse;P25799,Q04207;0,0;MI:0412- electrophoretic mobility supershift assay;16551748;30.01.05.01.04;"";"";""
5963;ALB-TGFbetaRII complex;;Rat;P02770,P38438;0,0;MI:0019- coimmunoprecipitation;19605630;30.05.01.18.01;"";"OMIM:600669 Epilepsy, idopathic generalized, susceptibility to";""
5980;LRRK2-CHIP-HSP90 complex;;Human;P08238,Q5S007,Q9UNE7;0,0,0;MI:0007- anti tag coimmunoprecipitation;19196961;14.13.01.01;"";"LRRK2 is involved in Parkinson disease.";""
5991;LRRK2-FADD-CASP8;;Human;Q14790,Q13158,Q5S007;0,0,0;MI:0019- coimmunoprecipitation;19176810;40.10.02.03;"";"";""
6023;Calcineurin;;Human;Q08209,P63098;0,0;MI:0114- x-ray crystallography;8524402;30.01.09.03;"";"";""
6025;UBC13-UEV1a complex;;Human;P61088,Q13404;0,0;MI:0004- affinity chromatography technologies;11057907;14.07.05;"";"";""
6036;PARK2-EPS15-EGFR;;Human;P00533,P42566,O60260;0,0,0;MI:0007- anti tag coimmunoprecipitation;16862145;20.09.13,30.05.01.12.01;"";"";""
6037;CHIP-HSC70 complex;;Human;P11142,Q9UNE7;0,0;MI:0019- coimmunoprecipitation;14612456;14.07.05,14.13.01.01;"";"CHIP-Hsc70 complex ubiquitinates phosphorylated Tau and enhances cell survival by decreasing the toxicity of hyperphosphorylated tau, a important factor in the neurofibrillary pathology of Alzheimer disease, via proteasomal degradation.";""
6038;dynein complex;;Mammalia;O14576,(Q14204,Q8NCM8),(Q9Y6G9,O43237,Q8TCX1),(P63167,Q96FJ2);0,(0,0),(0,0,0),(0,0);MI:0096- pull down;17403682;20.09.14;"";"";""
6039;dynein-dynactin complex;;Mammalia;Q14203,O14576,(Q14204,Q8NCM8),(Q9Y6G9,O43237,Q8TCX1),(P63167,Q96FJ2);0,0,(0,0),(0,0,0),(0,0);MI:0096- pull down;17403682;20.09.14;"";"";""
6041;DISC-FEZ1 complex;;Human;Q9NRI5,Q99689;0,0;MI:0018- two hybrid;12874605;40.01;"";"OMIM: 181500 Schizophrenia";""
6042;;;null;Q86X06,Q9Y250;0,0;MI:0018- two hybrid;16484223;;"";"";""
6043;DISC-FEZ1-F-actin complex;;Human;Q6PJ43,Q9NRI5,Q99689;0,0,0;MI:0019- coimmunoprecipitation;12874605;40.01;"";"OMIM: 181500 Schizophrenia";""
6045;;;Human;Q9NRI5,Q15049;0,0;MI:0018- two hybrid;14623284;;"";"";""
6046;;;Human;Q9NRI5,Q07343;0,0;MI:0018- two hybrid;14623284;;"";"";""
6048;dynein-dynactin complex;;Mouse;O08788,Q99KJ8,O88485;0,0,0;MI:0029- cosedimentation through density gradients;18094236;20.09.14;"";"";""
6049;Ncstn-Psen1 complex;;Mouse;P57716,P49769;0,0;MI:0019- coimmunoprecipitation | MI:0047- far western blotting;12603837;14.07.11,18.02.01.01.03,30.01.05.03,70.02,70.08;"The nicastrin-presenilin1 complex affects activity of gamma-secretase and is localized to the trans-Golgi network.";"Presenilins are catalytic components of gamma-secretase, the protease responsible for generating the Alzheimer's amyloid beta peptides.";""
6052;BAG3-HSC70-HSPB8-CHIP complex;;Human;O95817,P11142,Q9UJY1,Q9UNE7;0,0,0,0;MI:0007- anti tag coimmunoprecipitation;20060297;14.01,32.01;"The BAG3-HSC70-HSPB8-CHIP complex facilitates the degradation of damaged components, such as filamin, through chaperone-assisted selective autophagy (CASA).";"";""
6053;LKB1-STRAD-MO25 complex;;Human;Q9Y376,Q15831,Q7RTN6;0,0,0;MI:0114- x-ray crystallography;19892943;14.07.03,18.01.01;"";"Loss-of-function mutations in the tumor suppressor LKB1 cause the rare inherited disease Peutz-Jeghers syndrome (PJS) in humans and are associated with various sporadic cancers, in particular non–small cell lung cancer.";""
6056;null;;Mammalia;P05067,O75509;0,0;MI:0096- pull down | MI:0019- coimmunoprecipitation;19225519;;"interaction";"";""
6060;DISC1-ZNF365;;Human;;;MI:0018- two hybrid;19191256;;"";"";""
6061;DISC1-ZNF365 complex;;Human;Q9NRI5,Q70YC5;0,0;MI:0018- two hybrid;19191256;41.05.13;"";"";""
6062;DISC1-IMMT complex;;Mouse;Q811T9,Q8CAQ8;0,0;MI:0019- coimmunoprecipitation;20880836;;"";"";""
6066;Xanthine oxidase;;Human;P47989;0;MI:0071- molecular sieving;1627588;01.03.01.01;"";"";""
6067;ESR1-SP1 complex;;Human;P03372,P08047;0,0;MI:0045- experimental;10681512;;"";"";""
6068;ESR1-CEBPB complex;;Human;P17676,P03372;0,0;MI:0045- experimental;18852215;;"";"";""
6069;ESR1-GRIP1 complex;;Human;P03372,Q9Y3R0;0,0;MI:0045- experimental;10611355;;"";"";""
6072;TRA2B1-SRp30c-SRp55 complex;;Human;Q13247,Q13242,P62995;0,0,0;MI:0019- coimmunoprecipitation;15695522;11.04.03.01.10;"SRp30c is also known as SRSF9, and SRp55 as SRSF6.";"To confirm that the three factors can act as a complex, co-immunoprecipitations of the three proteins were done. It could be shown that htra2beta1 (a variant of TRA2B) interacts with SRp55 and that SRp30c interacts with both SRp55 and htra2beta1. ";"TRA2B1 variant was used-"
6073;SRp30c-SRp55 complex;;Human;Q13247,Q13242;0,0;MI:0019- coimmunoprecipitation;15695522;11.04.03.01.10;"";"Tau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c-SRp55 complex that either recruits or antagonizes htra2beta1 (a variant of TRA2B).";""