E2AB17 · F175B_CAMFO

Function

function

Component of the BRISC complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates (PubMed:26344097).
Does not have activity by itself, but the catalytic subunit BRCC3/BRCC36 needs to be associated into a heterotetramer with FAM175B for minimal in vitro activity (PubMed:26344097).
May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity).
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 numa1 (By similarity).

Caution

Expected to lack catalytic 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 Componentspindle pole
Molecular Functionmicrotubule binding
Molecular Functionpolyubiquitin modification-dependent protein binding
Biological Processattachment of spindle microtubules to kinetochore
Biological Processcell division
Biological Processmitotic spindle assembly
Biological Processprotein K63-linked deubiquitination

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    BRISC complex subunit FAM175B
  • Alternative names
    • BRISC complex subunit KIAA0157 homolog

Gene names

    • ORF names
      EAG_01033

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
    E2AB17

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
Mutagenesis177Strongly reduces deubiquitination by the BRISC complex.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004355291-471BRISC complex subunit FAM175B

Interaction

Subunit

Component of the BRISC complex, at least composed of FAM175B/ABRO1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Within the complex, interacts directly with BRCC3/BRCC36. The heterodimer with BRCC3/BRCC36 assembles into a heterotetramer. The BRISC complex binds polyubiquitin.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Domain7-161MPN
Coiled coil245-272
Region343-445Disordered
Compositional bias352-378Polar residues

Sequence similarities

Belongs to the FAM175 family. Abro1 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    52,574
  • Last updated
    2010-11-30 v1
  • Checksum
    A91CB24E699D2DC4
MADSDLLVTISGAALSLLFFENVRSVGNQMGFLLGEALEFIVKTYTDSDNQVETVKIHINVEAIVTCPLADLLHDSTNHINKEKLKDFVRDKSKQVIGWFCFRRNTTNLTLTLKDKLLHKQFASHFSGVNGCKEDFFLTCLLNASTSETSGTHKFRHVFLRHNKRGMFEPISLKINNLGDDASRHDGSDYKPTPVRKSTRTPDSFTKLIESLNLDVARIDGLDSAMLIQKAAEHHLMSLIPKVCESDLEVAELEKQVHELKIKIATQQLAKRLKINGENCDRISKASKDNCFSEKIDSSKKNEVRIGDDACLQREHIPSCTQSVGPNNRTVCRNTAACIAKSAEKSRRAGRSNLQESGNQQQETQNFFTNSRRSIPEIATESICQEGSEISMGRGRGSGRGSHEFTPGMKKIRRTPGTSHMHSSRERSTTPPEQDFSDAECPISSPVLRSYSQVTKKTNLDKCNSMAPLDI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias352-378Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL438234
EMBL· GenBank· DDBJ
EFN69293.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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