CDC37

CDC37
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCDC37, P50cell division cycle 37, cell division cycle 37, HSP90 cochaperone
External IDsOMIM: 605065; MGI: 109531; HomoloGene: 38268; GeneCards: CDC37; OMA:CDC37 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_007065

NM_016742
NM_001378796

RefSeq (protein)

NP_008996

NP_058022
NP_001365725

Location (UCSC)Chr 19: 10.39 – 10.42 MbChr 9: 21.04 – 21.06 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Cdc37 N terminal kinase binding
Identifiers
SymbolCDC37_N
PfamPF03234
InterProIPR013855
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cdc37 Hsp90 binding domain
complex of hsp90 and p50
Identifiers
SymbolCDC37_M
PfamPF08565
InterProIPR013874
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cdc37 C terminal domain
complex of hsp90 and p50
Identifiers
SymbolCDC37_C
PfamPF08564
InterProIPR013873
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105401Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019471Ensembl, 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.
  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.
  7. ^ "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)".