Q61081 · CDC37_MOUSE

  • Protein
    Hsp90 co-chaperone Cdc37
  • Gene
    Cdc37
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular ComponentHSP90-CDC37 chaperone complex
Cellular Componentprotein-containing complex
Cellular Componentruffle membrane
Molecular Functionheat shock protein binding
Molecular FunctionHsp90 protein binding
Molecular Functionkinase binding
Molecular Functionmitogen-activated protein kinase kinase kinase binding
Molecular Functionprotein kinase B binding
Molecular Functionprotein kinase binding
Molecular Functionprotein-folding chaperone binding
Molecular Functionscaffold protein binding
Molecular Functiontranscription corepressor binding
Molecular Functionunfolded protein binding
Biological Processpositive regulation of mitophagy in response to mitochondrial depolarization
Biological Processpost-transcriptional regulation of gene expression
Biological Processprotein folding
Biological Processprotein stabilization
Biological Processregulation of protein kinase activity
Biological Processregulation of type I interferon-mediated signaling pathway
Biological Processregulation of type II interferon-mediated signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Cdc37

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61081
  • Secondary accessions
    • Q3TGP0

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed; alternate
Modified residue1N-acetylmethionine
ChainPRO_00004231981-379Hsp90 co-chaperone Cdc37
Modified residue2N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed
ChainPRO_00001950582-379Hsp90 co-chaperone Cdc37, N-terminally processed
Modified residue13Phosphoserine
Modified residue119Phosphothreonine
Modified residue121Phosphoserine
Modified residue155N6-acetyllysine
Modified residue378Phosphoserine

Post-translational modification

Constitutively sumoylated by UBE2I.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (By similarity).
Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity).
Forms a complex with Hsp90/HSP90AB1 and CDK6 (By similarity).
Interacts with HSP90AA1 (By similarity).
Interacts with AR, CDK4, CDK6 and EIF2AK1 (By similarity).
Interacts with RB1 (By similarity).
Interacts with KSR1 (PubMed:10409742).
Interacts with FLCN, FNIP1 and FNIP2 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region124-146Disordered
Compositional bias132-146Basic and acidic residues
Region344-379Disordered

Sequence similarities

Belongs to the CDC37 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    379
  • Mass (Da)
    44,593
  • Last updated
    1996-11-01 v1
  • Checksum
    847C146B4FE3AAF1
MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQIKHFGMLHRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLLEAVPKAGNEKDVSA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1L1STC0A0A1L1STC0_MOUSECdc37353

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias132-146Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U43076
EMBL· GenBank· DDBJ
AAB18761.1
EMBL· GenBank· DDBJ
mRNA
AK010494
EMBL· GenBank· DDBJ
BAB26984.1
EMBL· GenBank· DDBJ
mRNA
AK013255
EMBL· GenBank· DDBJ
BAB28749.1
EMBL· GenBank· DDBJ
mRNA
AK145671
EMBL· GenBank· DDBJ
BAE26580.1
EMBL· GenBank· DDBJ
mRNA
AK168651
EMBL· GenBank· DDBJ
BAE40508.1
EMBL· GenBank· DDBJ
mRNA
BC060079
EMBL· GenBank· DDBJ
AAH60079.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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