DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. Only protein-protein interactions crigr Cricetulus griseus (Chinese hamster) Cricetulus barabensis griseus Chinese hamster anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. DIP original experiment: DIP-263838X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. DIP original experiment: DIP-263836X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. DIP original experiment: DIP-263834X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. DIP original experiment: DIP-263837X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zhou J., Liu CY., Back SH., Clark RL., Peisach D., Xu Z., Kaufman RJ. DIP original experiment: DIP-263835X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. e2ak3_mouse Eukaryotic translation initiation factor 2-alpha kinase 3 Eif2ak3 Pek Perk PRKR-like endoplasmic reticulum kinase Pancreatic eIF2-alpha kinase protein protein mouse Mus musculus Mouse MERATRPGPRALLLLLFLLLGCAAGISAVAPARSLLAPASETVFGLGAAAAPTSAARVPAVATAEVTVEDAEALPAAAGEPESRATEPDDDVELRPRGRSLVIISTLDGRIAALDAENDGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGDLFQWDRDRESMEAVPFTVESLLESSYKFGDDVVLVGGKSLITYGLSAYSGKLRYICSALGCRRWDSDEMEEEEDILLLQRTQKTVRAVGPRSGSEKWNFSVGHFELRYIPDMETRAGFIESTFKPGGNKEDSKIISDVEEQEATMLDTVIKVSVADWKVMAFSRKGGRLEWEYQFCTPIASAWLVRDGKVIPISLFDDTSYTASEEALGDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRVSEKFPTSPKALESVNGENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKYSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDSPHYSKNIRKKDPILLLHWWKEIFGTILLCIVATTFIVRRLFHPQPHRQRKESETQCQTESKYDSVSADVSDNSWNDMKYSGYVSRYLTDFEPIQCMGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLETPPEKWQEEMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFSTKEQIEVIAPSPERSRSFSVGISCGQTSSSESQFSPLEFSGTDCGDNSDSADAAYNLQDSCLTDCEDVEDGTVDGNDEGHSFELCPSEASPYTRSREGTSSSIVFEDSGCGNASSKEEPRGNRLHDGNHYVNKLTDLKCSSSRSSSEATTLSTSPTRPTTLSLDFTKNTVGQLQPSSPKVYLYIQMQLCRKENLKDWMNRRCSLEDREHGVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYATHTGQVGTKLYMSPEQIHGNNYSHKVDIFSLGLILFELLYPFSTQMERVRILTDVRNLKFPLLFTQKYPQEHMMVQDMLSPSPTERPEATDIIENAIFENLEFPGKTVLRQRSRSMSSSGTKHSRQPSCSYSPLPGN DIP protein Q9Z2B5 original sequence version: 139 65A47D6C0DD2E046 o75460-1 Serine/threonine-protein kinase/endoribonuclease IRE1 ERN1 IRE1 Endoplasmic reticulum-to-nucleus signaling 1 Inositol-requiring protein 1 Ire1-alpha protein protein human Homo sapiens Human MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL DIP protein O75460-1 original sequence version: 144 DIP protein O75460-1 original sequence version: 109 DIP protein O75460-1 original sequence version: 120 DIP protein O75460-1 original sequence version: 154 DIP protein O75460 original sequence version: 154 DIP protein O75460-1 original sequence version: 97 DIP protein O75460 original sequence version: 97 eif2ak3-1 2 6 unspecified role unspecified role unspecified role unspecified role Region 32-322 Region 32-322 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9Z2B5:p.[Lys194Pro;Leu196Pro] K194P/L196P mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L P certain certain sequence position certain certain certain sequence position certain K P This feature has been corrected as a result of our quality control procedures. The original label was 'K194P/L196P'. Wed May 02 14:27:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys194pro,leu196pro' Tue Jun 30 19:36:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys194Pro;Leu196Pro]' Q9Z2B5:p.Lys194Pro K194P mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K P This feature has been corrected as a result of our quality control procedures. The original label was 'K194P'. Wed May 02 16:49:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys194pro' Tue Jun 30 18:25:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys194Pro' Q9Z2B5:p.Leu196Pro L196P mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L P This feature has been corrected as a result of our quality control procedures. The original label was 'L196P'. Wed May 02 17:16:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu196pro' Tue Jun 30 17:47:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu196Pro' ecolx Escherichia coli direct interaction direct interaction ern1-6 3 7 unspecified role unspecified role unspecified role unspecified role Region 24-446 Region 24-446 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain O75460-1:p.Asp123Pro D123P mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D P This feature has been corrected as a result of our quality control procedures. The original label was 'D123P'. Wed May 02 17:33:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp123pro' Tue Jun 30 18:07:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp123Pro' O75460-1:p.Gln105Glu