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
External IDs	OMIM: 605882 MGI: 2442836 HomoloGene: 32766 GeneCards: BRIP1
Gene location (Human)
Chr.	Chromosome 17 (human)[1]
End	61,863,528 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	86,201,193 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• DNA binding; • 4 iron, 4 sulfur cluster binding; • nucleotide binding; • GO:0008026 helicase activity; • iron-sulfur cluster binding; • GO:0004003 DNA helicase activity; • metal ion binding; • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; • GO:0001948 protein binding; • nucleic acid binding; • hydrolase activity; • ATP binding; • chromatin binding;
Cellular component	• cytoplasm; • not the membrane; • nucleoplasm; • cell nucleus;
Biological process	• regulation of transcription from RNA polymerase II promoter; • DNA damage checkpoint; • cellular response to DNA damage stimulus; • cellular response to vitamin; • nucleobase-containing compound metabolic process; • negative regulation of cell proliferation; • DNA replication; • DNA duplex unwinding; • double-strand break repair; • DNA repair; • synapsis; • 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
	83990
	237911
	ENSG00000136492
	ENSMUSG00000034329
	Q9BX63
	Q5SXJ3
	NM_032043
	NM_178309
	NP_114432
	NP_840094
	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.[5][6][7]

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.[7]

This protein also appears to be important in ovarian cancer where it seems to act as a tumor suppressor.[8] Mutations in BRIP1 are associated with a 10-15% risk of ovarian cancer.[9]

Interactions

BRIP1 has been shown to interact with BRCA1.[10][11][12][13][14][15]

References

GRCh38: Ensembl release 89: ENSG00000136492 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000034329 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Menichini P, Linial M (November 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutation Research. 487 (1–2): 67–71. doi:10.1016/s0921-8777(01)00104-5. PMID 11595410.
Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM (April 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. S2CID 15966253.
"Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".
Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, et al. (October 2011). "Mutations in BRIP1 confer high risk of ovarian cancer". Nature Genetics. 43 (11): 1104–7. doi:10.1038/ng.955. hdl:2336/228034. PMID 21964575. S2CID 24535565.
Ring KL, Garcia C, Thomas MH, Modesitt SC (November 2017). "Current and future role of genetic screening in gynecologic malignancies". American Journal of Obstetrics and Gynecology. 217 (5): 512–521. doi:10.1016/j.ajog.2017.04.011. PMID 28411145. S2CID 29024566.
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.
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.
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. S2CID 29407635.
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.
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. S2CID 7354915.
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.

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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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000136492 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000034329 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11595410-5] Menichini P, Linial M (November 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutation Research. 487 (1–2): 67–71. doi:10.1016/s0921-8777(01)00104-5. PMID 11595410.

[pmid11301010-6] Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM (April 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. S2CID 15966253.

[entrez-7] "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".

[pmid21964575-8] Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, et al. (October 2011). "Mutations in BRIP1 confer high risk of ovarian cancer". Nature Genetics. 43 (11): 1104–7. doi:10.1038/ng.955. hdl:2336/228034. PMID 21964575. S2CID 24535565.

[9] Ring KL, Garcia C, Thomas MH, Modesitt SC (November 2017). "Current and future role of genetic screening in gynecologic malignancies". American Journal of Obstetrics and Gynecology. 217 (5): 512–521. doi:10.1016/j.ajog.2017.04.011. PMID 28411145. S2CID 29024566.

[pmid15242590-10] 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.

[pmid11877378-11] 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.

[pmid14576433-12] 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. S2CID 29407635.

[pmid14578343-13] 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.

[pmid15133502-14] 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. S2CID 7354915.

[pmid15208681-15] 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.

BRIP1

Function

Interactions

References

Further reading

External links