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BRIP1
   
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BRCA1 interacting protein C-terminal helicase 1
Identifiers
Symbols BRIP1; BACH1; OF; FANCJ; FLJ90232; MGC126521; MGC126523
External IDs OMIM: 605882 MGI2442836 HomoloGene32766
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 83990 237911
Ensembl ENSG00000136492 ENSMUSG00000034329
Uniprot Q9BX63 Q3TER9
Refseq NM_032043 (mRNA)
NP_114432 (protein)
NM_178309 (mRNA)
NP_840094 (protein)
Location Chr 17: 57.11 - 57.3 Mb Chr 11: 85.87 - 86.02 Mb
Pubmed search [1] [2]

BRCA1 interacting protein C-terminal helicase 1, also known as BRIP1 and DOG1, is a human gene.[1]

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.[1]

References

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. PMID 10669750. 
  • Cantor SB, Bell DW, Ganesan S, et al. (2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.". Cell 105 (1): 149–60. PMID 11301010. 
  • Menichini P, Linial M (2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutat. Res. 487 (1-2): 67–71. PMID 11595410. 
  • 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. PMID 11877378. 
  • 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. 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. PMID 12477932. 
  • 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. PMID 12565990. 
  • Rutter JL, Smith AM, Dαvila 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. PMID 14983014. 
  • 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. 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, Nominι 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. PMID 15302935. 
  • 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. PMID 15489334. 
  • 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. 


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