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Gene Review

BRIP1  -  BRCA1 interacting protein C-terminal...

Homo sapiens

Synonyms: ATP-dependent RNA helicase BRIP1, BACH1, BRCA1-associated C-terminal helicase 1, BRCA1-interacting protein 1, BRCA1-interacting protein C-terminal helicase 1, ...
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Disease relevance of BRIP1


Psychiatry related information on BRIP1

  • Aromatherapy, Bach flower remedies, hypnotherapy, massage, nutrition, reflexology, Reiki and yoga were all recommended as suitable treatments for stress/anxiety [7].
  • The current study extended previous research by Bach and Hayes (2002. The use of Acceptance and Commitment Therapy to prevent the rehospitalization of psychotic patients: A randomized controlled trial. Journal of Consulting and Clinical Psychology, 70, 1129-1139) using Acceptance and Commitment Therapy (ACT) in the treatment of psychosis [8].

High impact information on BRIP1


Chemical compound and disease context of BRIP1

  • On "The effect of intravenous lidocaine on nociceptive processing in diabetic neuropathy" by Bach et al. in Pain, 40 (1990) 29-34 [10].
  • The Bach model was developed to predict the absolute 10-year risk of developing lung cancer among smokers by use of participants in the Carotene and Retinol Efficacy Trial of lung cancer prevention [11].
  • We assessed the validity of the Bach model among 6239 smokers from the placebo arm of the Alpha-Tocopherol, Beta-Carotene Cancer Prevention (ATBC) Study. The expected numbers of lung cancer cases and deaths without lung cancer were calculated from the Bach model and compared with the observed numbers of corresponding events over 10 years [11].

Biological context of BRIP1


Anatomical context of BRIP1

  • RESULTS: Six BACH1 germ line alterations were observed in the mutation analysis, but none of these were found to associate with the cancer phenotype [3].
  • Moreover, we identified a homozygous nonsense mutation in BACH1 in a FA-J patient-derived cell line and could not detect BACH1 protein in this cell line [16].
  • Here we describe the gene structure of human BACH1, including a newly identified promoter and an alternatively RNA-spliced truncated form of BACH1, designated BACH1t, abundantly transcribed in human testis [4].
  • Whereas expression of Bach1 appears ubiquitous, that of Bach2 is restricted to monocytes and neuronal cells [17].
  • The contact of fibrin with the apical surface of human umbilical vein endothelial cells (HUVEC) can induce capillary tube formation via the interaction of fibrin beta15-42 with a putative cell receptor (Chalupowicz, D. G., Chowdhury, Z. A., Bach, T. L., Barsigian, C., and Martinez, J. (1995) J. Cell Biol. 130, 207-215) [18].

Associations of BRIP1 with chemical compounds


Physical interactions of BRIP1

  • FANCJ directly interacts with MLH1 independent of BRCA1, through its helicase domain [24].

Enzymatic interactions of BRIP1

  • Here we report the crystal structure of the BRCT repeats of human BRCA1 bound to a phosphorylated BACH1 peptide at 2.3 A resolution [19].

Regulatory relationships of BRIP1

  • Consistent with this, we show that FANCJ can inhibit RAD51 strand exchange, an activity that is likely to be important for its role in controlling DNA repair through homologous recombination [25].

Co-localisations of BRIP1


Other interactions of BRIP1


Analytical, diagnostic and therapeutic context of BRIP1

  • On the basis of published data and sequence analysis we suggest that SUVi/BACH1 may represent a novel subfamily of mammalian helicases, functioning in the processing of lesions induced by different genotoxic agents [31].
  • Northern blot analysis revealed that BACH1 was expressed in all tissues examined [32].
  • However, Bach1 did not bind to the MARE-like element in electrophoretic mobility shift assays (EMSA) [33].
  • Results recently obtained in animal models, discussed here by Jean François Bach particularly with anti-CD3 and anti-CD4 monoclonal antibodies, indicate that reestablishment of tolerance to self antigens is a feasible goal [34].
  • Hemispheric dominance in the processing of J.S. Bach fugues: a transcranial Doppler sonography (TCD) study with musicians [35].


