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BRCA1 interacting protein C-terminal helicase 1
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols BRIP1 ; BACH1; FANCJ; OF
External IDs OMIM605882 MGI2442836 HomoloGene32766 GeneCards: BRIP1 Gene
EC number
RNA expression pattern
PBB GE BRIP1 221703 at tn.png
More reference expression data
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:
59.76 – 59.94 Mb
Chr 11:
86.06 – 86.2 Mb
PubMed search [1] [2]

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]


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


  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. ^ a b "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. 

Further reading[edit]