ATM (ген)

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/ATM (ген) latin yazuında])
ATM
Сурәт
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген ATM[d][1]
Молекулярная функция трансферазная активность[d][2], ДНК-связывающий[d][2], нуклеотид-связывающий[d][2], protein kinase activity[d][2], DNA-dependent protein kinase activity[d][3], protein dimerization activity[d][3], protein N-terminus binding[d][4], 1-phosphatidylinositol-3-kinase activity[d][4], kinase activity[d][2][2], protein serine/threonine kinase activity[d][5][5][5][…], связывание с белками плазмы[d][6][4][7][…], АТФ-связанные[d][2], protein-containing complex binding[d][3] һәм protein serine/threonine kinase activity[d][2][2][2][…]
Күзәнәк компоненты Цитоплазма[2], DNA repair complex[d][8], Веретено деления[d][2], нуклеоплазма[d][2], Теломеры[d][9], цитоплазматическая везикула[d][2], Төш[5][5][10], ядрышко[d][11] һәм Төш[2][2][12][…]
Биологический процесс somitogenesis[d][2], response to ionizing radiation[d][2][2][4][…], neuron apoptotic process[d][2], reciprocal meiotic recombination[d][13], DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest[d][2], response to hypoxia[d][2], female gamete generation[d][2], determination of adult lifespan[d][2], фосфорилирование[d][2], establishment of protein-containing complex localization to telomere[d][14], meiotic telomere clustering[d][2], peptidyl-serine autophosphorylation[d][15], DNA damage checkpoint signaling[d][5], regulation of telomerase activity[d][16], positive regulation of telomerase catalytic core complex assembly[d][14], positive regulation of telomere maintenance via telomerase[d][2][2], positive regulation of neuron death[d][2], mitotic spindle assembly checkpoint signaling[d][17], oocyte development[d][2], lipoprotein catabolic process[d][2], regulation of cell cycle[d][2], фосфорилация белка[d][18][2][19], развитие сердца[d][2], развитие мозга[d][2], positive regulation of neuron apoptotic process[d][2], negative regulation of telomere capping[d][18], positive regulation of telomere maintenance via telomere lengthening[d][16][18], peptidyl-serine phosphorylation[d][12][20], cellular response to gamma radiation[d][21][22], intrinsic apoptotic signaling pathway in response to DNA damage[d][5], V(D)J-рекомбинация[d][2], positive regulation of apoptotic process[d][23], regulation of cellular response to heat[d][2], pre-B cell allelic exclusion[d][2][2], клеточный цикл[d][2], histone mRNA catabolic process[d][24], cellular response to nitrosative stress[d][25], positive regulation of DNA damage response, signal transduction by p53 class mediator[d][20], double-strand break repair via nonhomologous end joining[d][2], negative regulation of B cell proliferation[d][23], передача сигнала[d][13], establishment of RNA localization to telomere[d][14], апоптоз[d][2], Репликация ДНК[d][2], DNA double-strand break processing[d][2], regulation of signal transduction by p53 class mediator[d][2], regulation of autophagy[d][25][2], phosphatidylinositol-3-phosphate biosynthetic process[d][2], cellular response to X-ray[d][12], double-strand break repair via homologous recombination[d][2], regulation of apoptotic process[d][2], negative regulation of TORC1 signaling[d][26][5], ovarian follicle development[d][2], immune system process[d][2], immunoglobulin production[d][2], DNA damage induced protein phosphorylation[d][27][20], male meiotic nuclear division[d][2], female meiotic nuclear division[d][2], развитие яичников[d][2], post-embryonic development[d][2], multicellular organism growth[d][2], protein autophosphorylation[d][27][20][3], thymus development[d][2], chromosome organization involved in meiotic cell cycle[d][2], репарация ДНК[d][5][5], cellular response to DNA damage stimulus[d][28][29][30][…], regulation of telomere maintenance via telomerase[d][14], positive