  1. The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia. Levran, O., Attwooll, C., Henry, R.T., Milton, K.L., Neveling, K., Rio, P., Batish, S.D., Kalb, R., Velleuer, E., Barral, S., Ott, J., Petrini, J., Schindler, D., Hanenberg, H., Auerbach, A.D. Nat. Genet. (2005) [Pubmed]
  2. The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair. Bridge, W.L., Vandenberg, C.J., Franklin, R.J., Hiom, K. Nat. Genet. (2005) [Pubmed]
  3. BACH1 Ser919Pro variant and breast cancer risk. Vahteristo, P., Yliannala, K., Tamminen, A., Eerola, H., Blomqvist, C., Nevanlinna, H. BMC Cancer (2006) [Pubmed]
  4. Transcription factor BACH1 is recruited to the nucleus by its novel alternative spliced isoform. Kanezaki, R., Toki, T., Yokoyama, M., Yomogida, K., Sugiyama, K., Yamamoto, M., Igarashi, K., Ito, E. J. Biol. Chem. (2001) [Pubmed]
  5. Mutational analysis of the LMO4 gene, encoding a BRCA1-interacting protein, in breast carcinomas. Sutherland, K.D., Visvader, J.E., Choong, D.Y., Sum, E.Y., Lindeman, G.J., Campbell, I.G. Int. J. Cancer (2003) [Pubmed]
  6. A novel breast cancer-associated BRIP1 (FANCJ/BACH1) germ-line mutation impairs protein stability and function. De Nicolo, A., Tancredi, M., Lombardi, G., Flemma, C.C., Barbuti, S., Di Cristofano, C., Sobhian, B., Bevilacqua, G., Drapkin, R., Caligo, M.A. Clin. Cancer Res. (2008) [Pubmed]
  7. Which complementary and alternative therapies benefit which conditions? A survey of the opinions of 223 professional organizations. Long, L., Huntley, A., Ernst, E. Complementary therapies in medicine. (2001) [Pubmed]
  8. Acute treatment of inpatients with psychotic symptoms using Acceptance and Commitment Therapy: pilot results. Gaudiano, B.A., Herbert, J.D. Behaviour research and therapy. (2006) [Pubmed]
  9. Truncating mutations in the Fanconi anemia J gene BRIP1 are low-penetrance breast cancer susceptibility alleles. Seal, S., Thompson, D., Renwick, A., Elliott, A., Kelly, P., Barfoot, R., Chagtai, T., Jayatilake, H., Ahmed, M., Spanova, K., North, B., McGuffog, L., Evans, D.G., Eccles, D., Easton, D.F., Stratton, M.R., Rahman, N. Nat. Genet. (2006) [Pubmed]
  10. On "The effect of intravenous lidocaine on nociceptive processing in diabetic neuropathy" by Bach et al. in Pain, 40 (1990) 29-34. Coe, A.J., Dean, J., McClone, F., Leijon, G., Bowsher, D. Pain (1991) [Pubmed]
  11. Validation of a model of lung cancer risk prediction among smokers. Cronin, K.A., Gail, M.H., Zou, Z., Bach, P.B., Virtamo, J., Albanes, D. J. Natl. Cancer Inst. (2006) [Pubmed]
  12. 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. Rutter, J.L., Smith, A.M., Dávila, M.R., Sigurdson, A.J., Giusti, R.M., Pineda, M.A., Doody, M.M., Tucker, M.A., Greene, M.H., Zhang, J., Struewing, J.P. Hum. Mutat. (2003) [Pubmed]
  13. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Cantor, S., Drapkin, R., Zhang, F., Lin, Y., Han, J., Pamidi, S., Livingston, D.M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  14. The DNA helicase BRIP1 is defective in Fanconi anemia complementation group J. Levitus, M., Waisfisz, Q., Godthelp, B.C., de Vries, Y., Hussain, S., Wiegant, W.W., Elghalbzouri-Maghrani, E., Steltenpool, J., Rooimans, M.A., Pals, G., Arwert, F., Mathew, C.G., Zdzienicka, M.Z., Hiom, K., De Winter, J.P., Joenje, H. Nat. Genet. (2005) [Pubmed]
  15. Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer. Gupta, R., Sharma, S., Sommers, J.A., Jin, Z., Cantor, S.B., Brosh, R.M. J. Biol. Chem. (2005) [Pubmed]
  16. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Litman, R., Peng, M., Jin, Z., Zhang, F., Zhang, J., Powell, S., Andreassen, P.R., Cantor, S.B. Cancer Cell (2005) [Pubmed]
