Wikipedia

BRCA2

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

BRCA2
Сурәт
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген BRCA2[d][1]
Молекулярная 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]
Биологический 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[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

Искәрмәләр үзгәртү

  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 BV, 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 BV, 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 BV, 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 BV, 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 BV, 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 BV, 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 BV, 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 BV, 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. 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. ↑ Biswas K., Das R., Alter B. P. et al. A comprehensive functional characterization of BRCA2 variants associated with Fanconi anemia using mouse ES cell-based assay // Blood — American Society of Hematology, Elsevier BV, 2011. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2010-12-324541 — PMID:21719596
  36. ↑ Biswas K., Das R., Alter B. P. et al. A comprehensive functional characterization of BRCA2 variants associated with Fanconi anemia using mouse ES cell-based assay // Blood — American Society of Hematology, Elsevier BV, 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. 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 архивланды. 18 сентябрь, 2017 тикшерелгән.
  42. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар үзгәртү

  • 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.)


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