BARD1

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BRCA1 associated RING domain 1

PDB rendering based on 1jm7.
Identifiers
Symbols BARD1;
External IDs OMIM: 601593 MGI: 1328361 HomoloGene: 400 GeneCards: BARD1 Gene
RNA expression pattern
PBB GE BARD1 205345 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 580 12021
Ensembl ENSG00000138376 ENSMUSG00000026196
UniProt Q99728 O70445
RefSeq (mRNA) NM_000465.2 NM_007525.3
RefSeq (protein) NP_000456.2 NP_031551.1
Location (UCSC) Chr 2:
215.59 – 215.67 Mb		 Chr 1:
71.07 – 71.15 Mb
PubMed search [1] [2]
This box:

BRCA1-associated RING domain protein 1 is a protein that in humans is encoded by the BARD1 gene.[1][2][3]

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.[4]

[edit] Interactions

BARD1 has been shown to interact with BRE,[5] UBE2D1,[5][6][7][8][9][10][11][12] CSTF2,[13][14] BRCC3,[5] RAD51,[5] BCL3,[15] TACC1,[16] Ewing sarcoma breakpoint region 1,[17] FANCD2,[11] H2AFX,[6][8] CSTF1,[13][14] NPM1,[9] BRCA2,[5][16] BRCA1,[1][5][6][10][12][13][18][7][19][3][20][8][21][9][22][11][23][14][24][25][26][16][27][28][29][30][31][32][33][34][35][36] P53[5] and Aurora B kinase.[16]

