Cdc37 cell division cycle 37, HSP90 cochaperone [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Cdc37provided by RGD
Official Full Name: cell division cycle 37, HSP90 cochaperoneprovided by RGD
Primary source: RGD:71006
See related: Ensembl:ENSRNOG00000033426 AllianceGenome:RGD:71006
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables chaperone binding activity; protein C-terminus binding activity; and protein kinase binding activity. Involved in regulation of cell cycle. Located in cytoplasm and ruffle membrane. Part of protein-containing complex. Orthologous to human CDC37 (cell division cycle 37, HSP90 cochaperone). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Heart (RPKM 362.0), Muscle (RPKM 315.0) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 8q13

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	8	NC_086026.1 (27954292..27966935, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	8	NC_051343.1 (19677400..19690761, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	8	NC_005107.4 (22160922..22173797, complement)

Chromosome 8 - NC_086026.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Inhibition of Cdc37 Ameliorates Arthritis in Collagen-Induced Arthritis Rats by Inhibiting Synoviocyte Proliferation and Migration Through the ERK Pathway.
Title: Inhibition of Cdc37 Ameliorates Arthritis in Collagen-Induced Arthritis Rats by Inhibiting Synoviocyte Proliferation and Migration Through the ERK Pathway.
The expression of Cdc37 increased and reached a peak at one week after sciatic nerve crush.
Title: Up-Regulation of Cdc37 Contributes to Schwann Cell Proliferation and Migration After Sciatic Nerve Crush.
Blocking Hsp90-Cdc37 interactions during pressure overload hypertrophy results in ubiquitin-mediated proteasomal degradation of TGFBR2 leading to termination of TGF beta mediated signaling.
Title: Hsp90/Cdc37 assembly modulates TGFβ receptor-II to act as a profibrotic regulator of TGFβ signaling during cardiac hypertrophy.
C-terminal tail and determinants in the alphaE-helix of the catalytic domain allows the chaperones Hsp90 and Cdc37 to bind newly synthesized PKC beta II, a required event in the processing of PKC by phosphorylation
Title: The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.
CK2 activity was investigated both in vitro and in cultured cells by using anti-[pSer13]-Cdc37 antibody.
Title: Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37.
Results unveil a regulatory mechanism of Cdc37, identify a molecular link between casein kinase 2 (CK2) and many crucial protein kinases via Cdc37, and reveal the molecular basis for the ability of CK2 to regulate pleiotropic cellular functions.
Title: CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.
CK2 and Cdc37 constitute a positive feedback machinery to control multiple Cdc37-dependent signaling protein kinases.
Title: CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables Hsp90 protein binding	IEA Inferred from Electronic Annotation more info
enables Hsp90 protein binding	ISO Inferred from Sequence Orthology more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables heat shock protein binding	IEA Inferred from Electronic Annotation more info
enables heat shock protein binding	ISO Inferred from Sequence Orthology more info
enables kinase binding	ISO Inferred from Sequence Orthology more info
enables mitogen-activated protein kinase kinase kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase B binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IEA Inferred from Electronic Annotation more info
enables protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase regulator activity	IEA Inferred from Electronic Annotation more info
contributes_to protein kinase regulator activity	ISO Inferred from Sequence Orthology more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables scaffold protein binding	IEA Inferred from Electronic Annotation more info
enables scaffold protein binding	ISO Inferred from Sequence Orthology more info
enables transcription corepressor binding	IPI Inferred from Physical Interaction more info	PubMed
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in positive regulation of mitophagy in response to mitochondrial depolarization	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of mitophagy in response to mitochondrial depolarization	ISO Inferred from Sequence Orthology more info
involved_in post-transcriptional regulation of gene expression	IEA Inferred from Electronic Annotation more info
involved_in post-transcriptional regulation of gene expression	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein stabilization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	IEA Inferred from Electronic Annotation more info
involved_in regulation of type I interferon-mediated signaling pathway	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within regulation of type I interferon-mediated signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in regulation of type II interferon-mediated signaling pathway	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within regulation of type II interferon-mediated signaling pathway	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
part_of HSP90-CDC37 chaperone complex	IEA Inferred from Electronic Annotation more info
part_of HSP90-CDC37 chaperone complex	ISO Inferred from Sequence Orthology more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
part_of protein folding chaperone complex	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed
located_in ruffle membrane	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); cell division cycle 37 homolog; hsp90 chaperone protein kinase-targeting subunit; p50Cdc37

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_053743.2 → NP_446195.2 hsp90 co-chaperone Cdc37

Status: VALIDATED

Source sequence(s)

JAXUCZ010000008

UniProtKB/Swiss-Prot

Q63692, Q8CH95

UniProtKB/TrEMBL

A0A140TAG9

Related

ENSRNOP00000076743.1, ENSRNOT00000112085.1

Conserved Domains (3) summary

smart01071
Location:1 → 128

CDC37_N; Cdc37 N terminal kinase binding

smart01069
Location:288 → 378

CDC37_C; Cdc37 C terminal domain

smart01070
Location:134 → 276

CDC37_M; Cdc37 Hsp90 binding domain

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086026.1 Reference GRCr8

Range

27954292..27966935 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_039080700.2 → XP_038936628.1 hsp90 co-chaperone Cdc37 isoform X1

UniProtKB/TrEMBL

A0A140TAG9

Conserved Domains (3) summary

smart01071
Location:1 → 127

CDC37_N; Cdc37 N terminal kinase binding

smart01069
Location:337 → 427

CDC37_C; Cdc37 C terminal domain

smart01070
Location:183 → 325

CDC37_M; Cdc37 Hsp90 binding domain