CDC37

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Cdc37 N terminal kinase binding
Cdc37 N terminal kinase binding
Identifiers
Symbol	CDC37_N
Pfam	PF03234
InterPro	IPR013855
SCOP2	1us7 / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

CDC37
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1US7, 2K5B, 2W0G, 2N5X, 2NCA, 5FWM, 5FWL, 5FWK
Identifiers
Aliases	CDC37, P50cell division cycle 37, cell division cycle 37, HSP90 cochaperone
External IDs	OMIM: 605065; MGI: 109531; HomoloGene: 38268; GeneCards: CDC37; OMA:CDC37 - orthologs
Gene location (Human)
Chr.	Chromosome 19 (human)
End	10,420,121 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	21,061,278 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; apex of heart; ; granulocyte; ; body of uterus; ; left uterine tube; ; upper lobe of left lung; ; left lobe of thyroid gland; ; gastric mucosa; ; right uterine tube; ; canal of the cervix;
	Top expressed in
	maxillary prominence; ; mandibular prominence; ; right ventricle; ; neural layer of retina; ; somite; ; dentate gyrus of hippocampal formation granule cell; ; epiblast; ; abdominal wall; ; efferent ductule; ; neural tube;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	unfolded protein binding; Hsp90 protein binding; kinase binding; chaperone binding; protein binding; protein kinase binding; heat shock protein binding; protein kinase regulator activity; protein tyrosine kinase activity; scaffold protein binding;
Cellular component	extracellular exosome; HSP90-CDC37 chaperone complex; cytoplasm; cytosol; chaperone complex;
Biological process	posttranscriptional regulation of gene expression; protein _targeting; protein stabilization; regulation of cyclin-dependent protein serine/threonine kinase activity; regulation of type I interferon-mediated signaling pathway; regulation of interferon-gamma-mediated signaling pathway; positive regulation of mitophagy in response to mitochondrial depolarization; regulation of protein kinase activity; protein folding; peptidyl-tyrosine phosphorylation; ERBB2 signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	11140
	12539
	ENSG00000105401
	ENSMUSG00000019471
	Q16543
	Q61081
	NM_007065
	NM_016742; NM_001378796
	NP_008996
	NP_058022; NP_001365725
	Wikidata
View/Edit Human	View/Edit Mouse

Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.^[5] This protein is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone^[6] 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.^[7]

Cdc37 Hsp90 binding domain

complex of hsp90 and p50

Identifiers

Symbol

CDC37_M

1us7 / SCOPe / SUPFAM

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Cdc37 C terminal domain

complex of hsp90 and p50

Identifiers

Symbol

CDC37_C

1us7 / SCOPe / SUPFAM

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Interactions

CDC37 has been shown to interact with:

Domain architecture

CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases.^[16] The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain.^[17] The function of the C-terminal domain is unclear.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000105401 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000019471 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Dai K, Kobayashi R, Beach D (September 1996). "Physical interaction of mammalian CDC37 with CDK4". The Journal of Biological Chemistry. 271 (36): 22030–22034. doi:10.1074/jbc.271.36.22030. PMID 8703009.
^ Mollapour M, Neckers L (March 2012). "Post-translational modifications of Hsp90 and their contributions to chaperone regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (3): 648–655. doi:10.1016/j.bbamcr.2011.07.018. PMC 3226900. PMID 21856339.
^ "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)".
^ Stepanova L, Leng X, Parker SB, Harper JW (June 1996). "Mammalian p50Cdc37 is a protein kinase-_targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes & Development. 10 (12): 1491–1502. doi:10.1101/gad.10.12.1491. PMID 8666233.
^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
^ Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, et al. (April 1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene. 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.
^ Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, et al. (January 2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell. 116 (1): 87–98. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169. S2CID 797232.
^ Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB (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. 273 (32): 20090–20095. doi:10.1074/jbc.273.32.20090. PMID 9685350.
^ Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
^ ^a ^b Chen G, Cao P, Goeddel DV (February 2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Molecular Cell. 9 (2): 401–410. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.
^ Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR (March 2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". The Biochemical Journal. 370 (Pt 3): 849–857. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981.
^ Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, et al. (July 1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes & Development. 11 (14): 1775–1785. doi:10.1101/gad.11.14.1775. PMID 9242486.
^ Turnbull EL, Martin IV, Fantes PA (August 2005). "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". The FEBS Journal. 272 (16): 4129–4140. doi:10.1111/j.1742-4658.2005.04825.x. PMID 16098195. S2CID 23442218.

External links

Human CDC37 genome location and CDC37 gene details page in the UCSC Genome Browser.

This article incorporates text from the public domain Pfam and InterPro: IPR013855

This article incorporates text from the public domain Pfam and InterPro: IPR013874

This article incorporates text from the public domain Pfam and InterPro: IPR013873

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000105401 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000019471 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8703009-5] Dai K, Kobayashi R, Beach D (September 1996). "Physical interaction of mammalian CDC37 with CDK4". The Journal of Biological Chemistry. 271 (36): 22030–22034. doi:10.1074/jbc.271.36.22030. PMID 8703009.

[6] Mollapour M, Neckers L (March 2012). "Post-translational modifications of Hsp90 and their contributions to chaperone regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (3): 648–655. doi:10.1016/j.bbamcr.2011.07.018. PMC 3226900. PMID 21856339.

[entrez-7] "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)".

[pmid8666233-8] Stepanova L, Leng X, Parker SB, Harper JW (June 1996). "Mammalian p50Cdc37 is a protein kinase-_targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes & Development. 10 (12): 1491–1502. doi:10.1101/gad.10.12.1491. PMID 8666233.

[pmid17353931-9] Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

[pmid9150368-10] Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, et al. (April 1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene. 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.

[pmid14718169-11] Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, et al. (January 2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell. 116 (1): 87–98. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169. S2CID 797232.

[pmid9685350-12] Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB (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. 273 (32): 20090–20095. doi:10.1074/jbc.273.32.20090. PMID 9685350.

[pmid14743216-13] Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.

[pmid11864612-14] Chen G, Cao P, Goeddel DV (February 2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Molecular Cell. 9 (2): 401–410. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.

[pmid12489981-15] Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR (March 2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". The Biochemical Journal. 370 (Pt 3): 849–857. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981.

[pmid9242486-16] Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, et al. (July 1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes & Development. 11 (14): 1775–1785. doi:10.1101/gad.11.14.1775. PMID 9242486.

[pmid16098195-17] Turnbull EL, Martin IV, Fantes PA (August 2005). "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". The FEBS Journal. 272 (16): 4129–4140. doi:10.1111/j.1742-4658.2005.04825.x. PMID 16098195. S2CID 23442218.

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CDC37

Contents

Interactions

Domain architecture

References

Further reading

External links