E2AB17 · F175B_CAMFO
- ProteinBRISC complex subunit FAM175B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | spindle pole | |
Molecular Function | microtubule binding | |
Molecular Function | polyubiquitin modification-dependent protein binding | |
Biological Process | attachment of spindle microtubules to kinetochore | |
Biological Process | cell division | |
Biological Process | mitotic spindle assembly | |
Biological Process | protein K63-linked deubiquitination |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameBRISC complex subunit FAM175B
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Formicinae > Camponotus
Accessions
- Primary accessionE2AB17
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 177 | Strongly reduces deubiquitination by the BRISC complex. | ||||
Sequence: N → R |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435529 | 1-471 | BRISC complex subunit FAM175B | |||
Sequence: MADSDLLVTISGAALSLLFFENVRSVGNQMGFLLGEALEFIVKTYTDSDNQVETVKIHINVEAIVTCPLADLLHDSTNHINKEKLKDFVRDKSKQVIGWFCFRRNTTNLTLTLKDKLLHKQFASHFSGVNGCKEDFFLTCLLNASTSETSGTHKFRHVFLRHNKRGMFEPISLKINNLGDDASRHDGSDYKPTPVRKSTRTPDSFTKLIESLNLDVARIDGLDSAMLIQKAAEHHLMSLIPKVCESDLEVAELEKQVHELKIKIATQQLAKRLKINGENCDRISKASKDNCFSEKIDSSKKNEVRIGDDACLQREHIPSCTQSVGPNNRTVCRNTAACIAKSAEKSRRAGRSNLQESGNQQQETQNFFTNSRRSIPEIATESICQEGSEISMGRGRGSGRGSHEFTPGMKKIRRTPGTSHMHSSRERSTTPPEQDFSDAECPISSPVLRSYSQVTKKTNLDKCNSMAPLDI |
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
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-161 | MPN | ||||
Sequence: LVTISGAALSLLFFENVRSVGNQMGFLLGEALEFIVKTYTDSDNQVETVKIHINVEAIVTCPLADLLHDSTNHINKEKLKDFVRDKSKQVIGWFCFRRNTTNLTLTLKDKLLHKQFASHFSGVNGCKEDFFLTCLLNASTSETSGTHKFRHVFLR | ||||||
Coiled coil | 245-272 | |||||
Sequence: ESDLEVAELEKQVHELKIKIATQQLAKR | ||||||
Region | 343-445 | Disordered | ||||
Sequence: AEKSRRAGRSNLQESGNQQQETQNFFTNSRRSIPEIATESICQEGSEISMGRGRGSGRGSHEFTPGMKKIRRTPGTSHMHSSRERSTTPPEQDFSDAECPISS | ||||||
Compositional bias | 352-378 | Polar residues | ||||
Sequence: SNLQESGNQQQETQNFFTNSRRSIPEI |
Sequence similarities
Belongs to the FAM175 family. Abro1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length471
- Mass (Da)52,574
- Last updated2010-11-30 v1
- ChecksumA91CB24E699D2DC4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 352-378 | Polar residues | ||||
Sequence: SNLQESGNQQQETQNFFTNSRRSIPEI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL438234 EMBL· GenBank· DDBJ | EFN69293.1 EMBL· GenBank· DDBJ | Genomic DNA |