CDC37

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Protein-coding gene in humans

title: "CDC37" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["co-chaperones"] description: "Protein-coding gene in humans" topic_path: "general/co-chaperones" source: "https://en.wikipedia.org/wiki/CDC37" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in humans ::

| Symbol = CDC37_N | Name = Cdc37 N terminal kinase binding | image = | width = | caption = | Pfam = PF03234 | Pfam_clan = | InterPro = IPR013855 | SMART = | PROSITE = | MEROPS = | SCOP = 1us7 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | Symbol = CDC37_M | Name = Cdc37 Hsp90 binding domain | image = PDB 1us7 EBI.jpg | width = | caption = complex of hsp90 and p50 | Pfam = PF08565 | Pfam_clan = | InterPro = IPR013874 | SMART = | PROSITE = | MEROPS = | SCOP = 1us7 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | Symbol = CDC37_C | Name = Cdc37 C terminal domain | image = PDB 1us7 EBI.jpg | width = | caption = complex of hsp90 and p50 | Pfam = PF08564 | Pfam_clan = | InterPro = IPR013873 | SMART = | PROSITE = | MEROPS = | SCOP = 1us7 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene. This protein is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.

Interactions

CDC37 has been shown to interact with:

Domain architecture

CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases. The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain. The function of the C-terminal domain is unclear.

References

References

  1. (September 1996). "Physical interaction of mammalian CDC37 with CDK4". The Journal of Biological Chemistry.
  2. (March 2012). "Post-translational modifications of Hsp90 and their contributions to chaperone regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.
  3. "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)".
  4. (June 1996). "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes & Development.
  5. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology.
  6. (April 1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene.
  7. (January 2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell.
  8. (August 1998). "p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site". The Journal of Biological Chemistry.
  9. (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology.
  10. (February 2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Molecular Cell.
  11. (March 2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". The Biochemical Journal.
  12. (July 1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes & Development.
  13. (August 2005). "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". The FEBS Journal.

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co-chaperones