BARD1

From Wikipedia, the free encyclopedia

BRCA1 associated RING domain 1

PDB rendering based on 1jm7.

Available structures: 1jm7

Identifiers

Symbol(s)

BARD1;

External IDs

OMIM: 601593 MGI: 1328361 HomoloGene: 400

Gene ontology
Molecular Function:	• RNA binding • ubiquitin-protein ligase activity • protein binding • zinc ion binding • kinase binding • protein homodimerization activity • metal ion binding • protein heterodimerization activity
Cellular Component:	• ubiquitin ligase complex • intracellular • nucleus • cytoplasm • BRCA1-BARD1 complex
Biological Process:	• tissue homeostasis • response to DNA damage stimulus • cell cycle arrest • protein ubiquitination • negative regulation of mRNA 3'-end processing • regulation of phosphorylation • positive regulation of apoptosis • negative regulation of apoptosis • positive regulation of protein catabolic process • negative regulation of protein export from nucleus

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000465 (mRNA)
NP_000456 (protein)

NM_007525 (mRNA)
NP_031551 (protein)

Location

Chr 2: 215.3 - 215.38 Mb

Chr 1: 70.96 - 71.04 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ Entrez Gene: BARD1 BRCA1 associated RING domain 1.

[edit] 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.