Q21209 · BARD1_CAEEL
- ProteinBRCA1-associated RING domain protein 1
- Genebrd-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids702 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity (PubMed:16628214).
When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase (PubMed:16628214).
Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites (PubMed:16628214).
To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:14711411, PubMed:30383754).
Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation for example (PubMed:14711411, PubMed:30383754).
In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability (PubMed:14711411).
When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase (PubMed:16628214).
Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites (PubMed:16628214).
To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:14711411, PubMed:30383754).
Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation for example (PubMed:14711411, PubMed:30383754).
In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability (PubMed:14711411).
Catalytic activity
Activity regulation
E3 ubiquitin-protein ligase activity of CeBCD complexes occurs at DNA damage sites. Following DNA damage, E3 ubiquitin-protein ligase activity is reduced by caffeine treatment (inhibitor of ATM and ATK kinase activity).
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | BRCA1-A complex | |
Cellular Component | BRCA1-BARD1 complex | |
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | DNA damage response | |
Biological Process | DNA repair | |
Biological Process | positive regulation of double-strand break repair via homologous recombination | |
Biological Process | protein K6-linked ubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBRCA1-associated RING domain protein 1
- EC number
- Short namesBARD1 ; Ce-BRD-1 ; Cebrd-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ21209
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Co-localizes with brc-1 in germline nuclei at meiotic prophase I (PubMed:30383754).
At the transition between mid- and late- pachytene, localization together with brc-1 is less diffuse and becomes a linear pattern along the chromosomes (PubMed:30383754).
In late pachytene nuclei, co-localizes with brc-1 at crossover sites and the short arm of homologous chromosomes (PubMed:30383754).
At the transition between mid- and late- pachytene, localization together with brc-1 is less diffuse and becomes a linear pattern along the chromosomes (PubMed:30383754).
In late pachytene nuclei, co-localizes with brc-1 at crossover sites and the short arm of homologous chromosomes (PubMed:30383754).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
DNA damage repair defects following ionizing radiation with reduced ubiquitination at DNA damage sites (PubMed:16628214).
RNAi-mediated knockdown results in elevated levels of chromosome non-disjunction that manifest as a high incidence of males, impaired progeny survival and chromosome fragmentation after irradiation and elevated levels of p53-dependent germ cell death before and after irradiation (PubMed:14711411).
Absence of S-phase checkpoint function
RNAi-mediated knockdown results in elevated levels of chromosome non-disjunction that manifest as a high incidence of males, impaired progeny survival and chromosome fragmentation after irradiation and elevated levels of p53-dependent germ cell death before and after irradiation (PubMed:14711411).
Absence of S-phase checkpoint function
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000403993 | 1-702 | BRCA1-associated RING domain protein 1 | ||
Post-translational modification
Autoubiquitinated.
Phosphorylation of CeBCD complexes is required for E3 ubiquitin-protein ligase activity.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Heterodimer (via RING-type zinc finger) with brc-1 to form the core CeBCD complex (PubMed:16628214).
Brc-1-brd-1 heterodimer-containing CeBCD complexes bound to chromatin are activated as an E3-ubiquitin ligase in response to DNA damage (PubMed:16628214).
The heterodimer interacts with the recombinase rad-51 following ionizing irradiation; the interaction is direct (PubMed:16628214).
The heterodimer interacts the E2-ubiquitin-conjugating enzyme let-70 following ionizing irradiation (PubMed:16628214).
The heterodimer interacts with the pro-crossover proteins msh-5 and syp-3 (PubMed:30383754).
Interacts with smt-3, tac-1 and ubc-9 (PubMed:14711411).
Brc-1-brd-1 heterodimer-containing CeBCD complexes bound to chromatin are activated as an E3-ubiquitin ligase in response to DNA damage (PubMed:16628214).
The heterodimer interacts with the recombinase rad-51 following ionizing irradiation; the interaction is direct (PubMed:16628214).
The heterodimer interacts the E2-ubiquitin-conjugating enzyme let-70 following ionizing irradiation (PubMed:16628214).
The heterodimer interacts with the pro-crossover proteins msh-5 and syp-3 (PubMed:30383754).
Interacts with smt-3, tac-1 and ubc-9 (PubMed:14711411).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q21209 | brc-1 B6VQ60 | 4 | EBI-3895480, EBI-3895496 | |
BINARY | Q21209 | smo-1 P55853 | 3 | EBI-3895480, EBI-313647 | |
BINARY | Q21209 | ubc-9 Q95017 | 4 | EBI-3895480, EBI-328938 |
Complex viewer
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger, compositional bias, region, repeat, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Zinc finger | 18-67 | RING-type | |||
Compositional bias | 153-176 | Basic and acidic residues | |||
Region | 153-205 | Disordered | |||
Compositional bias | 185-200 | Basic and acidic residues | |||
Region | 281-346 | Disordered | |||
Compositional bias | 290-323 | Basic and acidic residues | |||
Repeat | 347-376 | ANK 1 | |||
Repeat | 379-408 | ANK 2 | |||
Repeat | 413-442 | ANK 3 | |||
Domain | 601-702 | BRCT | |||
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length702
- Mass (Da)78,804
- Last updated2010-08-10 v3
- Checksum2BEE4F198D1180FE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 153-176 | Basic and acidic residues | |||
Compositional bias | 185-200 | Basic and acidic residues | |||
Compositional bias | 290-323 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FO081584 EMBL· GenBank· DDBJ | CCD72622.1 EMBL· GenBank· DDBJ | Genomic DNA |