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

    Gene ID: 11140, updated on 28-Oct-2024

    Summary

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    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

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    See CDC37 in Genome Data Viewer
    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_000019.10Genomic Context describing neighboring genes Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10443599-10444515 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10445230-10445848 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10448906-10449654 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13959 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13960 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10450403-10451150 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10451151-10451898 Neighboring gene intercellular adhesion molecule 3 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10463923-10464686 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10474734-10475234 Neighboring gene tyrosine kinase 2 Neighboring gene H3K27ac hESC enhancer GRCh37_chr19:10491214-10491877 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13962 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13963 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10499431-10499931 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10066 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13965 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10067 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13966 Neighboring gene microRNA 1181 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10068 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13967 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10527911-10528462 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10528463-10529013 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10530007-10530886 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10069 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10070 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13968 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13969 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10071 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10072 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10542553-10543236 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10543237-10543919 Neighboring gene phosphodiesterase 4A Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10546465-10546964 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13970 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13971 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10075 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10076 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:10572008-10572732 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13973 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:10602595-10603095 Neighboring gene Sharpr-MPRA regulatory region 8442 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 13974 Neighboring gene H3K27ac hESC enhancer GRCh37_chr19:10612744-10613299 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10078 Neighboring gene kelch like ECH associated protein 1

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • 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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    Related articles in PubMed

    1. p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function. Grammatikakis N, et al. Mol Cell Biol, 1999 Mar. PMID 10022854, Free PMC Article
    2. Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors. Smith JR, et al. Oncogene, 2009 Jan 15. PMID 18931700, Free PMC Article
    3. Cdc37 enhances proliferation and is necessary for normal human prostate epithelial cell survival. Schwarze SR, et al. Cancer Res, 2003 Aug 1. PMID 12907640
    4. p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. Hartson SD, et al. Biochemistry, 2000 Jun 27. PMID 10858314
    5. The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. Sreeramulu S, et al. J Biol Chem, 2009 Feb 6. PMID 19073599

    See all (297) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
      Title: HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
    3. The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases.
      Title: The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases.
    4. 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.
    5. 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.
    6. 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.
    7. [Cdc37 Expression in Multiple Myeloma and Its Role in Cell Proliferation].
      Title: [Cdc37 Expression in Multiple Myeloma and Its Role in Cell Proliferation].
    8. 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.
    9. 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.
    10. 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
    Host-microbe interactions have shaped the genetic architecture of inflammatory bowel disease.
    EBI GWAS Catalog

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    Genotypes

    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

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    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 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)

    1. 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

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000019.10 Reference GRCh38.p14 Primary Assembly

      Range
      10391133..10403542 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060943.1 Alternate T2T-CHM13v2.0

      Range
      10517575..10529998 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q16543.1 GenPept UniProtKB/Swiss-Prot:Q16543

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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