BRIP1

From Wikipedia, the free encyclopedia

BRCA1 interacting protein C-terminal helicase 1

Identifiers

BRIP1; BACH1; OF; FANCJ; FLJ90232; MGC126521; MGC126523

External IDs

OMIM: 605882 MGI: 2442836 HomoloGene: 32766

Gene ontology
Molecular Function:	• nucleotide binding • DNA binding • ATP-dependent DNA helicase activity • protein binding • ATP binding • hydrolase activity • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Cellular Component:	• 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

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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, 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]

[edit] References

^ ^a ^b Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1.

[edit] 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, 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. 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, 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. 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.