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: 9|9 A3
Cellular Component:  chaperone complex; cytoplasm; cytosol; HSP90-CDC37 chaperone complex; protein-containing complex; ruffle membrane
Molecular Function:  chaperone binding; heat shock protein binding; Hsp90 protein binding; kinase binding; mitogen-activated protein kinase kinase kinase binding; protein binding; protein C-terminus binding; protein kinase B binding; protein kinase binding; scaffold protein binding; unfolded protein binding
Biological Process:  positive regulation of mitophagy in response to mitochondrial depolarization; posttranscriptional regulation of gene expression; protein folding; protein stabilization; regulation of interferon-gamma-mediated signaling pathway; regulation of protein kinase activity; regulation of type I interferon-mediated signaling pathway
Reference #:  Q61081 (UniProtKB)
Alt. Names/Synonyms: Cdc37; cell division cycle 37 homolog (S. cerevisiae); Hsp90 chaperone protein kinase-targeting subunit; Hsp90 co-chaperone Cdc37; p50; p50Cdc37
Gene Symbols: Cdc37
Molecular weight: 44,593 Da
Basal Isoelectric point: 5.24  Predict pI for various phosphorylation states
CST Pathways:  Inhibition of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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CDC37

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene