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.
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Protein type: Chaperone |
Chromosomal Location of human Ortholog: 19p13.2 |
Cellular Component:
cytoplasm; cytosol; HSP90-CDC37 chaperone complex; protein folding chaperone complex
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Molecular Function:
heat shock protein binding; Hsp90 protein binding; kinase binding; protein binding; protein kinase binding; protein kinase regulator activity; protein-folding chaperone binding; scaffold protein binding; unfolded protein binding
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Biological Process:
positive regulation of mitophagy in response to mitochondrial depolarization; post-transcriptional regulation of gene expression; protein folding; protein stabilization; protein targeting; regulation of cyclin-dependent protein serine/threonine kinase activity; regulation of type I interferon-mediated signaling pathway; regulation of type II interferon-mediated signaling pathway
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Reference #:
Q16543
(UniProtKB)
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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
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Gene Symbols: CDC37
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Molecular weight:
44,468 Da
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Basal Isoelectric point:
5.17
Predict pI for various phosphorylation states
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CST Pathways:
Inhibition of Apoptosis
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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