[edit] References

  1. ^ a b Wu LC, Wang ZW, Tsan JT, Spillman MA, Phung A, Xu XL, Yang MC, Hwang LY, Bowcock AM, Baer R (January 1997). "Identification of a RING protein that can interact in vivo with the BRCA1 gene product". Nat Genet 14 (4): 430–440. doi:10.1038/ng1296-430. PMID 8944023. 
  2. ^ Thai TH, Du F, Tsan JT, Jin Y, Phung A, Spillman MA, Massa HF, Muller CY, Ashfaq R, Mathis JM, Miller DS, Trask BJ, Baer R, Bowcock AM (March 1998). "Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers". Hum Mol Genet 7 (2): 195–202. doi:10.1093/hmg/7.2.195. PMID 9425226. 
  3. ^ a b Fabbro M, Savage K, Hobson K, Deans AJ, Powell SN, McArthur GA, Khanna KK (July 2004). "BRCA1-BARD1 complexes are required for p53Ser-15 phosphorylation and a G1/S arrest following ionizing radiation-induced DNA damage". J Biol Chem 279 (30): 31251–31258. doi:10.1074/jbc.M405372200. PMID 15159397. 
  4. ^ "Entrez Gene: BARD1 BRCA1 associated RING domain 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=580. 
  5. ^ a b c d e f g Dong, Yuanshu; Hakimi Mohamed-Ali, Chen Xiaowei, Kumaraswamy Easwari, Cooch Neil S, Godwin Andrew K, Shiekhattar Ramin (November 2003). "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair". Mol. Cell (United States) 12 (5): 1087–1099. doi:10.1016/S1097-2765(03)00424-6. ISSN 1097-2765. PMID 14636569. 
  6. ^ a b c Mallery, Donna L; Vandenberg Cassandra J, Hiom Kevin (Dec. 2002). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". EMBO J. (England) 21 (24): 6755–6762. doi:10.1093/emboj/cdf691. ISSN 0261-4189. PMC 139111. PMID 12485996. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139111. 
  7. ^ a b Kentsis, Alex; Gordon Ronald E, Borden Katherine L B (November 2002). "Control of biochemical reactions through supramolecular RING domain self-assembly". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (24): 15404–15409. doi:10.1073/pnas.202608799. ISSN 0027-8424. PMC 137729. PMID 12438698. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=137729. 
  8. ^ a b c Chen, Angus; Kleiman Frida E, Manley James L, Ouchi Toru, Pan Zhen-Qiang (June 2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase". J. Biol. Chem. (United States) 277 (24): 22085–22092. doi:10.1074/jbc.M201252200. ISSN 0021-9258. PMID 11927591. 
  9. ^ a b c Sato, Ko; Hayami Ryosuke, Wu Wenwen, Nishikawa Toru, Nishikawa Hiroyuki, Okuda Yoshiko, Ogata Haruki, Fukuda Mamoru, Ohta Tomohiko (July 2004). "Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. (United States) 279 (30): 30919–30922. doi:10.1074/jbc.C400169200. ISSN 0021-9258. PMID 15184379. 
  10. ^ a b Wu-Baer, Foon; Lagrazon Karen, Yuan Wei, Baer Richard (September 2003). "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin". J. Biol. Chem. (United States) 278 (37): 34743–34746. doi:10.1074/jbc.C300249200. ISSN 0021-9258. PMID 12890688. 
  11. ^ a b c Vandenberg, Cassandra J; Gergely Fanni, Ong Chong Yi, Pace Paul, Mallery Donna L, Hiom Kevin, Patel Ketan J (July 2003). "BRCA1-independent ubiquitination of FANCD2". Mol. Cell (United States) 12 (1): 247–254. doi:10.1016/S1097-2765(03)00281-8. ISSN 1097-2765. PMID 12887909. 
  12. ^ a b Hashizume, R; Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T (May 2001). "The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation". J. Biol. Chem. (United States) 276 (18): 14537–14540. doi:10.1074/jbc.C000881200. ISSN 0021-9258. PMID 11278247. 
  13. ^ a b c Kleiman, F E; Manley J L (March 2001). "The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression". Cell (United States) 104 (5): 743–753. doi:10.1016/S0092-8674(01)00270-7. ISSN 0092-8674. PMID 11257228. 
  14. ^ a b c Kleiman, F E; Manley J L (September 1999). "Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50". Science (UNITED STATES) 285 (5433): 1576–1579. doi:10.1126/science.285.5433.1576. ISSN 0036-8075. PMID 10477523. 
  15. ^ Dechend, R; Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn F G, Scheidereit C, Leutz A (June 1999). "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators". Oncogene (ENGLAND) 18 (22): 3316–3323. doi:10.1038/sj.onc.1202717. ISSN 0950-9232. PMID 10362352. 
  16. ^ a b c d Ryser, Stephan; Dizin Eva, Jefford Charles Edward, Delaval Bénédicte, Gagos Sarantis, Christodoulidou Agni, Krause Karl-Heinz, Birnbaum Daniel, Irminger-Finger Irmgard (February 2009). "Distinct roles of BARD1 isoforms in mitosis: full-length BARD1 mediates Aurora B degradation, cancer-associated BARD1beta scaffolds Aurora B and BRCA2". Cancer Res. (United States) 69 (3): 1125–1134. doi:10.1158/0008-5472.CAN-08-2134. PMID 19176389. 
  17. ^ Spahn, Laura; Petermann Robert, Siligan Christine, Schmid Johannes A, Aryee Dave N T, Kovar Heinrich (August 2002). "Interaction of the EWS NH2 terminus with BARD1 links the Ewing's sarcoma gene to a common tumor suppressor pathway". Cancer Res. (United States) 62 (16): 4583–7. ISSN 0008-5472. PMID 12183411. 
  18. ^ Wang, Q; Zhang H, Guerrette S, Chen J, Mazurek A, Wilson T, Slupianek A, Skorski T, Fishel R, Greene M I (August 2001). "Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1". Oncogene (England) 20 (34): 4640–4649. doi:10.1038/sj.onc.1204625. ISSN 0950-9232. PMID 11498787. 
