E2AXC7 · BRCC3_CAMFO

Function

function

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097).
Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity).
Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

125320406080100120140160180200220240
TypeIDPosition(s)Description
Binding site94Zn2+ (UniProtKB | ChEBI); catalytic
Binding site96Zn2+ (UniProtKB | ChEBI); catalytic
Binding site107Zn2+ (UniProtKB | ChEBI); catalytic

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 ComponentBRCA1-A complex
Cellular ComponentBRISC complex
Cellular Componentcytoplasm
Cellular Componentspindle pole
Molecular Functioncysteine-type deubiquitinase activity
Molecular Functionmetal ion binding
Molecular Functionmetal-dependent deubiquitinase activity
Molecular Functionpolyubiquitin modification-dependent protein binding
Biological Processcell division
Biological Processdouble-strand break repair
Biological Processpositive regulation of NLRP3 inflammasome complex assembly
Biological Processprotein K63-linked deubiquitination
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Lys-63-specific deubiquitinase BRCC36
  • EC number

Gene names

    • Name
      BRCC3
    • Synonyms
      BRCC36
    • ORF names
      EAG_15736

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Formicinae > Camponotus

Accessions

  • Primary accession
    E2AXC7

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Note: A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis30Abolishes metalloprotease activity.
Mutagenesis94-96Abolishes zinc binding and disrupts the structure of the active site region.
Mutagenesis99Nearly abolishes metalloprotease activity.
Mutagenesis117Nearly abolishes metalloprotease activity.
Mutagenesis183Abolishes metalloprotease activity; when associated with A-186.
Mutagenesis186Abolishes metalloprotease activity; when associated with A-183.
Mutagenesis205Abolishes tetramerization and metalloprotease activity; when associated with D-212.
Mutagenesis212Abolishes tetramerization and metalloprotease activity; when associated with D-205.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004355301-253Lys-63-specific deubiquitinase BRCC36

Interaction

Subunit

Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Within the complex, interacts directly with ABRAXAS2. The heterodimer with ABRAXAS2 assembles into a heterotetramer. The BRISC complex binds polyubiquitin.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, motif, coiled coil.

TypeIDPosition(s)Description
Domain9-145MPN
Motif94-107JAMM motif
Coiled coil227-249

Sequence similarities

Belongs to the peptidase M67A family. BRCC36 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    253
  • Mass (Da)
    28,745
  • Last updated
    2010-11-30 v1
  • Checksum
    CD6A4911B66BABFB
MDDSSLQKVELQTDVYMVCLQHALSTENFEVMGLLIGNFACGIAKISAVIILRRLDKKKDRVEISSEQLLKAAAEAERLTVELNRPMRVLGWYHSHPHITVCPSHVDVRTQATYQTMDHSFVGLIFSVFSEGKESKEHEIFLNCFQSDNGEATEIPLEIVHTPDISDRCLRTMTDLSKILVQEEEDMAEACKDHPDVLASIHNNAVRTRALIHITDIITKPLVQTFEKRIALNKLRATHLQRQLQELQKMCNG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL443548
EMBL· GenBank· DDBJ
EFN61907.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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