CDC37

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
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)[1] Band 19p13.2 Start 10,391,133 bp[1] End 10,420,121 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 A3 Start 21,044,518 bp[2] End 21,061,278 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 11140 12539 Ensembl ENSG00000105401 ENSMUSG00000019471 UniProt Q16543 Q61081 RefSeq (mRNA) NM_007065 NM_016742 NM_001378796 RefSeq (protein) NP_008996 NP_058022 NP_001365725 Location (UCSC) Chr 19: 10.39 – 10.42 Mb Chr 9: 21.04 – 21.06 Mb PubMed search [3] [4]
Wikidata
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Cdc37 N terminal kinase binding
Identifiers
Symbol	CDC37_N
Pfam	PF03234
InterPro	IPR013855
SCOP2	1us7 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Cdc37 Hsp90 binding domain
complex of hsp90 and p50
Identifiers
Symbol	CDC37_M
Pfam	PF08565
InterPro	IPR013874
SCOP2	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
Pfam	PF08564
InterPro	IPR013873
SCOP2	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:

• CDK4,^{[5][8][9][10]}
• HSP90AA1^[11][12]
• IKBKG,^[13][14]
• IKK2,^[14] and
• STK11.^[15]

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.