Wikipedia

BIRC5

BIRC5 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[33][34]

BIRC5
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген Сурвивин[d][1]
Молекуляр функция peptidase inhibitor activity[d][2], cobalt ion binding[d][3], chaperone binding[d][4], гомодимеризация белка[d][5][6][3], связывание с ионом металла[d][2], ubiquitin-protein transferase activity[d][7], tubulin binding[d][8], cysteine-type endopeptidase inhibitor activity involved in apoptotic process[d][8], связывание с белками плазмы[d][9][10][11][…], связывание похожих белков[d][12][13], protein heterodimerization activity[d][5], enzyme binding[d][14], microtubule binding[d][15][8], zinc ion binding[d][3][6], cysteine-type endopeptidase inhibitor activity[d][7][7], cysteine-type endopeptidase inhibitor activity[d][2], microtubule binding[d][16] һәм cysteine-type endopeptidase inhibitor activity involved in apoptotic process[d][17]
Күзәнәк компоненты цитозоль[d][2][18], веретено деления[d][2], Хромосома[2], нуклеоплазма[d][2], chromosome passenger complex[d][19][18], ядерная хромосома[d][14], interphase microtubule organizing center[d][8], spindle microtubule[d][8][20], центриоль[d][8], cytoplasmic microtubule[d][8], цитоскелет[d][2], микротрубочка[d][2], кинетохор[d][2], midbody[d][2][21][22], цитоплазма[7][5][23][…], центромера[d][2][14][22], төш[7][24][25][…], төш[2][26][10][…], цитоплазма[2][26][27][…] һәм spindle microtubule[d][17]
Биологик процесс negative regulation of peptidase activity[d][2], negative regulation of cysteine-type endopeptidase activity involved in apoptotic process[d][8][28], ДНК-зависимая регуляция транскрипции[d][7], inhibition of cysteine-type endopeptidase activity involved in apoptotic process[d][7], establishment of chromosome localization[d][29], chromosome segregation[d][2], positive regulation of mitotic cell cycle[d][5], positive regulation of exit from mitosis[d][29], транскрипция, ДНК-зависимая[d][7], деление клетки[d][29][7], фосфорилация белка[d][30], mitotic spindle assembly[d][17], regulation of signal transduction[d][7], G2/M transition of mitotic cell cycle[d][8], позитивная регуляция пролиферации клеток[d][31], protein-containing complex localization[d][32], клеточный цикл[d][2], negative regulation of transcription, DNA-templated[d][10], апоптоз[d][2], regulation of apoptotic process[d][2], негативная регуляция апоптоза[d][16][26][27], regulation of mitotic cell cycle[d][7], митоз[d][5], ишетү[d][26], mitotic cytokinesis[d][29], mitotic spindle assembly checkpoint signaling[d][29], cytokine-mediated signaling pathway[d][2], protein ubiquitination[d][7], negative regulation of endopeptidase activity[d][2], деление клетки[d][2] һәм negative regulation of cysteine-type endopeptidase activity involved in apoptotic process[d][17]
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 GOA
  3. ↑ 3,0 3,1 3,2 Kleman J. P. Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions // Mol. Cell — Cell Press, Elsevier BV, 2000. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(05)00020-1; doi:10.1016/S1097-2765(00)00019-8 — PMID:10949039
  4. ↑ Kang B. H., Altieri D. C. Hsp60 regulation of tumor cell apoptosis // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2008. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M705904200 — PMID:18086682
  5. ↑ 5,0 5,1 5,2 5,3 5,4 Noton E. A., Colnaghi R., Tate S. et al. Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2006. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M508773200 — PMID:16291752
  6. ↑ 6,0 6,1 Verdecia M. A., H Huang, E Dutil et al. Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement // Nature structural biology — NPG, 2000. — ISSN 1072-8368; 2331-365X — doi:10.1038/76838 — PMID:10876248
  7. ↑ 7,00 7,01 7,02 7,03 7,04 7,05 7,06 7,07 7,08 7,09 7,10 7,11 GOA
  8. ↑ 8,0 8,1 8,2 8,3 8,4 8,5 8,6 8,7 8,8 F Li, G Ambrosini, Chu E. Y. et al. Control of apoptosis and mitotic spindle checkpoint by survivin // Nature / M. Skipper — NPG, Springer Science+Business Media, 1998. — ISSN 1476-4687; 0028-0836 — doi:10.1038/25141 — PMID:9859993
  9. ↑ Earnshaw W. C., Khaled W. Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M311299200 — PMID:14610074
  10. ↑ 10,0 10,1 10,2 Cooper Z. A., Elenitoba-Johnson K. S. J. Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity, Acetylation Directs Survivin Nuclear Localization to Repress STAT3 Oncogenic Activity // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2010. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M110.152777 — PMID:20826784
  11. ↑ Jobst-Schwan T., Nielsen R., Eckardt K. Renal uptake of the antiapoptotic protein survivin is mediated by megalin at the apical membrane of the proximal tubule // American journal of physiology: Renal Physiology — 2013. — ISSN 1931-857X; 1522-1466; 0363-6127 — doi:10.1152/AJPRENAL.00546.2012 — PMID:23825075
  12. ↑ Knauer S. K. The Survivin-Crm1 interaction is essential for chromosomal passenger complex localization and function // EMBO Rep. — NPG, 2006. — ISSN 1469-221X; 1469-3178 — doi:10.1038/SJ.EMBOR.7400824 — PMID:17099693
