MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. EMBO Rep. (1469-221X) 2006 imex curation Yang Q., Kim YS., Lin Y., Lewis J., Neckers L., Liu ZG. 2009-01-08 Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Yang Q., Kim YS., Lin Y., Lewis J., Neckers L., Liu ZG. EMBO Rep. (1469-221X) 2006 2009-01-08 Only protein-protein interactions imex curation Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. EMBO Rep. (1469-221X) 2006 imex curation Yang Q., Kim YS., Lin Y., Lewis J., Neckers L., Liu ZG. 2009-01-08 Only protein-protein interactions mouse-3t3 Mus musculus embryo cells 3t3 Mouse embryo fibroblast cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Yang Q., Kim YS., Lin Y., Lewis J., Neckers L., Liu ZG. EMBO Rep. (1469-221X) 2006 2009-01-08 Only protein-protein interactions imex curation Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. EMBO Rep. (1469-221X) 2006 imex curation Yang Q., Kim YS., Lin Y., Lewis J., Neckers L., Liu ZG. 2009-01-08 Only protein-protein interactions mouse-3t3 Mus musculus embryo cells 3t3 Mouse embryo fibroblast cells imaging technique imaging technique microscopy experimental particp experimental participant identification experimental particp Yang Q., Kim YS., Lin Y., Lewis J., Neckers L., Liu ZG. EMBO Rep. (1469-221X) 2006 2009-01-08 Only protein-protein interactions imex curation calx_mouse Calnexin Canx protein protein mouse Mus musculus Mouse MEGKWLLCLLLVLGTAAVEAHDGHDDDAIDIEDDLDDVIEEVEDSKSKSDASTPPSPKVTYKAPVPTGEVYFADSFDRGSLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTAELSLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIADPDAVKPDDWDEDAPSKIPDEEATKPEGWLDDEPEYIPDPDAEKPEDWDEDMDGEWEAPQIANPKCESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFKMTPFSAIGLELWSMTSDIFFDNFIISGDRRVVDDWANDGWGLKKAADGAAEPGVVLQMLEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQSNAMEYKKTDAPQPDVKDEEGKEEEKNKRDEEEEEEKLEEKQKSDAEEDGVTGSQDEEDSKPKAEEDEILNRSPRNRKPRRE 0D9F8FE03434BADC ripk1_mouse Receptor-interacting serine/threonine-protein kinase 1 Cell death protein RIP Receptor-interacting protein 1 Ripk1 Rinp Rip protein protein mouse Mus musculus Mouse MQPDMSLDNIKMASSDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEFRPFYLSHFEEYVEEDVASLKKEYPDQSPVLQRMFSLQHDCVPLPPSRSNSEQPGSLHSSQGLQMGPVEESWFSSSPEYPQDENDRSVQAKLQEEASYHAFGIFAEKQTKPQPRQNEAYNREEERKRRVSHDPFAQQRARENIKSAGARGHSDPSTTSRGIAVQQLSWPATQTVWNNGLYNQHGFGTTGTGVWYPPNLSQMYSTYKTPVPETNIPGSTPTMPYFSGPVADDLIKYTIFNSSGIQIGNHNYMDVGLNSQPPNNTCKEESTSRHQAIFDNTTSLTDEHLNPIRENLGRQWKNCARKLGFTESQIDEIDHDYERDGLKEKVYQMLQKWLMREGTKGATVGKLAQALHQCCRIDLLNHLIRASQS DIP protein Q60855 original sequence version: 85 DIP protein Q60855 original sequence version: 109 DIP protein Q60855 original sequence version: 152 DIP protein Q60855 original sequence version: 130 DIP protein Q60855 original sequence version: 84 DIP protein Q60855 original sequence version: 123 DIP protein Q60855 original sequence version: 158 ABB350B523879933 tnr1a_mouse Tumor necrosis factor receptor superfamily member 1A p60 Tumor necrosis factor receptor 1 Tumor necrosis factor receptor type I p55 Tnfrsf1a Tnfr1 Tnfr-1 protein protein mouse Mus musculus Mouse