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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Fanconi anemia group J protein''' is a [[protein]] that in humans is encoded by the ''BRCA1-interacting protein 1'' (''BRIP1'') [[gene]].<ref name="pmid11595410">{{cite journal | vauthors = Menichini P, Linial M | title = SUVi and BACH1: a new subfamily of mammalian helicases? | journal = Mutation Research | volume = 487 | issue = 1–2 | pages = 67–71 | date = November 2001 | pmid = 11595410 | pmc =  | doi = 10.1016/s0921-8777(01)00104-5 }}</ref><ref name="pmid11301010">{{cite journal | vauthors = Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM | title = BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function | journal = Cell | volume = 105 | issue = 1 | pages = 149–60 | date = April 2001 | pmid = 11301010 | pmc = | doi = 10.1016/S0092-8674(01)00304-X }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83990| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = BRCA1 interacting protein C-terminal helicase 1
| HGNCid = 20473
| Symbol = BRIP1
| AltSymbols =; BACH1; OF; FANCJ; FLJ90232; MGC126521; MGC126523
| OMIM = 605882
| ECnumber = 
| Homologene = 32766
| MGIid = 2442836
| GeneAtlas_image1 = PBB_GE_BRIP1_221703_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004003 |text = ATP-dependent DNA helicase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016818 |text = hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000077 |text = DNA damage checkpoint}} {{GNF_GO|id=GO:0006139 |text = nucleobase, nucleoside, nucleotide and nucleic acid metabolic process}} {{GNF_GO|id=GO:0006302 |text = double-strand break repair}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 83990
    | Hs_Ensembl = ENSG00000136492
    | Hs_RefseqProtein = NP_114432
    | Hs_RefseqmRNA = NM_032043
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 57114767
    | Hs_GenLoc_end = 57295537
    | Hs_Uniprot = Q9BX63
    | Mm_EntrezGene = 237911
    | Mm_Ensembl = ENSMUSG00000034329
    | Mm_RefseqmRNA = NM_178309
    | Mm_RefseqProtein = NP_840094
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 85874331
    | Mm_GenLoc_end = 86017388
    | Mm_Uniprot = Q3TER9
  }}
}}
'''BRCA1 interacting protein C-terminal helicase 1''', also known as '''BRIP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83990| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83990| accessdate = }}</ref>
}}


==References==
This protein also appears to be important in ovarian cancer where it seems to act as a tumor suppressor.<ref name="pmid21964575">{{cite journal | vauthors = Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, Besenbacher S, Lundin P, Stacey SN, Gudmundsson J, Magnusson OT, le Roux L, Orlygsdottir G, Helgadottir HT, Johannsdottir H, Gylfason A, Tryggvadottir L, Jonasson JG, de Juan A, Ortega E, Ramon-Cajal JM, García-Prats MD, Mayordomo C, Panadero A, Rivera F, Aben KK, van Altena AM, Massuger LF, Aavikko M, Kujala PM, Staff S, Aaltonen LA, Olafsdottir K, Bjornsson J, Kong A, Salvarsdottir A, Saemundsson H, Olafsson K, Benediktsdottir KR, Gulcher J, Masson G, Kiemeney LA, Mayordomo JI, Thorsteinsdottir U, Stefansson K | display-authors = 6 | title = Mutations in BRIP1 confer high risk of ovarian cancer | journal = Nature Genetics | volume = 43 | issue = 11 | pages = 1104–7 | date = October 2011 | pmid = 21964575 | doi = 10.1038/ng.955 }}</ref> Mutations in BRIP1 are associated with a 10-15% risk of ovarian cancer.<ref>{{cite journal | vauthors = Ring KL, Garcia C, Thomas MH, Modesitt SC | title = Current and future role of genetic screening in gynecologic malignancies | journal = American Journal of Obstetrics and Gynecology | volume = 217 | issue = 5 | pages = 512–521 | date = November 2017 | pmid = 28411145 | doi = 10.1016/j.ajog.2017.04.011 }}</ref>
{{reflist|2}}
 
==Further reading==
== Interactions ==
 
BRIP1 has been shown to [[Protein-protein interaction|interact]] with [[BRCA1]].<ref name = pmid15242590>{{cite journal | vauthors = Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G | title = Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains | journal = Structure | volume = 12 | issue = 7 | pages = 1137–46 | date = July 2004 | pmid = 15242590 | pmc = 3652423 | doi = 10.1016/j.str.2004.06.002 }}</ref><ref name = pmid11877378>{{cite journal | vauthors = Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP | title = Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure | journal = Genes & Development | volume = 16 | issue = 5 | pages = 583–93 | date = March 2002 | pmid = 11877378 | pmc = 155350 | doi = 10.1101/gad.959202 }}</ref><ref name = pmid14576433>{{cite journal | vauthors = Yu X, Chini CC, He M, Mer G, Chen J | title = The BRCT domain is a phospho-protein binding domain | journal = Science | volume = 302 | issue = 5645 | pages = 639–42 | date = October 2003 | pmid = 14576433 | doi = 10.1126/science.1088753 }}</ref><ref name = pmid14578343>{{cite journal | vauthors = Rodriguez M, Yu X, Chen J, Songyang Z | title = Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains | journal = The Journal of Biological Chemistry | volume = 278 | issue = 52 | pages = 52914–8 | date = December 2003 | pmid = 14578343 | doi = 10.1074/jbc.C300407200 }}</ref><ref name = pmid15133502>{{cite journal | vauthors = Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ | title = Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer | journal = Nature Structural & Molecular Biology | volume = 11 | issue = 6 | pages = 512–8 | date = June 2004 | pmid = 15133502 | doi = 10.1038/nsmb775 }}</ref><ref name = pmid15208681>{{cite journal | vauthors = Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S | title = BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220 | journal = Oncogene | volume = 23 | issue = 35 | pages = 6000–5 | date = August 2004 | pmid = 15208681 | doi = 10.1038/sj.onc.1207786 }}</ref>
 
