BRCA2

BRCA2
Рәсем
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген BRCA2[d][1]
Молекуляр функция ДНК-связывающий[d][2], H4 histone acetyltransferase activity[d][3], H3 histone acetyltransferase activity[d][3], protease binding[d][4], histone acetyltransferase activity[d][5], связывание с белками плазмы[d][6][7][8][…], gamma-tubulin binding[d][9], single-stranded DNA binding[d][10], protein C-terminus binding[d][11], связывание похожих белков[d][12][13], protease binding[d][14][15], single-stranded DNA binding[d][16][15], histone acetyltransferase activity[d][17][15], связывание с белками плазмы[d][18][19][20][…], protein C-terminus binding[d][21][15], связывание похожих белков[d][22][23][15] һәм gamma-tubulin binding[d][24][15]
Күзәнәк компоненты центросома[d][25][9], BRCA2-MAGE-D1 complex[d][8], secretory granule[d][26], нуклеоплазма[d][2][2], центр организации микротрубочек[d][2], төш[27][27][28][…], цитоскелет[d][2], lateral element[d][11], цитоплазма[2][2], цитозоль[d][2], protein-containing complex[d][11][11], lateral element[d][21][15], төш[2][2][29][…], нуклеоплазма[d][27][27][15], центросома[d][24][30][15], цитозоль[d][27][15], secretory granule[d][31][15] һәм BRCA2-MAGE-D1 complex[d][18][15]
Биологик процесс chordate embryonic development[d][2], Эксцизионная репарация нуклеотидов[d][32], intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator[d][2], DNA recombination[d][2], regulation of cytokinesis[d][2], replication fork protection[d][2], centrosome duplication[d][9], male meiosis I[d][2], negative regulation of mammary gland epithelial cell proliferation[d][8], positive regulation of mitotic cell cycle[d][2], chromosome organization[d][2], развитие яичников[d][2], inner cell mass cell proliferation[d][2], ДНК-зависимая позитивная регуляция транскрипции[d][33], telomere maintenance via recombination[d][2], развитие мозга[d][2], oocyte maturation[d][2], histone H3 acetylation[d][3], Сперматогенез[d][2], intrinsic apoptotic signaling pathway in response to DNA damage[d][2], establishment of protein localization to telomere[d][2][34], histone H4 acetylation[d][3], cellular response to DNA damage stimulus[d][2][2], клеточный цикл[d][2], пролиферация клеток[d][2], response to gamma radiation[d][2], response to UV-C[d][2], response to X-ray[d][2], DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator[d][2], mitotic recombination-dependent replication fork processing[d][34], double-strand break repair via homologous recombination[d][35][27][27][…], репарация ДНК[d][2][2], double-strand break repair[d][32][2], mitotic cytokinesis[d][9], гемопоэз[d][2], telomere maintenance via recombination[d][27][15], double-strand break repair via homologous recombination[d][36][2][2][…], oocyte maturation[d][27][15], inner cell mass cell proliferation[d][27][15], Эксцизионная репарация нуклеотидов[d][37][15], DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator[d][27][15], male meiosis I[d][27][15], Сперматогенез[d][27][15], развитие мозга[d][27][15], response to nutrient[d][15], развитие яичников[d][27][15], response to X-ray[d][27][15], response to UV-C[d][27][15], response to gamma radiation[d][27][15], meiotic DNA repair synthesis involved in reciprocal meiotic recombination[d][15], гемопоэз[d][27][15], развитие молочных желёз[d][15], homologous chromosome orientation involved in meiotic metaphase I plate congression[d][15], response to estradiol[d][15], regulation of cytokinesis[d][27][15], negative regulation of mammary gland epithelial cell proliferation[d][18][15], multicellular organism growth[d][15], intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator[d][27][15], DNA synthesis involved in double-strand break repair via homologous recombination[d][15], histone H3 acetylation[d][38][15], histone H4 acetylation[d][38][15], ДНК-зависимая позитивная регуляция транскрипции[d][39][15], positive regulation of mitotic cell cycle[d][27][15], replication fork protection[d][27][15], centrosome duplication[d][24][15], контрольная точка мейотической рекомбинации[d][15], establishment of protein localization to telomere[d][27][40][15] һәм mitotic recombination-dependent replication fork processing[d][40][15]
Изображение Gene Atlas

BRCA2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[41][42]

Искәрмәләр

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 2,35 2,36 2,37 2,38 2,39 GOA
  3. ↑ 3,0 3,1 3,2 3,3 H. Siddique, Zou J. P., Rao V. N. et al. The BRCA2 is a histone acetyltransferase // Oncogene — NPG, 1998. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1202003 — PMID:9619837
  4. ↑ Schoenfeld A. R. BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage // Mol. Cell. Biol. — ASM, 2004. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.24.17.7444-7455.2004 — PMID:15314155
  5. ↑ F Fuks, J Milner, T Kouzarides BRCA2 associates with acetyltransferase activity when bound to P/CAF // Oncogene — NPG, 1998. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1202475 — PMID:9824164
  6. ↑ Daniel D. C. Highlight: BRCA1 and BRCA2 proteins in breast cancer // Microsc. Res. Tech. — Wiley-Blackwell, 2002. — ISSN 1059-910X; 1097-0029 — doi:10.1002/JEMT.10178 — PMID:12242698
  7. ↑ Band V. Centrobin: a novel daughter centriole-associated protein that is required for centriole duplication // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2005. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200506185 — PMID:16275750
  8. ↑ 8,0 8,1 8,2 Band V. BRCA2 suppresses cell proliferation via stabilizing MAGE-D1 // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2005. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-05-0018 — PMID:15930293
  9. ↑ 9,0 9,1 9,2 9,3 Nakanishi A. Interference with BRCA2, which localizes to the centrosome during S and early M phase, leads to abnormal nuclear division // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier, 2007. — ISSN 0006-291X; 1090-2104 — doi:10.1016/J.BBRC.2007.01.100 — PMID:17286961
  10. ↑ Carreira A. Purified human BRCA2 stimulates RAD51-mediated recombination // Nature / M. Skipper — NPG, Springer Science+Business Media, 2010. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE09399 — PMID:20729832
  11. ↑ 11,0 11,1 11,2 11,3 Couch F. J. Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells // Mol. Cell — Cell Press, Elsevier, 1998. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(00)80276-2 — PMID:9774970
  12. ↑ Omi T., Morimatsu M. Valine 1532 of human BRC repeat 4 plays an important role in the interaction between BRCA2 and RAD51 // FEBS Letters — Elsevier, 2011. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2011.05.027 — PMID:21601571
  13. ↑ Malivert L., McIlwraith M. J., Zhang X. et al. Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor // Nat. Struct. Mol. Biol. — USA: NPG, 2014. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB.2899 — PMID:25282148
  14. ↑ Schoenfeld A. R. BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage // Mol. Cell. Biol. — ASM, 2004. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.24.17.7444-7455.2004 — PMID:15314155
  15. ↑ 15,00 15,01 15,02 15,03 15,04 15,05 15,06 15,07 15,08 15,09 15,10 15,11 15,12 15,13 15,14 15,15 15,16 15,17 15,18 15,19 15,20 15,21 15,22 15,23 15,24 15,25 15,26 15,27 15,28 15,29 15,30 15,31 15,32 15,33 15,34 15,35 15,36 15,37 15,38 15,39 15,40 15,41 15,42 15,43 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
  16. ↑ Carreira A. Purified human BRCA2 stimulates RAD51-mediated recombination // Nature / M. Skipper — NPG, Springer Science+Business Media, 2010. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE09399 — PMID:20729832
  17. ↑ F Fuks, J Milner, T Kouzarides BRCA2 associates with acetyltransferase activity when bound to P/CAF // Oncogene — NPG, 1998. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1202475 — PMID:9824164
  18. ↑ 18,0 18,1 18,2 Band V. BRCA2 suppresses cell proliferation via stabilizing MAGE-D1 // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2005. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-05-0018 — PMID:15930293
  19. ↑ A Ashworth Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals // Mol. Cell. Biol. — ASM, 1999. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.19.7.4633 — PMID:10373512
  20. ↑ Davies O. R. Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats // Nat. Struct. Mol. Biol. — USA: NPG, 2007. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB1251 — PMID:17515903
  21. ↑ 21,0 21,1 Couch F. J. Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells // Mol. Cell — Cell Press, Elsevier, 1998. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(00)80276-2 — PMID:9774970
  22. ↑ Malivert L., McIlwraith M. J., Zhang X. et al. Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor // Nat. Struct. Mol. Biol. — USA: NPG, 2014. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB.2899 — PMID:25282148
  23. ↑ Omi T., Morimatsu M. Valine 1532 of human BRC repeat 4 plays an important role in the interaction between BRCA2 and RAD51 // FEBS Letters — Elsevier, 2011. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2011.05.027 — PMID:21601571
  24. ↑ 24,0 24,1 24,2 Nakanishi A. Interference with BRCA2, which localizes to the centrosome during S and early M phase, leads to abnormal nuclear division // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier, 2007. — ISSN 0006-291X; 1090-2104 — doi:10.1016/J.BBRC.2007.01.100 — PMID:17286961
  25. ↑ Cappelli E., Townsend S., Griffin C. et al. Homologous recombination proteins are associated with centrosomes and are required for mitotic stability // Exp. Cell. Res. — Academic Press, Elsevier, 2011. — ISSN 0014-4827; 1090-2422 — doi:10.1016/J.YEXCR.2011.01.021 — PMID:21276791
  26. ↑ King M. BRCA1 is secreted and exhibits properties of a granin // Nature Genetics / M. Axton, T. Faial — NPG, 1996. — ISSN 1061-4036; 1546-1718 — doi:10.1038/NG0396-303 — PMID:8589722
  27. ↑ 27,00 27,01 27,02 27,03 27,04 27,05 27,06 27,07 27,08 27,09 27,10 27,11 27,12 27,13 27,14 27,15 27,16 27,17 27,18 27,19 27,20 27,21 27,22 27,23 GOA
  28. ↑ Chen P. L., Chen C. F., Y. Chen et al. The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.9.5287 — PMID:9560268
  29. ↑ Chen P. L., Chen C. F., Y. Chen et al. The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.9.5287 — PMID:9560268
  30. ↑ Cappelli E., Townsend S., Griffin C. et al. Homologous recombination proteins are associated with centrosomes and are required for mitotic stability // Exp. Cell. Res. — Academic Press, Elsevier, 2011. — ISSN 0014-4827; 1090-2422 — doi:10.1016/J.YEXCR.2011.01.021 — PMID:21276791
  31. ↑ King M. BRCA1 is secreted and exhibits properties of a granin // Nature Genetics / M. Axton, T. Faial — NPG, 1996. — ISSN 1061-4036; 1546-1718 — doi:10.1038/NG0396-303 — PMID:8589722
  32. ↑ 32,0 32,1 Cipak L. The role of BRCA2 in replication-coupled DNA interstrand cross-link repair in vitro // Nat. Struct. Mol. Biol. — USA: NPG, 2006. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB1120 — PMID:16845393
  33. ↑ J Milner, B Ponder, L Hughes-Davies et al. Transcriptional activation functions in BRCA2 // Nature / M. Skipper — NPG, Springer Science+Business Media, 1997. — ISSN 1476-4687; 0028-0836 — doi:10.1038/386772A0 — PMID:9126734
  34. ↑ 34,0 34,1 Carlos A. R., Blasco M. A., Benitez J. et al. BRCA2 acts as a RAD51 loader to facilitate telomere replication and capping // Nat. Struct. Mol. Biol. — USA: NPG, 2010. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB.1943 — PMID:21076401
  35. ↑ Kuznetsov S. G., Burkett S., R. Andrew Byrd A comprehensive functional characterization of BRCA2 variants associated with Fanconi anemia using mouse ES cell-based assay, A comprehensive functional characterization of BRCA2 variants associated with Fanconi anemia using mouse ES cell–based assay // Blood — American Society of Hematology, Elsevier, 2011. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2010-12-324541 — PMID:21719596
  36. ↑ Kuznetsov S. G., Burkett S., R. Andrew Byrd A comprehensive functional characterization of BRCA2 variants associated with Fanconi anemia using mouse ES cell-based assay, A comprehensive functional characterization of BRCA2 variants associated with Fanconi anemia using mouse ES cell–based assay // Blood — American Society of Hematology, Elsevier, 2011. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2010-12-324541 — PMID:21719596
  37. ↑ Cipak L. The role of BRCA2 in replication-coupled DNA interstrand cross-link repair in vitro // Nat. Struct. Mol. Biol. — USA: NPG, 2006. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB1120 — PMID:16845393
  38. ↑ 38,0 38,1 H. Siddique, Zou J. P., Rao V. N. et al. The BRCA2 is a histone acetyltransferase // Oncogene — NPG, 1998. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1202003 — PMID:9619837
  39. ↑ J Milner, B Ponder, L Hughes-Davies et al. Transcriptional activation functions in BRCA2 // Nature / M. Skipper — NPG, Springer Science+Business Media, 1997. — ISSN 1476-4687; 0028-0836 — doi:10.1038/386772A0 — PMID:9126734
  40. ↑ 40,0 40,1 Carlos A. R., Blasco M. A., Benitez J. et al. BRCA2 acts as a RAD51 loader to facilitate telomere replication and capping // Nat. Struct. Mol. Biol. — USA: NPG, 2010. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB.1943 — PMID:21076401
  41. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  42. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)

Content Disclaimer

Informasi ini disarikan dari Wikipedia dan disajikan kembali untuk tujuan edukasi. Konten tersedia di bawah lisensi CC BY-SA 3.0. Kami tidak bertanggung jawab atas ketidakakuratan data yang bersumber dari kontribusi publik tersebut.

  1. The information displayed on this website is sourced in part or in whole from Wikipedia and has been adapted for the purpose of restating it. We strive to provide accurate and relevant information, however:
  2. There is no guarantee of absolute accuracy. Wikipedia is an open, collaborative project that can be edited by anyone, so information is subject to change.
  3. It is not intended to constitute professional advice. The content displayed is for informational and educational purposes only. For important decisions (e.g., medical, legal, or financial), please consult a professional.
  4. Content copyright. Wikipedia is licensed under the Creative Commons Attribution-ShareAlike License (CC BY-SA). This means that content may be reused with appropriate attribution and shared under a similar license.
  5. Responsible use. Any risk arising from the use of information from this website is entirely the responsibility of the user.