BARD1

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BRCA1 associated RING domain 1
PDB rendering based on 1jm7.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols BARD1 ;
External IDs Template:OMIM5 Template:MGI HomoloGene400
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

BRCA1 associated RING domain 1, also known as BARD1, is a human gene.

BARD1 interacts with the N-terminal region of BRCA1. In addition to its ability to bind BRCA1 in vivo and in vitro, BARD1 shares homology with the 2 most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes. The BARD1 protein also contains 3 tandem ankyrin repeats. The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. BARD1 may be the target of oncogenic mutations in breast or ovarian cancer.[1]

References

  1. "Entrez Gene: BARD1 BRCA1 associated RING domain 1".

Further reading

  • Irminger-Finger I, Leung WC (2002). "BRCA1-dependent and independent functions of BARD1". Int. J. Biochem. Cell Biol. 34 (6): 582–7. PMID 11943588.
  • Irminger-Finger I (2003). "3rd Geneva aging workshop 2002: cancer, apoptosis and aging". Biochim. Biophys. Acta. 1653 (1): 41–5. PMID 12781370.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Wu LC, Wang ZW, Tsan JT; et al. (1997). "Identification of a RING protein that can interact in vivo with the BRCA1 gene product". Nat. Genet. 14 (4): 430–40. doi:10.1038/ng1296-430. PMID 8944023.
  • Jin Y, Xu XL, Yang MC; et al. (1997). "Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains". Proc. Natl. Acad. Sci. U.S.A. 94 (22): 12075–80. PMID 9342365.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Thai TH, Du F, Tsan JT; et al. (1998). "Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers". Hum. Mol. Genet. 7 (2): 195–202. PMID 9425226.
  • Yu X, Wu LC, Bowcock AM; et al. (1998). "The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression". J. Biol. Chem. 273 (39): 25388–92. PMID 9738006.
  • Ayi TC, Tsan JT, Hwang LY; et al. (1998). "Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein". Oncogene. 17 (16): 2143–8. doi:10.1038/sj.onc.1202123. PMID 9798686.
  • Meza JE, Brzovic PS, King MC, Klevit RE (1999). "Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1". J. Biol. Chem. 274 (9): 5659–65. PMID 10026184.
  • Dechend R, Hirano F, Lehmann K; et al. (1999). "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators". Oncogene. 18 (22): 3316–23. doi:10.1038/sj.onc.1202717. PMID 10362352.
  • Kleiman FE, Manley JL (1999). "Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50". Science. 285 (5433): 1576–9. PMID 10477523.
  • Scully R, Ganesan S, Vlasakova K; et al. (2000). "Genetic analysis of BRCA1 function in a defined tumor cell line". Mol. Cell. 4 (6): 1093–9. PMID 10635334.
  • Yu X, Baer R (2000). "Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor". J. Biol. Chem. 275 (24): 18541–9. doi:10.1074/jbc.M909494199. PMID 10764811.
  • Kleiman FE, Manley JL (2001). "The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression". Cell. 104 (5): 743–53. PMID 11257228.
  • Hashizume R, Fukuda M, Maeda I; et al. (2001). "The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation". J. Biol. Chem. 276 (18): 14537–40. doi:10.1074/jbc.C000881200. PMID 11278247.
  • Wang Q, Zhang H, Guerrette S; et al. (2001). "Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1". Oncogene. 20 (34): 4640–9. doi:10.1038/sj.onc.1204625. PMID 11498787.
  • Chiba N, Parvin JD (2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. PMID 11504724.
  • Brzovic PS, Meza JE, King MC, Klevit RE (2001). "BRCA1 RING domain cancer-predisposing mutations. Structural consequences and effects on protein-protein interactions". J. Biol. Chem. 276 (44): 41399–406. doi:10.1074/jbc.M106551200. PMID 11526114.

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