C4A0D9 · BAP1_BRAFL

Function

function

Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By similarity).

Catalytic activity

  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
    EC:3.4.19.12 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, site.

169450100150200250300350400450500550600650
TypeIDPosition(s)Description
Active site91Nucleophile
Active site169Proton donor
Site184Important for enzyme 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
Cellular Componentnucleus
Cellular ComponentPR-DUB complex
Molecular Functionchromatin binding
Molecular Functioncysteine-type deubiquitinase activity
Biological Processchromatin organization
Biological Processnegative regulation of DNA-templated transcription
Biological Processprotein deubiquitination
Biological Processprotein K48-linked deubiquitination
Biological Processregulation of cell cycle
Biological Processregulation of cell growth
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin carboxyl-terminal hydrolase BAP1
  • EC number
  • Alternative names
    • BRCA1-associated protein 1

Gene names

    • Name
      BAP1
    • ORF names
      BRAFLDRAFT_277645

Organism names

Accessions

  • Primary accession
    C4A0D9

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Note: Mainly nuclear. Binds to chromatin.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003958221-694Ubiquitin carboxyl-terminal hydrolase BAP1

Interaction

Subunit

Component of the PR-DUB complex.

Protein-protein interaction databases

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain5-214UCH
Region392-427Disordered
Compositional bias396-415Polar residues
Region454-487Disordered
Compositional bias459-487Polar residues
Domain604-649UCH37-like C-terminal
Region665-694Disordered
Motif678-683Nuclear localization signal

Sequence similarities

Belongs to the peptidase C12 family. BAP1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    694
  • Mass (Da)
    77,164
  • Last updated
    2009-07-28 v1
  • Checksum
    6A4B1902DE067B3D
MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLSKPIEGPVYGFIFLFKWSEERRSRRKVGPSMEESFVVDEDIVNDMFFAQQLIPNSCATHALLSVLLNCPQISLGSTLTRLKYFTRGMGPESKGWAIGNVPEIARAHNSHARPEPRHLPEKQTGISSVRTAEAFHFVSYVTTNDRLFELDGLKPYPIDHGPWGEKEDWTEKFRRVISERIGNATGGENGHDIRFNLMAVVADRRQQYETKLNTLKTNRQIVLEALQQVGGVNTKKSIQYAEVSHVCLHPPKFVPCSDDCAIWDALRYSSALRCSLIQHGCEHPSIPRSDGSTLVSWPSCVTSVNIVVSGHLKYVLLCFSIILDHKLEKLVPARLDPIKVNEPHLTSLIPSAFGRESHHKSKASSTVTSSSAAASSSAAGTDGVQPAEMKPDEFLHPDASRRVGFLEMPWRSDEARPLSIHTGYSKIPSPAPSNESTDTASEIGSAFNSPVRSANRSALQTIPEGSITKQEGDTKTDANIITVCLKRSLSGEGGGPPAKRLHIGDPDMALQRLGSGDSVEGDPMALQGGSGTGDAQQDQHALQAGGARPNMAHAFAPKDLLALLKNVETEIQICEQHLKDEIEKRKKYKVDDCRRTHNYDDFIRTFLRMLAEQGQLSKLVDQHVLVRRRQGVSVGRLHKQRKPDRRRKRARVSDKYRRKKQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias396-415Polar residues
Compositional bias459-487Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG666800
EMBL· GenBank· DDBJ
EEN41742.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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