Q21209 · BARD1_CAEEL

  • Protein
    BRCA1-associated RING domain protein 1
  • Gene
    brd-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

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

AspectTerm
Cellular ComponentBRCA1-A complex
Cellular ComponentBRCA1-BARD1 complex
Cellular Componentchromosome
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Biological ProcessDNA damage response
Biological ProcessDNA repair
Biological Processpositive regulation of double-strand break repair via homologous recombination
Biological Processprotein K6-linked ubiquitination
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    BRCA1-associated RING domain protein 1
  • EC number
  • Short names
    BARD1
    ; Ce-BRD-1
    ; Cebrd-1
  • Alternative names
    • RING-type E3 ubiquitin transferase BARD1

Gene names

    • Name
      brd-1
    • ORF names
      K04C2.4

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q21209

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Chromosome
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).

Keywords

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

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004039931-702BRCA1-associated RING domain protein 1

Post-translational modification

Autoubiquitinated.
Phosphorylation of CeBCD complexes is required for E3 ubiquitin-protein ligase activity.

Keywords

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q21209brc-1 B6VQ604EBI-3895480, EBI-3895496
BINARY Q21209smo-1 P558533EBI-3895480, EBI-313647
BINARY Q21209ubc-9 Q950174EBI-3895480, EBI-328938

Complex viewer

View interactors in UniProtKB
View CPX-375 in Complex Portal

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for zinc finger, compositional bias, region, repeat, domain.

Type
IDPosition(s)Description
Zinc finger18-67RING-type
Compositional bias153-176Basic and acidic residues
Region153-205Disordered
Compositional bias185-200Basic and acidic residues
Region281-346Disordered
Compositional bias290-323Basic and acidic residues
Repeat347-376ANK 1
Repeat379-408ANK 2
Repeat413-442ANK 3
Domain601-702BRCT

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    702
  • Mass (Da)
    78,804
  • Last updated
    2010-08-10 v3
  • Checksum
    2BEE4F198D1180FE
MFENTKKALETFRTAIECVKCKKPRGDLQYLGSSCKHAYCWECIATFQQKPSGKRSSVARHMCPSCAFPLDTSKITEAHMLKTCFDTLSELNDLLQKVGTTSLTQAEFACTQNIFNKEKTPADAVEKFLETQAHMPDEMGQLGEEDDDLMCKDENRENSNSPELDIFHDYSKEASPTRNSTKRPSTVSVHERKPKRSSILKTSVKNEPAAPVVDLFASQVPQRTHQNDLLTPFIERRSTAPAATGVATYAQAFGSSSNPVKAEIIEEDIFSKAIPLTKRQASMSASAKKQPKLEPEEPEEVPSTSRSRKNSIKSDKIERRSQSPMSFGEKSMSVKSEQRRSSYGTRRGEAVLVNSIRNNRIPQLRSAVEAGTCVNEKEDGKTPLYVAVENSSLEAVKILVEAGAVINASCGSTLETTLHEAVRRQNTQIVEYLLSKGASIKIRNIAGKTVEEMAKSDPKIRKIIEKFKTEQRVLQPVVAPPKSRLHFVQLIDEKMLTESEKRKLPGKINIVPADMDSPTHVVVTVDLKTRVLNINKEHIGEILKAIIKSGMIVSRDWLRACIIDPSKVDDDRSYMVQKVRWMEGEVFENTIEQWKKTITKMQPKLFAGCKFFIPKPKYNFLDRPALFEIIRSAGGQAAAREPIIDEKDPPPYHNANLKPNFVLYSLTHDIGDKFRDCTKYNLVSEQWLIEAILGCSITTPPH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias153-176Basic and acidic residues
Compositional bias185-200Basic and acidic residues
Compositional bias290-323Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FO081584
EMBL· GenBank· DDBJ
CCD72622.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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