regulation of DNA catabolic process[d][2], regulation of microglial cell activation[d][2], regulation of cellular response to gamma radiation[d][2], positive regulation of response to DNA damage stimulus[d][2], telomere maintenance[d][5], replicative senescence[d][9][2], pre-B cell allelic exclusion[d][2], фосфорилация белка[d][18][19], regulation of autophagy[d][25], positive regulation of telomere maintenance via telomerase[d][2], negative regulation of TORC1 signaling[d][26], DNA damage checkpoint signaling[d][2][2][31], telomere maintenance[d][2][31], репарация ДНК[d][2][2], cellular response to DNA damage stimulus[d][23][15][3][…], intrinsic apoptotic signaling pathway in response to DNA damage[d][31], positive regulation of gene expression[d][32], positive regulation of cell migration[d][32], positive regulation of cell adhesion[d][2], положительная регуляция транскрипции РНК полимеразой II промотор[d][2], cellular response to retinoic acid[d][2], negative regulation of TORC1 signaling[d][25][31], intrinsic apoptotic signaling pathway in response to DNA damage[d][2][31], positive regulation of cell adhesion[d][2][2], положительная регуляция транскрипции РНК полимеразой II промотор[d][2][2], cellular response to retinoic acid[d][2][2], replicative senescence[d][9] һәм negative regulation of TORC1 signaling[d][25][2][31]

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

Искәрмәләр[үзгәртү | вики-текстны 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 2,40 2,41 2,42 2,43 2,44 2,45 2,46 2,47 2,48 2,49 2,50 2,51 2,52 2,53 2,54 2,55 2,56 2,57 2,58 2,59 2,60 2,61 2,62 2,63 2,64 2,65 2,66 2,67 2,68 2,69 2,70 2,71 2,72 2,73 2,74 2,75 2,76 2,77 2,78 2,79 2,80 2,81 2,82 GOA
  3. ↑ 3,0 3,1 3,2 3,3 3,4 Lee J., Paull T. T. ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex // Science / H. Thorp — AAAS, 2005. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.1108297 — PMID:15790808
  4. ↑ 4,0 4,1 4,2 4,3 S Kishi, Zhou X. Z., Y Ziv et al. Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2001. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M011534200 — PMID:11375976
  5. ↑ 5,00 5,01 5,02 5,03 5,04 5,05 5,06 5,07 5,08 5,09 5,10 GOA
  6. ↑ Aglipay J. A., Martin S. A., Tawara H. et al. ATM activation by ionizing radiation requires BRCA1-associated BAAT1 // 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.M510332200 — PMID:16452482
  7. ↑ Horejsí Z., Flynn H., Collis S. J. et al. CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for mTOR and SMG1 stability // Mol. Cell — Cell Press, Elsevier BV, 2010. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2010.08.037 — PMID:20864032
  8. ↑ Harper J. W., Gygi S. P. The histone demethylase LSD1/KDM1A promotes the DNA damage response // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2013. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.201302092 — PMID:24217620
  9. ↑ 9,0 9,1 9,2 Sedivy J. M. Telomere shortening triggers senescence of human cells through a pathway involving ATM, p53, and p21(CIP1), but not p16(INK4a) // Mol. Cell — Cell Press, Elsevier BV, 2004. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(04)00256-4 — PMID:15149599
  10. ↑ Zhao W., Groesser T., Dray E. NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability // Nucleic Acids Res. — OUP, University of Oxford, 2015. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKV859 — PMID:26323318
  11. ↑ Chen H., Han L., Tsai H. et al. PICT-1 is a key nucleolar sensor in DNA damage response signaling that regulates apoptosis through the RPL11-MDM2-p53 pathway // Oncotarget / M. Blagosklonny — Impact Journals LLC, 2016. — ISSN 1949-2553 — doi:10.18632/ONCOTARGET.13082 — PMID:27829214
  12. ↑ 12,0 12,1 12,2 Zhao W., Groesser T., Dray E. NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability // Nucleic Acids Res. — OUP, University of Oxford, 2015. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKV859 — PMID:26323318