  17. Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site. Oyake, T., Itoh, K., Motohashi, H., Hayashi, N., Hoshino, H., Nishizawa, M., Yamamoto, M., Igarashi, K. Mol. Cell. Biol. (1996) [Pubmed]
  18. Endothelial cell VE-cadherin functions as a receptor for the beta15-42 sequence of fibrin. Bach, T.L., Barsigian, C., Yaen, C.H., Martinez, J. J. Biol. Chem. (1998) [Pubmed]
  19. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. Shiozaki, E.N., Gu, L., Yan, N., Shi, Y. Mol. Cell (2004) [Pubmed]
  20. BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains. Magnard, C., Bachelier, R., Vincent, A., Jaquinod, M., Kieffer, S., Lenoir, G.M., Venezia, N.D. Oncogene (2002) [Pubmed]
  21. Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Botuyan, M.V., Nominé, Y., Yu, X., Juranic, N., Macura, S., Chen, J., Mer, G. Structure (Camb.) (2004) [Pubmed]
  22. Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene. Suzuki, H., Tashiro, S., Sun, J., Doi, H., Satomi, S., Igarashi, K. J. Biol. Chem. (2003) [Pubmed]
  23. Iron(II)-catalyzed sulfimidation and [2,3]-sigmatropic rearrangement of propargyl sulfides with tert-butoxycarbonyl azide. Access to N-allenylsulfenimides. Bacci, J.P., Greenman, K.L., Van Vranken, D.L. J. Org. Chem. (2003) [Pubmed]
  24. The FANCJ/MutLalpha interaction is required for correction of the cross-link response in FA-J cells. Peng, M., Litman, R., Xie, J., Sharma, S., Brosh, R.M., Cantor, S.B. EMBO J. (2007) [Pubmed]
  25. FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange. Sommers, J.A., Rawtani, N., Gupta, R., Bugreev, D.V., Mazin, A.V., Cantor, S.B., Brosh, R.M. J. Biol. Chem. (2009) [Pubmed]
  26. FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein. Gupta, R., Sharma, S., Sommers, J.A., Kenny, M.K., Cantor, S.B., Brosh, R.M. Blood (2007) [Pubmed]
  27. Functional interplay between BRCA2/FancD1 and FancC in DNA repair. Kitao, H., Yamamoto, K., Matsushita, N., Ohzeki, M., Ishiai, M., Takata, M. J. Biol. Chem. (2006) [Pubmed]
  28. Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1. Wang, Q., Zhang, H., Guerrette, S., Chen, J., Mazurek, A., Wilson, T., Slupianek, A., Skorski, T., Fishel, R., Greene, M.I. Oncogene (2001) [Pubmed]
  29. BRCA1 interacts with FHL2 and enhances FHL2 transactivation function. Yan, J., Zhu, J., Zhong, H., Lu, Q., Huang, C., Ye, Q. FEBS Lett. (2003) [Pubmed]
  30. Characterization of COBRA1 in human breast cancer cell lines using a new polyclonal antibody against COBRA1. Zhu, J., Song, S., Jiang, Z., Yan, J., Lu, Q., Huang, C., Ye, Q. IUBMB Life (2004) [Pubmed]
  31. SUVi and BACH1: a new subfamily of mammalian helicases? Menichini, P., Linial, M. Mutat. Res. (2001) [Pubmed]
  32. Characterization of a human homolog (BACH1) of the mouse Bach1 gene encoding a BTB-basic leucine zipper transcription factor and its mapping to chromosome 21q22.1. Ohira, M., Seki, N., Nagase, T., Ishikawa, K., Nomura, N., Ohara, O. Genomics (1998) [Pubmed]
  33. The promoter of mouse transcription repressor bach1 is regulated by Sp1 and trans-activated by Bach1. Sun, J., Muto, A., Hoshino, H., Kobayashi, A., Nishimura, S., Yamamoto, M., Hayashi, N., Ito, E., Igarashi, K. J. Biochem. (2001) [Pubmed]
  34. Immunosuppressive therapy of autoimmune diseases. Bach, J.F. Trends Pharmacol. Sci. (1993) [Pubmed]
  35. Hemispheric dominance in the processing of J.S. Bach fugues: a transcranial Doppler sonography (TCD) study with musicians. Vollmer-Haase, J., Finke, K., Hartje, W., Bulla-Hellwig, M. Neuropsychologia. (1998) [Pubmed]
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