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{{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 = Mutat Res | volume = 487 | issue = 1–2 | pages = 67–71 |date=Oct 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=Apr 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>
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{{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>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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>
| 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" />
}}
}}
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 | title = Mutations in BRIP1 confer high risk of ovarian cancer | journal = Nat. Genet. | volume = 43 | issue = 11 | pages = 1104–7 | year = 2011 | pmid = 21964575 | doi = 10.1038/ng.955 }}</ref>
==Interactions==
BRIP1 has been shown to [[Protein-protein interaction|interact]] with [[BRCA1]].<ref name = pmid15242590>{{cite journal | date = Jul 2004 | 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  | pmid = 15242590 | pmc = 3652423 | doi = 10.1016/j.str.2004.06.002}}</ref><ref name = pmid11877378>{{cite journal | date = Mar 2002 | 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 Dev. | volume = 16 | issue = 5 | pages = 583–93  | pmid = 11877378 | pmc = 155350 | doi = 10.1101/gad.959202}}</ref><ref name = pmid14576433>{{cite journal | date = Oct 2003 | 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  | pmid = 14576433 | doi = 10.1126/science.1088753}}</ref><ref name = pmid14578343>{{cite journal | date = Dec 2003 | vauthors = 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  | pmid = 14578343 | doi = 10.1074/jbc.C300407200}}</ref><ref name = pmid15133502>{{cite journal | date = Jun 2004 | 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 = Nat. Struct. Mol. Biol. | volume = 11 | issue = 6 | pages = 512–8  | pmid = 15133502 | doi = 10.1038/nsmb775}}</ref><ref name = pmid15208681>{{cite journal | date = Aug 2004 | 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  | pmid = 15208681 | doi = 10.1038/sj.onc.1207786}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|BACH1}}
* {{UCSC gene info|BRIP1}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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  | author=Kobayashi A |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=10.1128/MCB.20.5.1733-1746.2000 | pmc=85356 |name-list-format=vanc| author2=Yamagiwa H  | author3=Hoshino H  | display-authors=3  | last4=Muto  | first4=A.  | last5=Sato  | first5=K.  | last6=Morita | first6=M.  | last7=Hayashi  | first7=N. | last8=Yamamoto  | first8=M.  | last9=Igarashi  | first9=K. }}
*{{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  | author=Joo WS |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  | pmc=155350  |name-list-format=vanc| author2=Jeffrey PD  | author3=Cantor SB  | display-authors=3  | last4=Finnin  | first4=MS  | last5=Livingston  | first5=DM  | last6=Pavletich  | first6=NP }}
*{{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  | author=Luo L |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=10.1002/ijc.10214  |name-list-format=vanc| author2=Lei H | author3=Du Q  | display-authors=3  | last4=Von Wachenfeldt  | first4=Anna  | last5=Kockum  | first5=Ingrid  | last6=Luthman  | first6=Holger  | last7=Vorechovsky  | first7=Igor  | last8=Lindblom  | first8=Annika }}
*{{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  | author=Strausberg RL |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  | pmc=139241 |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{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  | author=Karppinen SM |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=10.1016/S0959-8049(02)00498-7 |name-list-format=vanc| author2=Vuosku J | author3=Heikkinen K  | display-authors=3  | last4=Allinen  | first4=M  | last5=Winqvist  | first5=R  }}
*{{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  | author=Rutter JL |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 |name-list-format=vanc| author2=Smith AM  | author3=Dávila MR  | display-authors=3  | last4=Sigurdson  | first4=Alice J. | last5=Giusti  | first5=Ruthann M. | last6=Pineda  | first6=Marbin A. | last7=Doody  | first7=Michele M.  | last8=Tucker  | first8=Margaret A.  | last9=Greene  | first9=Mark H. }}
*{{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  | author=Suzuki H |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 |name-list-format=vanc| author2=Tashiro S | author3=Sun J  | display-authors=3  | last4=Doi  | first4=H  | last5=Satomi  | first5=S  | last6=Igarashi  | first6=K }}
*{{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  | author=Yu X |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 |name-list-format=vanc| author2=Chini CC  | author3=He M  | display-authors=3  | last4=Mer  | first4=G  | last5=Chen  | first5=J }}
*{{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=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  | 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  | author=Ota T |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  |name-list-format=vanc| author2=Suzuki Y | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{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  | author=Cantor S |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=10.1073/pnas.0308717101  | pmc=356955  |name-list-format=vanc| author2=Drapkin R  | author3=Zhang F  | display-authors=3  | last4=Lin  | first4=Y  | last5=Han  | first5=J  | last6=Pamidi  | first6=S  | last7=Livingston  | first7=DM  }}
*{{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=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=10.1016/S1097-2765(04)00238-2  }}
*{{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=Clapperton JA |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  |name-list-format=vanc| author2=Manke IA  | author3=Lowery DM  | display-authors=3  | last4=Ho  | first4=Timmy  | last5=Haire  | first5=Lesley F  | last6=Yaffe  | first6=Michael B  | last7=Smerdon  | first7=Stephen J }}
*{{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=Wada O |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  |name-list-format=vanc| author2=Oishi H  | author3=Takada I  | display-authors=3  | last4=Yanagisawa  | first4=Junn  | last5=Yano  | first5=Tetsu  | last6=Kato  | first6=Shigeaki }}
*{{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=Botuyan MV |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  |name-list-format=vanc| author2=Nominé Y  | author3=Yu X  | display-authors=3  | last4=Juranic  | first4=Nenad  | last5=MacUra  | first5=Slobodan  | last6=Chen  | first6=Junjie  | last7=Mer  | first7=Georges | pmc=3652423}}
*{{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=Beausoleil SA |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  | pmc=514446  |name-list-format=vanc| author2=Jedrychowski M  | author3=Schwartz D  | display-authors=3  | last4=Elias  | first4=JE  | last5=Villén  | first5=J  | last6=Li  | first6=J  | last7=Cohn  | first7=MA  | last8=Cantley  | first8=LC  | last9=Gygi  | first9=SP }}
*{{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=Gerhard DS |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  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{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=Gupta R |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 |name-list-format=vanc| author2=Sharma S  | author3=Sommers JA  | display-authors=3  | last4=Jin  | first4=Z  | last5=Cantor  | first5=SB  | last6=Brosh Jr  | first6=RM }}
*{{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}}
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[[de:BRIP1]]
[[Category:Genes]]
{{WikiDoc Sources}}
[[Category:Human proteins]]

Revision as of 02:40, 30 August 2017

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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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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]

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]

Interactions

BRIP1 has been shown to interact with BRCA1.[5][6][7][8][9][10]

References

  1. ↑ Menichini P, Linial M (Oct 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutat Res. 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 (Apr 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, 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 (2011). "Mutations in BRIP1 confer high risk of ovarian cancer". Nat. Genet. 43 (11): 1104–7. doi:10.1038/ng.955. PMID 21964575.
  5. ↑ Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G (Jul 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.
  6. ↑ Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (Mar 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. PMC 155350. PMID 11877378.
  7. ↑ Yu X, Chini CC, He M, Mer G, Chen J (Oct 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–42. doi:10.1126/science.1088753. PMID 14576433.
  8. ↑ Rodriguez M, Yu X, Chen J, Songyang Z (Dec 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi:10.1074/jbc.C300407200. PMID 14578343.
  9. ↑ Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (Jun 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.
  10. ↑ Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S (Aug 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

Further reading

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