BARD1

BARD1

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

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: BARD1 BRCA1 associated RING domain 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=580| accessdate = ]

References

Further reading

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

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