DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nature structural & molecular biology 2011 imex curation Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. Only protein-protein interactions in vitro In vitro atpase assay atpase assay predetermined predetermined participant predetermined Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. DIP original experiment: DIP-255397X Nature structural & molecular biology 2011 IMEx Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nature structural & molecular biology 2011 imex curation Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. DIP original experiment: DIP-255398X Nature structural & molecular biology 2011 IMEx Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nature structural & molecular biology 2011 imex curation Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. DIP original experiment: DIP-255400X Nature structural & molecular biology 2011 IMEx Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nature structural & molecular biology 2011 imex curation Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Marcinowski M., Höller M., Feige MJ., Baerend D., Lamb DC., Buchner J. DIP original experiment: DIP-255399X Nature structural & molecular biology 2011 IMEx Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. bip_mouse Endoplasmic reticulum chaperone BiP Immunoglobulin heavy chain-binding protein Hspa5 Grp78 78 kDa glucose-regulated protein Binding-immunoglobulin protein Heat shock protein 70 family protein 5 Heat shock protein family A member 5 protein protein mouse Mus musculus Mouse MMKFTVVAAALLLLGAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL DIP protein P20029 original sequence version: 154 DIP protein P20029 original sequence version: 113 DIP protein P20029 original sequence version: 112 DIP protein P20029 original sequence version: 117 DIP protein P20029 original sequence version: 165 AFB795D15E20FAC2 djb11_mouse DnaJ homolog subfamily B member 11 Dnajb11 ER-associated Hsp40 co-chaperone ER-associated DNAJ APOBEC1-binding protein 2 Endoplasmic reticulum DNA J domain-containing protein 3 protein protein mouse Mus musculus Mouse MAPQNLSTFCLLLLYLIGTVIAGRDFYKILGVPRSASIKDIKKAYRKLALQLHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSSHGDIFSHFFGDFGFMFGGTPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFVEVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHRIFERRGDDLYTNVTVSLVEALVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAKEGIKQLLKQGPVQKVYNGLQGY DIP protein Q99KV1 original sequence version: 86 mint E53CE0B3DF7465B8 dnajb11-hspa5-2 1 6 unspecified role unspecified role unspecified role unspecified role Q99KV1:p.His53Gln H53Q mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain H Q This feature has been corrected as a result of our quality control procedures. The original label was 'H53Q'. Wed May 02 15:14:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his53gln' Tue Jun 30 19:39:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His53Gln' ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction dnajb11-hspa5-3 3 6 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 5 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair Atto532-label Atto532-label atto 532 atto 532 certain certain sequence position certain certain certain sequence position certain Atto647-label Atto647-label atto 647 atto 647 certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction dnajb11-hspa5-4 2 6 unspecified role unspecified role bait bait ecolx Escherichia coli 5 unspecified role unspecified role prey prey ecolx Escherichia coli direct interaction direct interaction dnajb11-hspa5-5 4 6 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 5 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair Atto532-label Atto532-label atto 532 atto 532 certain certain sequence position certain certain certain sequence position certain Atto647-label Atto647-label atto 647 atto 647 certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction