BRIP1

BRIP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1T15, 1T29, 3AL3
Identifiers
Aliases	BRIP1, BACH1, FANCJ, OF, BRCA1 interacting protein C-terminal helicase 1, BRCA1 interacting helicase 1
External IDs	OMIM: 605882; MGI: 2442836; HomoloGene: 32766; GeneCards: BRIP1; OMA:BRIP1 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q23.2 Start 61,679,139 bp End 61,863,559 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 C Start 85,948,964 bp End 86,092,019 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone gonad testicle secondary oocyte ganglionic eminence stromal cell of endometrium bone marrow bone marrow cells trabecular bone left testis Top expressed in zygote primary oocyte genital tubercle tail of embryo secondary oocyte yolk sac morula gray matter layer of cerebellum ventricular zone spermatid More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding 4 iron, 4 sulfur cluster binding nucleotide binding helicase activity iron-sulfur cluster binding DNA helicase activity metal ion binding hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides protein binding nucleic acid binding hydrolase activity ATP binding chromatin binding Cellular component cytoplasm nuclear membrane nucleoplasm nucleus Biological process regulation of transcription by RNA polymerase II DNA damage checkpoint signaling cellular response to DNA damage stimulus cellular response to vitamin nucleobase-containing compound metabolic process negative regulation of cell population proliferation DNA replication DNA duplex unwinding double-strand break repair DNA repair homologous chromosome pairing at meiosis spermatogenesis spermatogonial cell division spermatid development male gonad development response to toxic substance negative regulation of gene expression meiotic DNA double-strand break processing involved in reciprocal meiotic recombination chiasma assembly cellular response to hypoxia seminiferous tubule development cellular response to angiotensin double-strand break repair involved in meiotic recombination nucleotide-excision repair regulation of signal transduction by p53 class mediator Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 83990 237911 Ensembl ENSG00000136492 ENSMUSG00000034329 UniProt Q9BX63 Q5SXJ3 RefSeq (mRNA) NM_032043 NM_178309 RefSeq (protein) NP_114432 NP_840094 Location (UCSC) Chr 17: 61.68 – 61.86 Mb Chr 11: 85.95 – 86.09 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Function

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.

This protein also appears to be important in ovarian cancer where it seems to act as a tumor suppressor. Mutations in BRIP1 are associated with a 10-15% risk of ovarian cancer.

Interactions

BRIP1 has been shown to interact with BRCA1.

Further reading

• Kobayashi A, Yamagiwa H, Hoshino H, Muto A, Sato K, Morita M, Hayashi N, Yamamoto M, Igarashi K (March 2000). "A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain". Molecular and Cellular Biology. 20 (5): 1733–46. doi:10.1128/MCB.20.5.1733-1746.2000. PMC 85356. PMID 10669750.
• Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (March 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development. 16 (5): 583–93. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.
• Luo L, Lei H, Du Q, von Wachenfeldt A, Kockum I, Luthman H, Vorechovsky I, Lindblom A (April 2002). "No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22". International Journal of Cancer. 98 (4): 638–9. doi:10.1002/ijc.10214. PMID 11920628.
• Karppinen SM, Vuosku J, Heikkinen K, Allinen M, Winqvist R (February 2003). "No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families". European Journal of Cancer. 39 (3): 366–71. doi:10.1016/S0959-8049(02)00498-7. PMID 12565990.
• Rutter JL, Smith AM, Dávila MR, Sigurdson AJ, Giusti RM, Pineda MA, Doody MM, Tucker MA, Greene MH, Zhang J, Struewing JP (August 2003). "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". Human Mutation. 22 (2): 121–8. doi:10.1002/humu.10238. PMID 12872252.
• Suzuki H, Tashiro S, Sun J, Doi H, Satomi S, Igarashi K (December 2003). "Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene". The Journal of Biological Chemistry. 278 (49): 49246–53. doi:10.1074/jbc.M306764200. PMID 14504288.
• Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–42. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433.
• Rodriguez M, Yu X, Chen J, Songyang Z (December 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry. 278 (52): 52914–8. doi:10.1074/jbc.C300407200. PMID 14578343.
• Cantor S, Drapkin R, Zhang F, Lin Y, Han J, Pamidi S, Livingston DM (February 2004). "The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations". Proceedings of the National Academy of Sciences of the United States of America. 101 (8): 2357–62. Bibcode:2004PNAS..101.2357C. doi:10.1073/pnas.0308717101. PMC 356955. PMID 14983014.
• Shiozaki EN, Gu L, Yan N, Shi Y (May 2004). "Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling". Molecular Cell. 14 (3): 405–12. doi:10.1016/S1097-2765(04)00238-2. PMID 15125843.
• Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (June 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology. 11 (6): 512–8. doi:10.1038/nsmb775. PMID 15133502.
• Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S (August 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, Juranic N, Macura S, Chen J, Mer G (July 2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure. 12 (7): 1137–46. doi:10.1016/j.str.2004.06.002. PMC 3652423. PMID 15242590.
• Gupta R, Sharma S, Sommers JA, Jin Z, Cantor SB, Brosh RM (July 2005). "Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer". The Journal of Biological Chemistry. 280 (27): 25450–60. doi:10.1074/jbc.M501995200. PMID 15878853.

External links

• Human BACH1 genome location and BACH1 gene details page in the UCSC Genome Browser.
• Human BRIP1 genome location and BRIP1 gene details page in the UCSC Genome Browser.