Q105E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Q E This feature has been corrected as a result of our quality control procedures. The original label was 'Q105E'. Wed May 02 18:51:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln105glu' Tue Jun 30 16:19:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln105Glu' O75460-1:p.Trp125Ala W125A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A This feature has been corrected as a result of our quality control procedures. The original label was 'W125A'. Wed May 02 14:31:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp125ala' Tue Jun 30 19:01:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp125Ala' ecolx Escherichia coli direct interaction direct interaction ern1-ern1-2 1 7 unspecified role unspecified role prey prey Region 24-446 Region 24-446 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain O75460-1:p.Asp123Pro D123P mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D P This feature has been corrected as a result of our quality control procedures. The original label was 'D123P'. Wed May 02 15:28:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp123pro' Tue Jun 30 16:14:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp123Pro' HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range crigr Cricetulus griseus (Chinese hamster) Cricetulus barabensis griseus Chinese hamster 7 unspecified role unspecified role bait bait Region 24-446 Region 24-446 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain O75460-1:p.Asp123Pro D123P mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D P This feature has been corrected as a result of our quality control procedures. The original label was 'D123P'. Wed May 02 15:32:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp123pro' Tue Jun 30 17:08:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp123Pro' Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range crigr Cricetulus griseus (Chinese hamster) Cricetulus barabensis griseus Chinese hamster physical association physical association eif2ak3-2 4 6 unspecified role unspecified role unspecified role unspecified role Region 32-322 Region 32-322 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9Z2B5:p.[Lys194Pro;Leu196Pro] K194P/L196P mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L P certain certain sequence position certain certain certain sequence position certain K P This feature has been corrected as a result of our quality control procedures. The original label was 'K194P/L196P'. Wed May 02 16:52:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys194pro,leu196pro' Tue Jun 30 17:02:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys194Pro;Leu196Pro]' Q9Z2B5:p.Lys194Pro K194P mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K P This feature has been corrected as a result of our quality control procedures. The original label was 'K194P'. Wed May 02 19:15:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys194pro' Tue Jun 30 19:57:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys194Pro' Q9Z2B5:p.Leu196Pro L196P mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L P This feature has been corrected as a result of our quality control procedures. The original label was 'L196P'. Wed May 02 18:42:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu196pro' Tue Jun 30 16:52:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu196Pro' ecolx Escherichia coli direct interaction direct interaction ern1-2 5 7 unspecified role unspecified role unspecified role unspecified role Region 24-446 Region 24-446 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain O75460-1:p.Asp123Pro D123P mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D P This feature has been corrected as a result of our quality control procedures. The original label was 'D123P'. Wed May 02 15:32:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp123pro' Tue Jun 30 17:28:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp123Pro' O75460-1:p.Gln105Glu Q105E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Q E This feature has been corrected as a result of our quality control procedures. The original label was 'Q105E'. Wed May 02 19:23:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln105glu' Tue Jun 30 16:50:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln105Glu' O75460-1:p.Trp125Ala W125A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A This feature has been corrected as a result of our quality control procedures. The original label was 'W125A'. Wed May 02 15:07:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp125ala' Tue Jun 30 18:39:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp125Ala' ecolx Escherichia coli direct interaction direct interaction