IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ shatnyeva-2011-3 Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. human-skw6.4 Human B-lymphoblastoid EBV-transformed cell line skw6.4 Human B-lymphoblastoid EBV-transformed cell line anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de PLoS ONE 2011 Only protein-protein interactions imex curation shatnyeva-2011-1 Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de PLoS ONE 2011 Only protein-protein interactions imex curation shatnyeva-2011-2 Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. human-hut78 Homo sapiens HUT-78 T cell lymphoma hut78 HUT-78 human T cell lymphoma anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de PLoS ONE 2011 Only protein-protein interactions imex curation o15519-pro_0000004678 CASP8 and FADD-like apoptosis regulator subunit p43 CFLAR CASH CASP8AP1 CLARP MRIT Caspase homolog Caspase-eight-related protein Caspase-like apoptosis regulatory protein Cellular FLICE-like inhibitory protein FADD-like antiapoptotic molecule 1 Inhibitor of FLICE MACH-related inducer of toxicity Usurpin protein protein human Homo sapiens Human MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQSVYGVDQTHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVD 1 376 tnr6_human Tumor necrosis factor receptor superfamily member 6 FASLG receptor Apoptosis-mediating surface antigen FAS Apo-1 antigen FAS APT1 TNFRSF6 FAS1 protein protein human Homo sapiens Human MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV casp8_human Caspase-8 CASP8 MCH5 ICE-like apoptotic protease 5 MORT1-associated ced-3 homolog FADD-homologous ICE/ced-3-like protease FADD-like ICE Apoptotic cysteine protease Apoptotic protease Mch-5 CAP4 protein protein human Homo sapiens Human MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD fadd_human FAS-associated death domain protein FAS-associating death domain-containing protein Mediator of receptor induced toxicity FADD MORT1 GIG3 Growth-inhibiting gene 3 protein protein protein human Homo sapiens Human MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS q14790-pro_0000004629 Caspase-8 subunit p18 CASP8 MCH5 Apoptotic cysteine protease Apoptotic protease Mch-5 CAP4 FADD-homologous ICE/ced-3-like protease FADD-like ICE ICE-like apoptotic protease 5 MORT1-associated ced-3 homolog protein protein human Homo sapiens Human SESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETD 217 374 fas-casp8-11 1189290 n/a 1189293 unspecified role unspecified role prey prey n/a 1189294 unspecified role unspecified role bait bait n/a 1189295 unspecified role unspecified role prey prey association association false false false 6b and S5a These three protein plus FADD form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. The presence of CASP8 and cflar (FLIP) processed fragments was decreased upon Vibrio cholerae sialidase (VCN, reduces glycosilation of fas by cutting sialic acid unions) treatment (fig. 6b). The presence of cflar processed fragment was decreased upon treatment with tunicamycin (inhibits fas glycosylation at the ER level, fig. S5a). fas-casp8-8 1189290 n/a 1189295 unspecified role unspecified role prey prey n/a 1189296 unspecified role unspecified role prey prey n/a 1189294 unspecified role unspecified role bait bait association association false false false 7a These three protein plus FLIP form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. The presence of the p43/p41 fragment of casp8 and of fadd was disrupted when the mannosidase inhibitor DMM (causes inmature glycosylation of fas) was used. fas-casp8-10 1189291 n/a 1189297 unspecified role unspecified role prey prey n/a 1189295 unspecified role unspecified role prey prey n/a 1189296 unspecified role unspecified role prey prey n/a 1189294 unspecified role unspecified role bait bait association association false false false 5c These three protein plus FLIP form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. fas-casp8-12 1189292 n/a 1189293 unspecified role unspecified role prey prey n/a 1189294 unspecified role unspecified role bait bait n/a 1189295 unspecified role unspecified role prey prey association association false false false 6b and S5a These three protein plus FADD form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. The presence of CASP8 and cflar (FLIP) processed fragments was decreased upon Vibrio cholerae sialidase (VCN, reduces glycosilation of fas by cutting sialic acid unions) treatment (fig. 6b). The presence of cflar processed fragment was decreased upon treatment with tunicamycin (inhibits fas glycosylation at the ER level, fig. S5a).