A0A172LPE8 · A0A172LPE8_TACFU

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.

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
Molecular Functionheat shock protein binding
Molecular Functionprotein kinase binding
Molecular Functionprotein-folding chaperone binding
Molecular Functionunfolded protein binding
Biological Processprotein folding
Biological Processprotein stabilization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Hsp90 co-chaperone Cdc37
  • Alternative names
    • Hsp90 chaperone protein kinase-targeting subunit

Organism names

Accessions

  • Primary accession
    A0A172LPE8

Subcellular Location

Keywords

Interaction

Subunit

Forms a complex with Hsp90.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-128Cdc37 N-terminal
Region66-108Disordered
Domain121-282Cdc37 Hsp90 binding
Domain286-347Cdc37 C-terminal

Sequence similarities

Belongs to the CDC37 family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    349
  • Mass (Da)
    41,431
  • Last updated
    2016-09-07 v1
  • Checksum
    18C6AAE1D7DF8358
IDYSVWDHIEVSDDEDDTHPNIDTPSLFRWRHQARVERMEAFQMKGVELEKSLSEVRKKLSEAQRKVKKLEGASTEQAKKELEEAKNEEKQLRKEERSWEKKIDEHRREEKKMPWNVDTLSKEGFSKSVLNIKPEVKEETEEEKEKKHKTFVEKYETQIKHFGMLRRWDDSQKFLSDNPHLVCEETANYLVIMCIDLEVEEKHALMEQVAHQTIVMQFILELAKSLKIDPRGCFRQFFSKIKTADQQYQDAFNDELASFKERVRGRAKVRIEKAMKEYEEEERKKRLGPGGLDPVEVYDTLPQEMQKCFDDKDIQMLQDAISKMDPTEAKYHMKRCIDSGLWVPNSQPD

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue349

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KR673408
EMBL· GenBank· DDBJ
ANA95818.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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