CDC37 cell division cycle 37, HSP90 cochaperone [Homo sapiens (human)] - Gene

Summary

Official Symbol: CDC37provided by HGNC
Official Full Name: cell division cycle 37, HSP90 cochaperoneprovided by HGNC
Primary source: HGNC:HGNC:1735
See related: Ensembl:ENSG00000105401 MIM:605065; AllianceGenome:HGNC:1735
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: P50CDC37
Summary: The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular 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, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in fat (RPKM 70.6), spleen (RPKM 61.9) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 19p13.2

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (10391133..10403542, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (10517575..10529998, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (10501809..10514218, complement)

Chromosome 19 - NC_000019.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Structural insight into guanylyl cyclase receptor hijacking of the kinase-Hsp90 regulatory mechanism.
Title: Structural insight into guanylyl cyclase receptor hijacking of the kinase-Hsp90 regulatory mechanism.
HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
Title: HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases.
Title: The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases.
Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B.
Title: Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B.
Protein quality control of DYRK family protein kinases by the Hsp90-Cdc37 molecular chaperone.
Title: Protein quality control of DYRK family protein kinases by the Hsp90-Cdc37 molecular chaperone.
Hsp90 interacts with Cdc37, is phosphorylated by PKA/PKC, and regulates Src phosphorylation in human sperm capacitation.
Title: Hsp90 interacts with Cdc37, is phosphorylated by PKA/PKC, and regulates Src phosphorylation in human sperm capacitation.
[Cdc37 Expression in Multiple Myeloma and Its Role in Cell Proliferation].
Title: [Cdc37 Expression in Multiple Myeloma and Its Role in Cell Proliferation].
The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37.
Title: The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37.
The CDC37-HSP90 chaperone complex co-translationally degrades the nascent kinase-dead mutant of HIPK2.
Title: The CDC37-HSP90 chaperone complex co-translationally degrades the nascent kinase-dead mutant of HIPK2.
Medium-Throughput Detection of Hsp90/Cdc37 Protein-Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay.
Title: Medium-Throughput Detection of Hsp90/Cdc37 Protein-Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay.

Submit: New GeneRIF Correction See all GeneRIFs (66)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
Genetic risk and a primary role for cell-mediated immune mechanisms in multiple sclerosis. EBI GWAS Catalog EBI GWAS CatalogPubMed
Host-microbe interactions have shaped the genetic architecture of inflammatory bowel disease. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See Variation Viewer (GRCh37.p13)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Tat	tat	Hsp70 and Hsp90 and Cdc37 regulate the stabilization and folding of CDK9 as well as the assembly of an active CDK9/cyclin T1 complex responsible for P-TEFb-mediated HIV-1 Tat transactivation	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH41901 (e-PCR)
- UniSTS:51987

RH80833 (e-PCR)
- UniSTS:89945

NoName (e-PCR)
- UniSTS:486773

RH101844 (e-PCR)
- UniSTS:41856

D19S1108 (e-PCR)
- UniSTS:44424

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables Hsp90 protein binding	IEA Inferred from Electronic Annotation more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables heat shock protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IEA Inferred from Electronic Annotation more info
enables protein kinase regulator activity	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables scaffold protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in positive regulation of type 2 mitophagy	IEA Inferred from Electronic Annotation more info
involved_in post-transcriptional regulation of gene expression	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein targeting	TAS Traceable Author Statement more info	PubMed
involved_in regulation of cyclin-dependent protein serine/threonine kinase activity	TAS Traceable Author Statement more info	PubMed
acts_upstream_of_or_within regulation of type I interferon-mediated signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within regulation of type II interferon-mediated signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of HSP90-CDC37 chaperone complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
part_of protein folding chaperone complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: hsp90 co-chaperone Cdc37

Names: CDC37 (cell division cycle 37, S. cerevisiae, homolog); CDC37 cell division cycle 37 homolog; cell division cycle 37 homolog; hsp90 chaperone protein kinase-targeting subunit

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_007065.4 → NP_008996.1 hsp90 co-chaperone Cdc37

See identical proteins and their annotated locations for NP_008996.1

Status: REVIEWED

Source sequence(s)

BC000083, BE796008

Consensus CDS

CCDS12237.1

UniProtKB/Swiss-Prot

Q16543, Q53YA2

UniProtKB/TrEMBL

Q6FG59

Related

ENSP00000222005.1, ENST00000222005.7

Conserved Domains (3) summary

smart01071
Location:1 → 127

CDC37_N; Cdc37 N terminal kinase binding

smart01069
Location:287 → 377

CDC37_C; Cdc37 C terminal domain

smart01070
Location:133 → 275

CDC37_M; Cdc37 Hsp90 binding domain