CDC37 Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity. Belongs to the CDC37 family. Note: This description may include information from UniProtKB.
Protein type: Chaperone
Chromosomal Location of Human Ortholog: 19p13.2
Cellular Component:  chaperone complex; cytoplasm; cytosol; HSP90-CDC37 chaperone complex
Molecular Function:  heat shock protein binding; Hsp90 protein binding; kinase binding; protein binding; protein kinase binding; protein kinase regulator activity; scaffold protein binding
Biological Process:  ERBB2 signaling pathway; positive regulation of mitophagy in response to mitochondrial depolarization; posttranscriptional regulation of gene expression; protein targeting; regulation of cyclin-dependent protein serine/threonine kinase activity; regulation of interferon-gamma-mediated signaling pathway; regulation of type I interferon-mediated signaling pathway
Reference #:  Q16543 (UniProtKB)
Alt. Names/Synonyms: CDC37; CDC37 (cell division cycle 37, S. cerevisiae, homolog); CDC37 cell division cycle 37 homolog; CDC37A; cell division cycle 37 homolog; cell division cycle 37 homolog (S. cerevisiae); cell division cycle 37 protein; cell division cycle 37, HSP90 cochaperone; Hsp90 chaperone protein kinase-targeting subunit; Hsp90 co-chaperone Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed; p50Cdc37
Gene Symbols: CDC37
Molecular weight: 44,468 Da
Basal Isoelectric point: 5.17  Predict pI for various phosphorylation states
CST Pathways:  Inhibition of Apoptosis
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

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