P28707 · SBA1_YEAST

Function

function

Acts as a co-chaperone.

Miscellaneous

Present with 33700 molecules/cell in log phase SD medium.

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 Componentnucleus
Molecular FunctionHsp90 protein binding
Molecular Functionprotein-folding chaperone binding
Biological Processchaperone-mediated protein complex assembly
Biological Processpositive regulation of telomere maintenance via telomerase
Biological Processprotein folding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Co-chaperone protein SBA1

Gene names

    • Name
      SBA1
    • ORF names
      YKL518
    • Ordered locus names
      YKL117W

Organism names

Accessions

  • Primary accession
    P28707
  • Secondary accessions
    • D6VXH2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00002189592-216Co-chaperone protein SBA1

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with HSP82.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P28707HSP82 P028297EBI-26838, EBI-8659

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, repeat, region, compositional bias.

TypeIDPosition(s)Description
Domain5-108CS
Repeat141-156
Repeat160-174
Region169-216Disordered
Compositional bias198-216Acidic residues

Sequence similarities

Belongs to the p23/wos2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    216
  • Mass (Da)
    24,082
  • Last updated
    2007-01-23 v3
  • Checksum
    C51CDE30BF2FA945
MSDKVINPQVAWAQRSSTTDPERNYVLITVSIADCDAPELTIKPSYIELKAQSKPHVGDENVHHYQLHIDLYKEIIPEKTMHKVANGQHYFLKLYKKDLESEYWPRLTKEKVKYPYIKTDFDKWVDEDEQDEVEAEGNDAAQGMDFSQMMGGAGGAGGAGGMDFSQMMGGAGGAGSPDMAQLQQLLAQSGGNLDMGDFKENDEEDEEEEIEPEVKA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias198-216Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
S93804
EMBL· GenBank· DDBJ
AAB22000.1
EMBL· GenBank· DDBJ
Genomic DNA
Z28117
EMBL· GenBank· DDBJ
CAA81957.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006944
EMBL· GenBank· DDBJ
DAA09042.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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