== References ==
{{reflist}}
{{clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Kobayashi A, Yamagiwa H, Hoshino H, Muto A, Sato K, Morita M, Hayashi N, Yamamoto M, Igarashi K | title = A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain | journal = Molecular and Cellular Biology | volume = 20 | issue = 5 | pages = 1733–46 | date = March 2000 | pmid = 10669750 | pmc = 85356 | doi = 10.1128/MCB.20.5.1733-1746.2000 }}
| citations =
* {{cite journal | vauthors = Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP | title = Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure | journal = Genes & Development | volume = 16 | issue = 5 | pages = 583–93 | date = March 2002 | pmid = 11877378 | pmc = 155350 | doi = 10.1101/gad.959202 }}
*{{cite journal | author=Kobayashi A, Yamagiwa H, Hoshino H, ''et al.'' |title=A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain. |journal=Mol. Cell. Biol. |volume=20 |issue= 5 |pages= 1733-46 |year= 2000 |pmid= 10669750 |doi= }}
* {{cite journal | vauthors = Luo L, Lei H, Du Q, von Wachenfeldt A, Kockum I, Luthman H, Vorechovsky I, Lindblom A | title = No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22 | journal = International Journal of Cancer | volume = 98 | issue = 4 | pages = 638–9 | date = April 2002 | pmid = 11920628 | doi = 10.1002/ijc.10214 }}
*{{cite journal  | author=Cantor SB, Bell DW, Ganesan S, ''et al.'' |title=BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. |journal=Cell |volume=105 |issue= 1 |pages= 149-60 |year= 2001 |pmid= 11301010 |doi=  }}
* {{cite journal | vauthors = Karppinen SM, Vuosku J, Heikkinen K, Allinen M, Winqvist R | title = No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families | journal = European Journal of Cancer | volume = 39 | issue = 3 | pages = 366–71 | date = February 2003 | pmid = 12565990 | doi = 10.1016/S0959-8049(02)00498-7 }}
*{{cite journal  | author=Menichini P, Linial M |title=SUVi and BACH1: a new subfamily of mammalian helicases? |journal=Mutat. Res. |volume=487 |issue= 1-2 |pages= 67-71 |year= 2001 |pmid= 11595410 |doi=  }}
* {{cite journal | vauthors = Rutter JL, Smith AM, Dávila MR, Sigurdson AJ, Giusti RM, Pineda MA, Doody MM, Tucker MA, Greene MH, Zhang J, Struewing JP | title = 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 | journal = Human Mutation | volume = 22 | issue = 2 | pages = 121–8 | date = August 2003 | pmid = 12872252 | doi = 10.1002/humu.10238 }}
*{{cite journal | author=Joo WS, Jeffrey PD, Cantor SB, ''et al.'' |title=Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure. |journal=Genes Dev. |volume=16 |issue= 5 |pages= 583-93 |year= 2002 |pmid= 11877378 |doi= 10.1101/gad.959202 }}
* {{cite journal | vauthors = Suzuki H, Tashiro S, Sun J, Doi H, Satomi S, Igarashi K | title = Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene | journal = The Journal of Biological Chemistry | volume = 278 | issue = 49 | pages = 49246–53 | date = December 2003 | pmid = 14504288 | doi = 10.1074/jbc.M306764200 }}
*{{cite journal | author=Luo L, Lei H, Du Q, ''et al.'' |title=No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22. |journal=Int. J. Cancer |volume=98 |issue= 4 |pages= 638-9 |year= 2002 |pmid= 11920628 |doi=  }}
* {{cite journal | vauthors = Yu X, Chini CC, He M, Mer G, Chen J | title = The BRCT domain is a phospho-protein binding domain | journal = Science | volume = 302 | issue = 5645 | pages = 639–42 | date = October 2003 | pmid = 14576433 | doi = 10.1126/science.1088753 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Rodriguez M, Yu X, Chen J, Songyang Z | title = Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains | journal = The Journal of Biological Chemistry | volume = 278 | issue = 52 | pages = 52914–8 | date = December 2003 | pmid = 14578343 | doi = 10.1074/jbc.C300407200 }}
*{{cite journal | author=Karppinen SM, Vuosku J, Heikkinen K, ''et al.'' |title=No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families. |journal=Eur. J. Cancer |volume=39 |issue= 3 |pages= 366-71 |year= 2003 |pmid= 12565990 |doi= }}
* {{cite journal | vauthors = Cantor S, Drapkin R, Zhang F, Lin Y, Han J, Pamidi S, Livingston DM | title = The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 8 | pages = 2357–62 | date = February 2004 | pmid = 14983014 | pmc = 356955 | doi = 10.1073/pnas.0308717101 }}
*{{cite journal | author=Rutter JL, Smith AM, Dávila MR, ''et al.'' |title=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. |journal=Hum. Mutat. |volume=22 |issue= 2 |pages= 121-8 |year= 2004 |pmid= 12872252 |doi= 10.1002/humu.10238 }}
