BRIP1

BRCA1 interacting protein C-terminal helicase 1
Identifiers
Symbols	BRIP1; BACH1; FANCJ; FLJ90232; MGC126521; MGC126523; OF
External IDs	OMIM: 605882 MGI: 2442836 HomoloGene: 32766 GeneCards: BRIP1 Gene
EC number	3.6.4.13
Gene Ontology Molecular function • nucleotide binding • DNA binding • ATP-dependent DNA helicase activity • helicase activity • protein binding • ATP binding • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Cellular component • nucleus • nucleus • cytoplasm Biological process • DNA damage checkpoint • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process • double-strand break repair • regulation of transcription from RNA polymerase II promoter Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	83990	237911
Ensembl	ENSG00000136492	ENSMUSG00000034329
UniProt	Q9BX63	Q3TER9
RefSeq (mRNA)	NM_032043	NM_178309.2
RefSeq (protein)	NP_114432	NP_840094.1
Location (UCSC)	Chr 17: 59.76 – 59.94 Mb	Chr 11: 85.87 – 86.01 Mb
PubMed search	[1]	[2]

Fanconi anemia group J protein is a protein that in humans is encoded by the BRCA1-interacting protein 1 (BRIP1) gene.^[1][2][3]

The protein encoded by this gene is a member of the RecQ DEAH helicase family and interacts with the BRCT repeats of breast cancer, type 1 (BRCA1). The bound complex is important in the normal double-strand break repair function of breast cancer, type 1 (BRCA1). This gene may be a target of germline cancer-inducing mutations.^[3]

This protein also appears to be important in ovarian cancer where it seems to act as an antioncogene.^[4]

Interactions

BRIP1 has been shown to interact with BRCA1.^{[5][6][7][8][9][10]}

References

1. ^ Menichini P, Linial M (Oct 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutat Res 487 (1–2): 67–71. PMID 11595410. 
2. ^ Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM (Apr 2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell 105 (1): 149–60. doi:10.1016/S0092-8674(01)00304-X. PMID 11301010. 
3. ^ ^{a b} "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83990. 
4. ^ Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, Besenbacher S, Lundin P, Stacey SN, Gudmundsson J, Magnusson OT, le Roux L, Orlygsdottir G, Helgadottir HT, Johannsdottir H, Gylfason A, Tryggvadottir L, Jonasson JG, de Juan A, Ortega E, Ramon-Cajal JM, García-Prats MD, Mayordomo C, Panadero A, Rivera F, Aben KK, van Altena AM, Massuger LF, Aavikko M, Kujala PM, Staff S, Aaltonen LA, Olafsdottir K, Bjornsson J, Kong A, Salvarsdottir A, Saemundsson H, Olafsson K, Benediktsdottir KR, Gulcher J, Masson G, Kiemeney LA, Mayordomo JI, Thorsteinsdottir U, Stefansson K (2011) Mutations in BRIP1 confer high risk of ovarian cancer. Nat Genet doi: 10.1038/ng.955.
5. ^ Botuyan, Maria Victoria E; Nominé Yves, Yu Xiaochun, Juranic Nenad, Macura Slobodan, Chen Junjie, Mer Georges (Jul. 2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure (United States) 12 (7): 1137–46. doi:10.1016/j.str.2004.06.002. ISSN 0969-2126. PMID 15242590. 
6. ^ Joo, Woo S; Jeffrey Philip D, Cantor Sharon B, Finnin Michael S, Livingston David M, Pavletich Nikola P (Mar. 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes Dev. (United States) 16 (5): 583–93. doi:10.1101/gad.959202. ISSN 0890-9369. PMC 155350. PMID 11877378. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=155350. 
7. ^ Yu, Xiaochun; Chini Claudia Christiano Silva, He Miao, Mer Georges, Chen Junjie (Oct. 2003). "The BRCT domain is a phospho-protein binding domain". Science (United States) 302 (5645): 639–42. doi:10.1126/science.1088753. PMID 14576433. 
8. ^ Rodriguez, Maria; Yu Xiaochun, Chen Junjie, Songyang Zhou (Dec. 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. (United States) 278 (52): 52914–8. doi:10.1074/jbc.C300407200. ISSN 0021-9258. PMID 14578343. 
9. ^ Clapperton, Julie A; Manke Isaac A, Lowery Drew M, Ho Timmy, Haire Lesley F, Yaffe Michael B, Smerdon Stephen J (Jun. 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nat. Struct. Mol. Biol. (United States) 11 (6): 512–8. doi:10.1038/nsmb775. ISSN 1545-9993. PMID 15133502. 
10. ^ Wada, Osamu; Oishi Hajime, Takada Ichiro, Yanagisawa Junn, Yano Tetsu, Kato Shigeaki (Aug. 2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene (England) 23 (35): 6000–5. doi:10.1038/sj.onc.1207786. ISSN 0950-9232. PMID 15208681. 

