Q4UDU8 · HSP90_THEAN

  • Protein
    Heat shock protein 90
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).

Features

Showing features for binding site.

1722100200300400500600700
TypeIDPosition(s)Description
Binding site44ATP (UniProtKB | ChEBI)
Binding site86ATP (UniProtKB | ChEBI)
Binding site105ATP (UniProtKB | ChEBI)
Binding site131ATP (UniProtKB | ChEBI)
Binding site396ATP (UniProtKB | ChEBI)

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 Componentcytosol
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionunfolded protein binding
Biological Processcellular response to heat
Biological Processprotein stabilization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Heat shock protein 90
  • Short names
    HSP90

Gene names

    • ORF names
      TA12105

Organism names

  • Taxonomic identifier
  • Strain
    • Ankara
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Theileriidae > Theileria

Accessions

  • Primary accession
    Q4UDU8

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002326771-722Heat shock protein 90

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

Type
IDPosition(s)Description
Region219-273Disordered
Compositional bias237-270Basic and acidic residues
Region698-722Disordered
Motif718-722TPR repeat-binding

Domain

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.

Sequence similarities

Belongs to the heat shock protein 90 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    722
  • Mass (Da)
    83,825
  • Last updated
    2005-07-05 v1
  • Checksum
    06057681F0F67E6A
MASKEETPDQEVYAFNADISQLLSLIINAFYSNKEIFLRELISNASDALEKIRYEAIKDPKQIEDQPDYYIRLYADKNNNTLTIEDSGIGMTKADLVNNLGTIAKSGTRAFMEALQAGSDMSMIGQFGVGFYSAYLVADKVTVVSKNNADDQYVWESSASGHFTVKRDDSHEPLKRGTRLILHLKEDQTEYLEERRLKELVKKHSEFISFPISLSVEKTQETEVTDDEAEPEEEKKLEEEDKDKEEKVEDVTDEKVTDVTEEEEKKEEKKKKKRKVTNVTREWEMLNKQKPIWMRLPTEVTNEEYASFYKNLTNDWEDHLAVKHFSVEGQLEFKALLFVPRRAPFDMFESRKKKNNIKLYVRRVFIMDDCEELIPEWLSFVKGVVDSEDLPLNISRETLQQNKILKVIRKNLVKKCLELFNELTEKKEDFKKFYEQFSKNLKLGIHEDNANRSKIAELLRFETTKSGDELVSLKEYVDRMKSDQKFVYYITGESKQSVASSPFLETLKARDYEVLYMTDPIDEYAVQQIKEFEGKKLKCCTKEGLELDEGEDEKKSFEALKEEMEPLCKHIKEVLHDKVEKVVCGTRFTDSPCALVTSEFGWSANMERIMKAQALRDSSITSYMLSKKIMEINPRHSIMKELKARAANDKTDKTVKDLVWLLYDTALLTSGFNLDEPTQFGNRIYRMIKLGLSLDDEEHVEDDSSMPPLDEPVVDSKMEEVD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias237-270Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR940348
EMBL· GenBank· DDBJ
CAI74741.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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