  13. ↑ Kurt H. Impairment of glioma stem cell survival and growth by a novel inhibitor for Survivin-Ran protein complex // Clin. Cancer Res. / K. Flaherty — American Association for Cancer Research, 2012. — ISSN 1078-0432; 1557-3265 — doi:10.1158/1078-0432.CCR-12-0647 — PMID:23251006
  14. ↑ 14,0 14,1 14,2 Iglesias P. A. Chromosome alignment and segregation regulated by ubiquitination of survivin // Science / H. Thorp — Northern America: AAAS, 2005. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.1120160 — PMID:16322459
  15. ↑ Antipova N. V. Survivin monomer plays an essential role in apoptosis regulation, Survivin Monomer Plays an Essential Role in Apoptosis Regulation // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2011. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M111.237586 — PMID:21536684
  16. ↑ 16,0 16,1 Antipova N. V. Survivin monomer plays an essential role in apoptosis regulation, Survivin Monomer Plays an Essential Role in Apoptosis Regulation // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2011. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M111.237586 — PMID:21536684
  17. ↑ 17,0 17,1 17,2 17,3 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
  18. ↑ 18,0 18,1 Altieri D. C. A survivin-ran complex regulates spindle formation in tumor cells // Mol. Cell. Biol. — ASM, 2008. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.02039-07 — PMID:18591255
  19. ↑ Sampath S. C., Ohi R., Leismann O. et al. The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly // Cell — Cell Press, Elsevier BV, 2004. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2004.06.026 — PMID:15260989
  20. ↑ D S O'Connor, D Grossman, J Plescia et al. Regulation of apoptosis at cell division by p34cdc2 phosphorylation of survivin // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2000. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.240390697 — PMID:11069302
  21. ↑ Samuel T., Okada K., Hyer M. et al. cIAP1 Localizes to the nuclear compartment and modulates the cell cycle // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2005. — ISSN 0008-5472; 1538-7445 — PMID:15665297
  22. ↑ 22,0 22,1 Uren A., Vaux D. L. Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype // Curr. Biol. — United Kingdom: Cell Press, Elsevier BV, 2000. — ISSN 0960-9822; 1879-0445 — doi:10.1016/S0960-9822(00)00769-7 — PMID:11084331
  23. ↑ Stauber R., Schmidtmann I., Knauer S. K. Expression analysis suggests a potential cytoprotective role of Birc5 in the inner ear. // Mol. Cell. Neurosci. — Elsevier BV, 2010. — ISSN 1044-7431; 1095-9327 — doi:10.1016/J.MCN.2010.07.003 — PMID:20627126
  24. ↑ Stauber R., Knauer S. K. An otoprotective role for the apoptosis inhibitor protein survivin // Cell Death Dis. — London: Nature Publishing Group, 2010. — ISSN 2041-4889 — doi:10.1038/CDDIS.2010.25 — PMID:21364656
  25. ↑ Samuel T., Okada K., Hyer M. et al. cIAP1 Localizes to the nuclear compartment and modulates the cell cycle // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2005. — ISSN 0008-5472; 1538-7445 — PMID:15665297
  26. ↑ 26,0 26,1 26,2 26,3 Stauber R., Schmidtmann I., Knauer S. K. Expression analysis suggests a potential cytoprotective role of Birc5 in the inner ear. // Mol. Cell. Neurosci. — Elsevier BV, 2010. — ISSN 1044-7431; 1095-9327 — doi:10.1016/J.MCN.2010.07.003 — PMID:20627126
  27. ↑ 27,0 27,1 Stauber R., Knauer S. K. An otoprotective role for the apoptosis inhibitor protein survivin // Cell Death Dis. — London: Nature Publishing Group, 2010. — ISSN 2041-4889 — doi:10.1038/CDDIS.2010.25 — PMID:21364656
  28. ↑ Marusawa H., Matsuzawa S., Welsh K. et al. HBXIP functions as a cofactor of survivin in apoptosis suppression // EMBO J. — NPG, 2003. — ISSN 0261-4189; 1460-2075 — doi:10.1093/EMBOJ/CDG263 — PMID:12773388
  29. ↑ 29,0 29,1 29,2 29,3 29,4 Kops G., Agami R., Medema R. H. Survivin is required for a sustained spindle checkpoint arrest in response to lack of tension // EMBO J. — NPG, 2003. — ISSN 0261-4189; 1460-2075 — doi:10.1093/EMBOJ/CDG307 — PMID:12805209
  30. ↑ Rachel M A Barrett, Colnaghi R., Wheatley S. P. Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro // Cell Cycle / M. Blagosklonny — Landes Bioscience, Taylor & Francis, 2011. — ISSN 1538-4101; 1551-4005 — doi:10.4161/CC.10.3.14758 — PMID:21252625
  31. ↑ McNeish I. A. Survivin: a protein with dual roles in mitosis and apoptosis // International Review of Cytology — Elsevier BV, 2005. — ISSN 0074-7696; 2163-5854 — doi:10.1016/S0074-7696(05)47002-3 — PMID:16344111
  32. ↑ Vader G., Medema R. H. Survivin mediates targeting of the chromosomal passenger complex to the centromere and midbody // EMBO Rep. — NPG, 2006. — ISSN 1469-221X; 1469-3178 — doi:10.1038/SJ.EMBOR.7400562 — PMID:16239925
  33. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  34. ↑ 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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