Cdc37 cell division cycle 37 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Cdc37provided by MGI
Official Full Name: cell division cycle 37provided by MGI
Primary source: MGI:MGI:109531
See related: Ensembl:ENSMUSG00000019471 AllianceGenome:MGI:109531
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: p50; p50Cdc37
Summary: Enables Hsp90 protein binding activity and kinase binding activity. Contributes to protein kinase regulator activity. Involved in positive regulation of mitophagy in response to mitochondrial depolarization; posttranscriptional regulation of gene expression; and regulation of protein kinase activity. Located in cytosol. Part of HSP90-CDC37 chaperone complex. Is expressed in 2-cell stage embryo and 4-cell stage embryo. Orthologous to human CDC37 (cell division cycle 37, HSP90 cochaperone). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Ubiquitous expression in CNS E11.5 (RPKM 68.6), liver E14 (RPKM 50.3) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 9 A3; 9 7.72 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	9	NC_000075.7 (21050727..21061230, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	9	NC_000075.6 (21139431..21149934, complement)

Chromosome 9 - NC_000075.7 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: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Results showed that Cdc37 acts as a bridge to direct Hsp90 to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90, with or without binding to Hsp90, the interaction between Cdc37 and Hsp90 appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90-mediated protein maturation.
Title: The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.
Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth.
Title: Computational Discovery of Niclosamide Ethanolamine, a Repurposed Drug Candidate That Reduces Growth of Hepatocellular Carcinoma Cells In Vitro and in Mice by Inhibiting Cell Division Cycle 37 Signaling.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle.
Title: Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.
Hsp90-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha activity.
Title: Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.
JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways
Title: The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons.
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase pull-down assay, and the possible interaction model was suggested.
Title: Interaction of mouse Pem protein and cell division cycle 37 homolog.
CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells
Title: Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function.
This growth inhibition is partially rescued by expression of ectopic Gli1, suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.
Title: Fused kinase is stabilized by Cdc37/Hsp90 and enhances Gli protein levels.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (1)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

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

Process	Evidence Code	Pubs
involved_in positive regulation of mitophagy in response to mitochondrial depolarization	IDA Inferred from Direct Assay more info	PubMed
involved_in post-transcriptional regulation of gene expression	IDA Inferred from Direct Assay more info	PubMed
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 regulation of protein kinase activity	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within regulation of type I interferon-mediated signaling pathway	ISO Inferred from Sequence Orthology more info	PubMed
acts_upstream_of_or_within regulation of type II interferon-mediated signaling pathway	ISO Inferred from Sequence Orthology more info	PubMed

Component	Evidence Code	Pubs
part_of HSP90-CDC37 chaperone complex	IDA Inferred from Direct Assay more info	PubMed
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	ISO Inferred from Sequence Orthology more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
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	ISO Inferred from Sequence Orthology more info
located_in ruffle membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: hsp90 co-chaperone Cdc37

Names: 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_001378796.1 → NP_001365725.1 hsp90 co-chaperone Cdc37 isoform 1

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).

Source sequence(s)

AC163637

UniProtKB/TrEMBL

A0A1L1STC0

Related

ENSMUSP00000150265.2, ENSMUST00000215296.2

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
NM_016742.5 → NP_058022.1 hsp90 co-chaperone Cdc37 isoform 2

See identical proteins and their annotated locations for NP_058022.1

Status: VALIDATED

Source sequence(s)

AC163637

Consensus CDS

CCDS22894.1

UniProtKB/Swiss-Prot

Q3TGP0, Q61081

UniProtKB/TrEMBL

A0A1L1STC0

Related

ENSMUSP00000019615.10, ENSMUST00000019615.11

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