* {{cite journal | vauthors = Shiozaki EN, Gu L, Yan N, Shi Y | title = Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling | journal = Molecular Cell | volume = 14 | issue = 3 | pages = 405–12 | date = May 2004 | pmid = 15125843 | doi = 10.1016/S1097-2765(04)00238-2 }}
*{{cite journal | author=Suzuki H, Tashiro S, Sun J, ''et al.'' |title=Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene. |journal=J. Biol. Chem. |volume=278 |issue= 49 |pages= 49246-53 |year= 2004 |pmid= 14504288 |doi= 10.1074/jbc.M306764200 }}
* {{cite journal | vauthors = Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ | title = Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer | journal = Nature Structural & Molecular Biology | volume = 11 | issue = 6 | pages = 512–8 | date = June 2004 | pmid = 15133502 | doi = 10.1038/nsmb775 }}
*{{cite journal | author=Yu X, Chini CC, He M, ''et al.'' |title=The BRCT domain is a phospho-protein binding domain. |journal=Science |volume=302 |issue= 5645 |pages= 639-42 |year= 2003 |pmid= 14576433 |doi= 10.1126/science.1088753 }}
* {{cite journal | vauthors = Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S | title = BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220 | journal = Oncogene | volume = 23 | issue = 35 | pages = 6000–5 | date = August 2004 | pmid = 15208681 | doi = 10.1038/sj.onc.1207786 }}
*{{cite journal | author=Rodriguez M, Yu X, Chen J, Songyang Z |title=Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 52914-8 |year= 2004 |pmid= 14578343 |doi= 10.1074/jbc.C300407200 }}
* {{cite journal | vauthors = Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G | title = Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains | journal = Structure | volume = 12 | issue = 7 | pages = 1137–46 | date = July 2004 | pmid = 15242590 | pmc = 3652423 | doi = 10.1016/j.str.2004.06.002 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Gupta R, Sharma S, Sommers JA, Jin Z, Cantor SB, Brosh RM | title = Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer | journal = The Journal of Biological Chemistry | volume = 280 | issue = 27 | pages = 25450–60 | date = July 2005 | pmid = 15878853 | doi = 10.1074/jbc.M501995200 }}
*{{cite journal  | author=Cantor S, Drapkin R, Zhang F, ''et al.'' |title=The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 8 |pages= 2357-62 |year= 2004 |pmid= 14983014 |doi= }}
*{{cite journal | author=Shiozaki EN, Gu L, Yan N, Shi Y |title=Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. |journal=Mol. Cell |volume=14 |issue= 3 |pages= 405-12 |year= 2004 |pmid= 15125843 |doi= }}
*{{cite journal | author=Clapperton JA, Manke IA, Lowery DM, ''et al.'' |title=Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. |journal=Nat. Struct. Mol. Biol. |volume=11 |issue= 6 |pages= 512-8 |year= 2004 |pmid= 15133502 |doi= 10.1038/nsmb775 }}
*{{cite journal | author=Wada O, Oishi H, Takada I, ''et al.'' |title=BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220. |journal=Oncogene |volume=23 |issue= 35 |pages= 6000-5 |year= 2004 |pmid= 15208681 |doi= 10.1038/sj.onc.1207786 }}
*{{cite journal | author=Botuyan MV, Nominé Y, Yu X, ''et al.'' |title=Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. |journal=Structure |volume=12 |issue= 7 |pages= 1137-46 |year= 2005 |pmid= 15242590 |doi= 10.1016/j.str.2004.06.002 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Gupta R, Sharma S, Sommers JA, ''et al.'' |title=Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer. |journal=J. Biol. Chem. |volume=280 |issue= 27 |pages= 25450-60 |year= 2005 |pmid= 15878853 |doi= 10.1074/jbc.M501995200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
* {{UCSC gene info|BACH1}}
* {{UCSC gene info|BRIP1}}


[[de:BRIP1]]
[[Category:Genes]]
{{WikiDoc Sources}}
[[Category:Human proteins]]

Latest revision as of 19:42, 27 March 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

Interactions

BRIP1 has been shown to interact with BRCA1.[6][7][8][9][10][11]

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".
  4. ↑ 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. PMID 21964575.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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. doi:10.1126/science.1088753. PMID 14576433.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 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.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=BRIP1&oldid=1529176"