Property Summary

NCBI Gene PubMed Count 99
Grant Count 73
R01 Count 47
Funding $4,580,533.8
PubMed Score 12.45
PubTator Score 84.03

Knowledge Summary

Patent

No data available

Expression

  Differential Expression (3)

Disease log2 FC p
colon cancer 1.100 0.024
ovarian cancer 1.200 0.000
dermatomyositis -1.100 0.004

Synonym

Accession Q16543 Q53YA2
Symbols P50CDC37

Gene

PDB

5FWK   5FWL   5FWM   1US7   2K5B   2N5X   2NCA   2W0G  

Gene RIF (45)

PMID Text
26511315 Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.
25852146 RIP3 activation following the induction of necroptosis requires the activity of an HSP90 and CDC37 cochaperone complex.
25619116 The N-terminal tail serves as an intramolecular chaperone ensuring that CDC37 assumes one of two interconvertible states in a manner impacting the interaction of the client binding N-domain and the MC-domains, involved in dimerization and HSP90 binding.
25098386 Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.
24927996 As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.
24869908 Correlation between PDZK1, Cdc37, Akt and breast cancer malignancy: the role of PDZK1 in cell growth through Akt stabilization by increasing and interacting with Cdc37
24379398 SGK3 stability and kinase activation are regulated by the Hsp90-Cdc37 chaperone complex.
24292678 CDC37 has an important role in chaperoning protein kinases; it stabilizes kinase clients by a mechanism that is not dependent on a substantial direct interaction between CDC37 and HSP90, but requires HSP90 activity
23584476 CDC37 is a crucial HSP90-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors
23569206 Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.
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AA Sequence

MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKE      1 - 70
LEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDS     71 - 140
EEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVA    141 - 210
HQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEE    211 - 280
EERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASE    281 - 350
AKEGEEAGPGDPLLEAVPKTGDEKDVSV                                              351 - 378
//

Text Mined References (111)

PMID Year Title
27353360 2016 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
26511315 2015 Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.
26496610 2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
25852146 2015 A cytosolic heat shock protein 90 and cochaperone CDC37 complex is required for RIP3 activation during necroptosis.
25619116 2015 Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.
25486457 2015 Middle domain of human Hsp90 isoforms differentially binds Aha1 in human cells and alters Hsp90 activity in yeast.
25098386 2015 Suppressing the CDC37 cochaperone in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.
25036637 2014 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
24927996 2014 FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation.
24880080 2014 SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation.
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