Biology:BRIP1
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Short description: Mammalian protein found in Homo sapiens
 Generic protein structure example |
Fanconi anemia group J protein is a protein that in humans is encoded by the BRCA1-interacting protein 1 (BRIP1) gene.[1][2][3]
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.[3]
This protein also appears to be important in ovarian cancer where it seems to act as a tumor suppressor.[4] Mutations in BRIP1 are associated with a 10-15% risk of ovarian cancer.[5]
BRIP1 appears to have an important role in neuronal cells by suppressing oxidative stress, excitotoxicity induced DNA damage, and in protecting the integrity of mitochondria.[6] A deficiency of BRIP1 causes increased DNA damage, mitochondrial abnormalities and neuronal cell death.
DNA repair
BRIP1 protein is a DNA helicase that is employed in homologous recombinational repair, and in the response of the cell to DNA replication stress.[7] In part, BRIP1 carries out its function through interaction with other key DNA repair proteins, specifically MLH1, BRCA1 and BLM.[7] This group of proteins helps to ensuring genome stability, and in particular repairs DNA double-strand breaks during prophase 1 of meiosis.
Interactions
BRIP1 has been shown to interact with BRCA1.[8][9][10][11][12][13]
References
- ↑ "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutation Research 487 (1–2): 67–71. November 2001. doi:10.1016/s0921-8777(01)00104-5. PMID 11595410.
- ↑ "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell 105 (1): 149–160. April 2001. doi:10.1016/S0092-8674(01)00304-X. PMID 11301010.
- ↑ 3.0 3.1 "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83990.
- ↑ "Mutations in BRIP1 confer high risk of ovarian cancer". Nature Genetics 43 (11): 1104–1107. October 2011. doi:10.1038/ng.955. PMID 21964575.
- ↑ "Current and future role of genetic screening in gynecologic malignancies". American Journal of Obstetrics and Gynecology 217 (5): 512–521. November 2017. doi:10.1016/j.ajog.2017.04.011. PMID 28411145.
- ↑ "A Novel Role for BRIP1/FANCJ in Neuronal Cells Health and in Resolving Oxidative Stress-Induced DNA Lesions". Journal of Alzheimer's Disease 85 (1): 207–221. 2022. doi:10.3233/JAD-215305. PMID 34776453.
- ↑ 7.0 7.1 "FancJ (Brip1) loss-of-function allele results in spermatogonial cell depletion during embryogenesis and altered processing of crossover sites during meiotic prophase I in mice". Chromosoma 125 (2): 237–252. June 2016. doi:10.1007/s00412-015-0549-2. PMID 26490168.
- ↑ "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure 12 (7): 1137–1146. July 2004. doi:10.1016/j.str.2004.06.002. PMID 15242590.
- ↑ "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development 16 (5): 583–593. March 2002. doi:10.1101/gad.959202. PMID 11877378.
- ↑ "The BRCT domain is a phospho-protein binding domain". Science 302 (5645): 639–642. October 2003. doi:10.1126/science.1088753. PMID 14576433. Bibcode: 2003Sci...302..639Y.
- ↑ "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry 278 (52): 52914–52918. December 2003. doi:10.1074/jbc.C300407200. PMID 14578343.
- ↑ "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology 11 (6): 512–518. June 2004. doi:10.1038/nsmb775. PMID 15133502.
- ↑ "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene 23 (35): 6000–6005. August 2004. doi:10.1038/sj.onc.1207786. PMID 15208681.
Further reading
- "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): 1733–1746. March 2000. doi:10.1128/MCB.20.5.1733-1746.2000. PMID 10669750.
- "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development 16 (5): 583–593. March 2002. doi:10.1101/gad.959202. PMID 11877378.
- "No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22". International Journal of Cancer 98 (4): 638–639. April 2002. doi:10.1002/ijc.10214. PMID 11920628.
- "No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families". European Journal of Cancer 39 (3): 366–371. February 2003. doi:10.1016/S0959-8049(02)00498-7. PMID 12565990.
- "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): 121–128. August 2003. doi:10.1002/humu.10238. PMID 12872252.
- "Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene". The Journal of Biological Chemistry 278 (49): 49246–49253. December 2003. doi:10.1074/jbc.M306764200. PMID 14504288.
- "The BRCT domain is a phospho-protein binding domain". Science 302 (5645): 639–642. October 2003. doi:10.1126/science.1088753. PMID 14576433. Bibcode: 2003Sci...302..639Y.
- "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry 278 (52): 52914–52918. December 2003. doi:10.1074/jbc.C300407200. PMID 14578343.
- "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): 2357–2362. February 2004. doi:10.1073/pnas.0308717101. PMID 14983014. Bibcode: 2004PNAS..101.2357C.
- "Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling". Molecular Cell 14 (3): 405–412. May 2004. doi:10.1016/S1097-2765(04)00238-2. PMID 15125843.
- "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology 11 (6): 512–518. June 2004. doi:10.1038/nsmb775. PMID 15133502.
- "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene 23 (35): 6000–6005. August 2004. doi:10.1038/sj.onc.1207786. PMID 15208681.
- "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure 12 (7): 1137–1146. July 2004. doi:10.1016/j.str.2004.06.002. PMID 15242590.
- "Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer". The Journal of Biological Chemistry 280 (27): 25450–25460. July 2005. doi:10.1074/jbc.M501995200. PMID 15878853.
External links
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.
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