{"systematicName":"CDC37:2xHSP90AA1","synonyms":[],"functions":["A chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The complex prevents the aggregation and degradation of protein kinases while maintaining the proper structure of their domains, recognizing and binding the extended kinase domain formed by reorganisation of the client protein to enable replacement of a hydrolyzed ADP with a new ATP molecule.  The highly conserved, phosphorylated CDC37 Ser-13 is essential for complex assembly and target protein binding.\r\n\r\nCDC37 Ser-13 is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. CDC37 Ser-13 is de-phosphorylated by PP5 (P53041). Target proteins are recognised by the CDC37 subunit. The complex  associates with intrinsically unstable kinases, recognizing and folding both nascent kinase polypeptides emerging from ribosomes and mature kinases to maintain their activity and stability. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.kinases to maintain their activity and stability Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins."],"properties":["CDC37 asymmetrically interacts across the HSP90 dimer and also binds client protein kinase. CDC37 binds its target proteins via its N-terminus (1-120 aa, InterPro IPR013855) and the HSP90 subunit via its central domain. Binding of CDC37 to HSP90 blocks the ATP binding site on HSP90."],"ac":"EBI-9990629","complexAc":"CPX-3288","name":"HSP90A-CDC37 chaperone complex","species":"Homo sapiens; 9606","ligands":[],"complexAssemblies":["Heterotrimer"],"diseases":[],"participants":[{"interactorAC":"EBI-9991822","identifier":"Q16543","identifierLink":"https://www.uniprot.org/uniprotkb/Q16543/entry","name":"CDC37","description":"Hsp90 co-chaperone Cdc37","stochiometry":"minValue: 1, maxValue: 1","bioRole":"unspecified role","bioRoleMI":"MI:0499","bioRoleDefinition":"Role not specified or not applicable to the data.","interactorType":"protein","interactorTypeMI":"MI:0326","interactorTypeDefinition":"A linear polymer of amino acids joined by peptide bonds in a specific sequence.","linkedFeatures":[{"featureAc":"EBI-9991834","participantId":"P07900","name":"cdc37 binding region","featureType":"binding region","featureTypeMI":"MI:0117","featureTypeDefinition":"A region of a molecule or a component of a complex identified as being involved in an interaction. This may or may not be a region of the molecule in direct contact with the interacting partner.","featureTypeUrl":"http://www.ebi.ac.uk/ols/ontologies/mi/terms?obo_id=MI:0117","featureRole":null,"featureRoleMI":null,"featureRoleDefinition":null,"featureRoleUrl":null,"ranges":["17-225"],"linkedFeatures":["EBI-9991824"],"crossReferences":[{"database":"interpro","qualifier":"identical object in an external resource","identifier":"IPR020575","description":null,"searchURL":"https://www.ebi.ac.uk/interpro/entry/InterPro/IPR020575","dbMI":"MI:0449","qualifierMI":"MI:0356","dbdefinition":"InterPro combines a number of databases (referred to as member databases) that use different methodologies and a varying degree of biological information on well-characterised proteins to derive protein signatures that predict family membership and domain composition of naive protein sequences.","qualifierDefinition":"Reference to the corresponding object in another database. 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This may or may not be a region of the molecule in direct contact with the interacting partner.","featureTypeUrl":"http://www.ebi.ac.uk/ols/ontologies/mi/terms?obo_id=MI:0117","featureRole":null,"featureRoleMI":null,"featureRoleDefinition":null,"featureRoleUrl":null,"ranges":["17-225"],"linkedFeatures":["EBI-9991824"],"crossReferences":[{"database":"interpro","qualifier":"identical object in an external resource","identifier":"IPR020575","description":null,"searchURL":"https://www.ebi.ac.uk/interpro/entry/InterPro/IPR020575","dbMI":"MI:0449","qualifierMI":"MI:0356","dbdefinition":"InterPro combines a number of databases (referred to as member databases) that use different methodologies and a varying degree of biological information on well-characterised proteins to derive protein signatures that predict family membership and domain composition of naive protein sequences.","qualifierDefinition":"Reference to the corresponding object in another database. Correspondence may be complete or partial.","qualifierUrl":"http://www.ebi.ac.uk/ols/ontologies/mi/terms?obo_id=MI:0356"}]}],"otherFeatures":[]},{"interactorAC":"EBI-9991833","identifier":"P07900","identifierLink":"https://www.uniprot.org/uniprotkb/P07900/entry","name":"HSP90AA1","description":"Heat shock protein HSP 90-alpha","stochiometry":"minValue: 2, maxValue: 2","bioRole":"unspecified role","bioRoleMI":"MI:0499","bioRoleDefinition":"Role not specified or not applicable to the data.","interactorType":"protein","interactorTypeMI":"MI:0326","interactorTypeDefinition":"A linear polymer of amino acids joined by peptide bonds in a specific sequence.","linkedFeatures":[{"featureAc":"EBI-9991824","participantId":"Q16543","name":"HSP90 binding domain","featureType":"binding region","featureTypeMI":"MI:0117","featureTypeDefinition":"A region of a molecule or a component of a complex identified as being involved in an interaction. 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Correspondence may be complete or partial.","qualifierUrl":"http://www.ebi.ac.uk/ols/ontologies/mi/terms?obo_id=MI:0356"}]},{"featureAc":"EBI-9991819","participantId":"P07900","name":"dimerisation domain","featureType":"binding region","featureTypeMI":"MI:0117","featureTypeDefinition":"A region of a molecule or a component of a complex identified as being involved in an interaction. 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