  19. ^ Fabbro, Megan; Rodriguez Jose A, Baer Richard, Henderson Beric R (June 2002). "BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export". J. Biol. Chem. (United States) 277 (24): 21315–21324. doi:10.1074/jbc.M200769200. ISSN 0021-9258. PMID 11925436. 
  20. ^ Rodriguez, José Antonio; Schüchner Stefan, Au Wendy W Y, Fabbro Megan, Henderson Beric R (March 2004). "Nuclear-cytoplasmic shuttling of BARD1 contributes to its proapoptotic activity and is regulated by dimerization with BRCA1". Oncogene (England) 23 (10): 1809–1820. doi:10.1038/sj.onc.1207302. ISSN 0950-9232. PMID 14647430. 
  21. ^ Brzovic, Peter S; Keeffe Jennifer R, Nishikawa Hiroyuki, Miyamoto Keiko, Fox David, Fukuda Mamoru, Ohta Tomohiko, Klevit Rachel (May 2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex". Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (10): 5646–5651. doi:10.1073/pnas.0836054100. ISSN 0027-8424. PMC 156255. PMID 12732733. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156255. 
  22. ^ Nishikawa, Hiroyuki; Ooka Seido, Sato Ko, Arima Kei, Okamoto Joji, Klevit Rachel E, Fukuda Mamoru, Ohta Tomohiko (February 2004). "Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. (United States) 279 (6): 3916–3924. doi:10.1074/jbc.M308540200. ISSN 0021-9258. PMID 14638690. 
  23. ^ Chiba, N; Parvin J D (October 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. (United States) 276 (42): 38549–38554. doi:10.1074/jbc.M105227200. ISSN 0021-9258. PMID 11504724. 
  24. ^ Morris, Joanna R; Keep Nicholas H, Solomon Ellen (March 2002). "Identification of residues required for the interaction of BARD1 with BRCA1". J. Biol. Chem. (United States) 277 (11): 9382–9386. doi:10.1074/jbc.M109249200. ISSN 0021-9258. PMID 11773071. 
  25. ^ Brzovic, P S; Meza J E, King M C, Klevit R E (November 2001). "BRCA1 RING domain cancer-predisposing mutations. Structural consequences and effects on protein-protein interactions". J. Biol. Chem. (United States) 276 (44): 41399–41406. doi:10.1074/jbc.M106551200. ISSN 0021-9258. PMID 11526114. 
  26. ^ Xia, Yan; Pao Gerald M, Chen Hong-Wu, Verma Inder M, Hunter Tony (February 2003). "Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein". J. Biol. Chem. (United States) 278 (7): 5255–5263. doi:10.1074/jbc.M204591200. ISSN 0021-9258. PMID 12431996. 
  27. ^ Meza, J E; Brzovic P S, King M C, Klevit R E (February 1999). "Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1". J. Biol. Chem. (UNITED STATES) 274 (9): 5659–5665. doi:10.1074/jbc.274.9.5659. ISSN 0021-9258. PMID 10026184. 
  28. ^ Brzovic, P S; Rajagopal P, Hoyt D W, King M C, Klevit R E (October 2001). "Structure of a BRCA1-BARD1 heterodimeric RING-RING complex". Nat. Struct. Biol. (United States) 8 (10): 833–837. doi:10.1038/nsb1001-833. ISSN 1072-8368. PMID 11573085. 
  29. ^ Yu, X; Wu L C, Bowcock A M, Aronheim A, Baer R (September 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. (UNITED STATES) 273 (39): 25388–25392. doi:10.1074/jbc.273.39.25388. ISSN 0021-9258. PMID 9738006. 
  30. ^ Jin, Y; Xu X L, Yang M C, Wei F, Ayi T C, Bowcock A M, Baer R (October 1997). "Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (22): 12075–12080. doi:10.1073/pnas.94.22.12075. ISSN 0027-8424. PMC 23707. PMID 9342365. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23707. 
  31. ^ Scully, R; Ganesan S, Vlasakova K, Chen J, Socolovsky M, Livingston D M (Dec. 1999). "Genetic analysis of BRCA1 function in a defined tumor cell line". Mol. Cell (UNITED STATES) 4 (6): 1093–1099. doi:10.1016/S1097-2765(00)80238-5. ISSN 1097-2765. PMID 10635334. 
  32. ^ Tascou, S; Kang T W, Trappe R, Engel W, Burfeind P (September 2003). "Identification and characterization of NIF3L1 BP1, a novel cytoplasmic interaction partner of the NIF3L1 protein". Biochem. Biophys. Res. Commun. (United States) 309 (2): 440–448. doi:10.1016/j.bbrc.2003.07.008. ISSN 0006-291X. PMID 12951069. 
  33. ^ Benezra, Miriam; Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D (July 2003). "BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit". J. Biol. Chem. (United States) 278 (29): 26333–26341. doi:10.1074/jbc.M303076200. ISSN 0021-9258. PMID 12700228. 
  34. ^ Cantor, S B; Bell D W, Ganesan S, Kass E M, Drapkin R, Grossman S, Wahrer D C, Sgroi D C, Lane W S, Haber D A, Livingston D M (April 2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell (United States) 105 (1): 149–160. doi:10.1016/S0092-8674(01)00304-X. ISSN 0092-8674. PMID 11301010. 
  35. ^ Wang, Q; Zhang H, Kajino K, Greene M I (October 1998). "BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells". Oncogene (ENGLAND) 17 (15): 1939–1948. doi:10.1038/sj.onc.1202403. ISSN 0950-9232. PMID 9788437. 
  36. ^ Nishikawa, Hiroyuki; Wu Wenwen, Koike Ayaka, Kojima Ryoko, Gomi Hiromichi, Fukuda Mamoru, Ohta Tomohiko (January 2009). "BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity". Cancer Res. (United States) 69 (1): 111–119. doi:10.1158/0008-5472.CAN-08-3355. PMID 19117993. 

[edit] Further reading

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