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 http://mint.bio.uniroma2.it/mint ali-2011-2 Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response. in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Ali MM., Bagratuni T., Davenport EL., Nowak PR., Silva-Santisteban MC., Hardcastle A., McAndrews C., Rowlands MG., Morgan GJ., Aherne W., Collins I., Davies FE., Pearl LH. maruf.ali@imperial.ac.uk EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation ali-2011-1 Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ali MM., Bagratuni T., Davenport EL., Nowak PR., Silva-Santisteban MC., Hardcastle A., McAndrews C., Rowlands MG., Morgan GJ., Aherne W., Collins I., Davies FE., Pearl LH. maruf.ali@imperial.ac.uk EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation ern1_human Serine/threonine-protein kinase/endoribonuclease IRE1 ERN1 Inositol-requiring protein 1 Ire1-alpha Endoplasmic reticulum-to-nucleus signaling 1 IRE1 protein protein human Homo sapiens Human MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL s2 RRRLSFAEPG peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RRRLSFAEPG mint ern1-1 1022991 ern1_human Ire1 alpha 1022993 western blot western blot Immuno blot Immuno blot self self self self purified purified phosphorylated phosphorylated residue phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) western blot western blot Immuno blot Immuno blot certain certain sequence position certain certain certain sequence position certain false resulting-ptm phosphorylation phosphorylation reaction phosphorylation false true false mint f2b f4a f4b true ern1-s2 1022991 s2 S2 1022994 peptide synthesis peptide synthesis enzyme target enzyme target substrate substrate neutral component neutral component purified purified biotin tag biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ern1_human Ire1 alpha 1022993 predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified phosphorylation phosphorylation reaction phosphorylation false false false f4e mint ern1-1 1022992 ern1_human Ire1 alpha 1022993 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false mint f1 f2a t1