Further reading

• Kobayashi A, Yamagiwa H, Hoshino H et al. (2000). "A Combinatorial Code for Gene Expression Generated by Transcription Factor Bach2 and MAZR (MAZ-Related Factor) through the BTB/POZ Domain". Mol. Cell. Biol. 20 (5): 1733–46. doi:10.1128/MCB.20.5.1733-1746.2000. PMC 85356. PMID 10669750. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85356. 
• Joo WS, Jeffrey PD, Cantor SB et al. (2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes Dev. 16 (5): 583–93. doi:10.1101/gad.959202. PMC 155350. PMID 11877378. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=155350. 
• Luo L, Lei H, Du Q et al. (2002). "No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22". Int. J. Cancer 98 (4): 638–9. doi:10.1002/ijc.10214. PMID 11920628. 
• Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Karppinen SM, Vuosku J, Heikkinen K et al. (2003). "No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families". Eur. J. Cancer 39 (3): 366–71. doi:10.1016/S0959-8049(02)00498-7. PMID 12565990. 
• Rutter JL, Smith AM, Dávila MR et al. (2004). "Mutational analysis of the BRCA1-interacting genes ZNF350/ZBRK1 and BRIP1/BACH1 among BRCA1 and BRCA2-negative probands from breast-ovarian cancer families and among early-onset breast cancer cases and reference individuals". Hum. Mutat. 22 (2): 121–8. doi:10.1002/humu.10238. PMID 12872252. 
• Suzuki H, Tashiro S, Sun J et al. (2004). "Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene". J. Biol. Chem. 278 (49): 49246–53. doi:10.1074/jbc.M306764200. PMID 14504288. 
• Yu X, Chini CC, He M et al. (2003). "The BRCT domain is a phospho-protein binding domain". Science 302 (5645): 639–42. doi:10.1126/science.1088753. PMID 14576433. 
• Rodriguez M, Yu X, Chen J, Songyang Z (2004). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi:10.1074/jbc.C300407200. PMID 14578343. 
• Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Cantor S, Drapkin R, Zhang F et al. (2004). "The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations". Proc. Natl. Acad. Sci. U.S.A. 101 (8): 2357–62. doi:10.1073/pnas.0308717101. PMC 356955. PMID 14983014. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=356955. 
• Shiozaki EN, Gu L, Yan N, Shi Y (2004). "Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling". Mol. Cell 14 (3): 405–12. doi:10.1016/S1097-2765(04)00238-2. PMID 15125843. 
• Clapperton JA, Manke IA, Lowery DM et al. (2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nat. Struct. Mol. Biol. 11 (6): 512–8. doi:10.1038/nsmb775. PMID 15133502. 
• Wada O, Oishi H, Takada I et al. (2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene 23 (35): 6000–5. doi:10.1038/sj.onc.1207786. PMID 15208681. 
• Botuyan MV, Nominé Y, Yu X et al. (2005). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure 12 (7): 1137–46. doi:10.1016/j.str.2004.06.002. PMID 15242590. 
• Beausoleil SA, Jedrychowski M, Schwartz D et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446. 
• Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Gupta R, Sharma S, Sommers JA et al. (2005). "Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer". J. Biol. Chem. 280 (27): 25450–60. doi:10.1074/jbc.M501995200. PMID 15878853.