MGLPTVPGLLLSLVLLALLMGIHPSGVTGLVPSLGDREKRDSLCPQGKYVHSKNNSICCTKCHKGTYLVSDCPSPGRDTVCRECEKGTFTASQNYLRQCLSCKTCRKEMSQVEISPCQADKDTVCGCKENQFQRYLSETHFQCVDCSPCFNGTVTIPCKETQNTVCNCHAGFFLRESECVPCSHCKKNEECMKLCLPPPLANVTNPQDSGTAVLLPLVILLGLCLLSFIFISLMCRYPRWRPEVYSIICRDPVPVKEEKAGKPLTPAPSPAFSPTSGFNPTLGFSTPGFSSPVSSTPISPIFGPSNWHFMPPVSEVVPTQGADPLLYESLCSVPAPTSVQKWEDSAHPQRPDNADLAILYAVVDGVPPARWKEFMRFMGLSEHEIERLEMQNGRCLREAQYSMLEAWRRRTPRHEDTLEVVGLVLSKMNLAGCLENILEALRNPAPSSTTRLPR DIP protein P25118 original sequence version: 102 DIP protein P25118 original sequence version: 93 DIP protein P25118 original sequence version: 158 0710C2E8C3C2B6D9 ern1_mouse Serine/threonine-protein kinase/endoribonuclease IRE1 Ern1 Ire1 Endoplasmic reticulum-to-nucleus signaling 1 Inositol-requiring protein 1 Ire1-alpha protein protein mouse Mus musculus Mouse MPARWLLLLLALLLPPPGPGSFGRTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGGKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQGEVLRKVVHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDLKFDPGLKGKSKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKRSFEEVINIVGQTSDNTPTTVSQDVEEKLARAPAKPEAPVDSMLKDMATIILSTFLLVGWVAFIITYPLSVHQQRQLQHQQFQKELEKIQLLQQQQLPFHPHGDLTQDPEFLDSSGPFSESSGTSSPSPSPRASNHSLHPSSSASRAGTSPSLEQDDEDEETRMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKDNPTYTVDIFSAGCVFYYVISEGNHPFGKSLQRQANILLGACNLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKEALDGPIVRQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPVEVQETLGSIPDDFVRYFTSRFPHLLSHTYQAMELCRHERLFQTYYWHEPTEPQPPVIPYAL 216E3E2FA2FF3F70 canx-tnfrsf1a 3 6 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 4 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 colocalization colocalization F4C EMBO-Reports As shown in Fig 4C, there is a small amount of TNFR1 localized at ER before Tg treatment. But the level of TNFR1 at ER is markedly increased after Tg treatment. homomint mint tnfrsf1a-ern1 2 6 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 7 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association F4D EMBO-Reports Both RIP and IRE1a were coprecipitatedwith TNFR1 in response to Tg treatment, indicating that TNFR1, IRE1a and RIP might form a complex in cells under ER stress. homomint mint tnfrsf1a-ripk1-5 2 6 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association F4D EMBO-Reports Both RIP and IRE1a were coprecipitatedwith TNFR1 in response to Tg treatment, indicating that TNFR1, IRE1a and RIP might form a complex in cells under ER stress. homomint mint tnfrsf1a-ern1-1 1 7 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell flag tagged flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell gfp tagged gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 physical association physical association F4B EMBO-Reports As it is known that IRE1a interacts with TRAF2 and that TRAF2 is a key effector of TNFR1 signalling, we performed similar co-immunoprecipitation experiments in TRAF2-/- fibroblast cells to rule out the possibility that the interaction between IRE1a and TNFR1 is mediated by TRAF2, and similar results to those in Fig 4B were obtained with traf2-/- cells homomint mint