DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ martn_benito-2007-1 ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Martín-Benito J., Gómez-Reino J., Stirling PC., Lundin VF., Gómez-Puertas P., Boskovic J., Chacón P., Fernández JJ., Berenguer J., Leroux MR., Valpuesta JM. DIP original experiment: DIP-66404X Structure (London, England : 1993) 2007 IMEx Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart. Martín-Benito J., Gómez-Reino J., Stirling PC., Lundin VF., Gómez-Puertas P., Boskovic J., Chacón P., Fernández JJ., Berenguer J., Leroux MR., Valpuesta JM. Only protein-protein interactions imex curation martn_benito-2007-2 in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Martín-Benito J., Gómez-Reino J., Stirling PC., Lundin VF., Gómez-Puertas P., Boskovic J., Chacón P., Fernández JJ., Berenguer J., Leroux MR., Valpuesta JM. DIP original experiment: DIP-66405X Structure (London, England : 1993) 2007 IMEx Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart. Martín-Benito J., Gómez-Reino J., Stirling PC., Lundin VF., Gómez-Puertas P., Boskovic J., Chacón P., Fernández JJ., Berenguer J., Leroux MR., Valpuesta JM. Only protein-protein interactions imex curation martn_benito-2007-3 ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Martín-Benito J., Gómez-Reino J., Stirling PC., Lundin VF., Gómez-Puertas P., Boskovic J., Chacón P., Fernández JJ., Berenguer J., Leroux MR., Valpuesta JM. DIP original experiment: DIP-66406X Structure (London, England : 1993) 2007 IMEx Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart. Martín-Benito J., Gómez-Reino J., Stirling PC., Lundin VF., Gómez-Puertas P., Boskovic J., Chacón P., Fernández JJ., Berenguer J., Leroux MR., Valpuesta JM. Only protein-protein interactions imex curation pfdb_pyrho Prefoldin subunit beta pfdB GimC subunit beta PH0532 protein protein pyrho Pyrococcus horikoshii MQNIPPQVQAMLGQLDTYQQQLQLVIQQKQKVQADLNEAKKALEEIETLPDDAQIYKTVGTLIVKTTKEKAVQELKEKIETLEVRLNALNRQEQKINEKVKELTQKIQAALRPPTAG FBF39C9878BDB427 pfda_pyrho Prefoldin subunit alpha pfdA GimC subunit alpha PH0527 protein protein pyrho Pyrococcus horikoshii MAQNNKELEKLAYEYQVLQAQAQILAQNLELLNLAKAEVQTVRETLENLKKIEEEKPEILVPIGAGSFLKGVIVDKNNAIVSVGSGYAVERSIDEAISFLEKRLKEYDEAIKKTQGALAELEKRIGEVARKAQEVQQKQSMTSFKVKK 46AB8EA20A4AC8BD ths_pyrho Thermosome subunit ths PH0017 Chaperonin subunit protein protein pyrho Pyrococcus horikoshii MAQLAGQPILILPEGTQRYVGRDAQRMNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVITNDGATILDEMDIQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELLKKAEELLDQNIHPSIIIKGYTLASQKAQEILDSIAKEVKPDDEEVLLKAAMTAITGKAAEEEREYLAKLAVEAVKLVAEEKDGKLKVDIDNIKLEKKEGGAVRDTRLIRGVVIDKEVVHPGMPKRIENAKIALINDALEVKETETDAEIRITSPEQLQAFLEQEEKMLKEMVDKIKEVGANVVFVQKGIDDLAQHYLAKYGILAVRRVKKSDMEKLAKATGAKIVTNIRDLTPEDLGEAELVEERKVAGENMIFVEGCKNPKAVTILIRGGTEHVVDEVERALEDAIKVVKDILEDGKIIAGGGASEIELSIKLDEYAKEVGGKEQLAIEAFAEALKVIPRTLAENAGLDPIETLVKVIAAHKEKGQTIGIDVYEGEPADMMERGVIEPVRVKKQAIKSASEAAIMILRIDDVIAASKLEKEKEGEKGGGSEEFSGSSDLD 9A451CA8C6CFEB4D Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity mint phpfda-phpfdb-1 3152059 N/A 3152062 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3152063 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false phpfda-phpfdb-2 3152060 N/A 3152064 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3152062 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3152063 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false phtherm-1 3152061 N/A 3152064 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false