  13. ↑ 13,0 13,1 Collins F. A single ataxia telangiectasia gene with a product similar to PI-3 kinase // Science / H. Thorp — AAAS, 1995. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.7792600 — PMID:7792600
  14. ↑ 14,0 14,1 14,2 14,3 Zhu X., Lange T. d., Sfeir A. et al. ATM and ATR Signaling Regulate the Recruitment of Human Telomerase to Telomeres // Cell Reports — Cell Press, Elsevier BV, 2015. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2015.10.041 — PMID:26586433
  15. ↑ 15,0 15,1 Huggins D., Jeyasekharan A. D. PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2014. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1317585111 — PMID:24550317
  16. ↑ 16,0 16,1 Greider C. W. ATM Kinase Is Required for Telomere Elongation in Mouse and Human Cells // Cell Reports — Cell Press, Elsevier BV, 2015. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2015.10.035 — PMID:26586427
  17. ↑ Nakamura M., Zhou X. Z., Kishi S. et al. Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle // FEBS Letters — Elsevier BV, 2002. — ISSN 0014-5793; 1873-3468 — doi:10.1016/S0014-5793(02)02363-3 — PMID:11943150
  18. ↑ 18,0 18,1 18,2 18,3 Zhu X., Wu Y. MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control // Nat. Struct. Mol. Biol. — USA: NPG, 2007. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB1286 — PMID:17694070
  19. ↑ 19,0 19,1 Ronai Z., Takahashi S. ATM-dependent phosphorylation of ATF2 is required for the DNA damage response // Mol. Cell — Cell Press, Elsevier BV, 2005. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2005.04.015 — PMID:15916964
  20. ↑ 20,0 20,1 20,2 20,3 K Tamai, Siliciano J. D. Activation of the ATM kinase by ionizing radiation and phosphorylation of p53 // Science / H. Thorp — AAAS, 1998. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.281.5383.1677 — PMID:9733515
  21. ↑ Takagi M., Absalon M. J., McLure K. G. et al. Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin // Cell — Cell Press, Elsevier BV, 2005. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2005.07.034 — PMID:16213212
  22. ↑ Tibbetts R. S., Brumbaugh K. M., Williams J. M. et al. A role for ATR in the DNA damage-induced phosphorylation of p53 // Genes Dev. — Cold Spring Harbor Laboratory Press, 1999. — ISSN 0890-9369; 1549-5477 — doi:10.1101/GAD.13.2.152 — PMID:9925639
  23. ↑ 23,0 23,1 23,2 Armitage J. O., Vose J. M., Bierman P. J. et al. ATM, CTLA4, MNDA, and HEM1 in high versus low CD38 expressing B-cell chronic lymphocytic leukemia // Clin. Cancer Res. / K. Flaherty — American Association for Cancer Research, 2007. — ISSN 1078-0432; 1557-3265 — doi:10.1158/1078-0432.CCR-07-0283 — PMID:17875758
  24. ↑ Marzluff W. F. Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1 // Nat. Struct. Mol. Biol. — USA: NPG, 2005. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB972 — PMID:16086026
  25. ↑ 25,0 25,1 25,2 25,3 25,4 Tripathi D. N., Chowdhury R., Trudel L. J. et al. Reactive nitrogen species regulate autophagy through ATM-AMPK-TSC2-mediated suppression of mTORC1 // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2013. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1307736110 — PMID:23878245
  26. ↑ 26,0 26,1 Tripathi D. N., Chowdhury R., Trudel L. J. et al. Reactive nitrogen species regulate autophagy through ATM-AMPK-TSC2-mediated suppression of mTORC1 // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2013. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1307736110 — PMID:23878245
  27. ↑ 27,0 27,1 Carranza D., Martinez-Gonzalez L. J., Molina I. J. Molecular and Functional Characterization of a Cohort of Spanish Patients with Ataxia-Telangiectasia // Neuromol. Med. — Springer Science+Business Media, 2016. — ISSN 1535-1084; 1559-1174 — doi:10.1007/S12017-016-8440-8 — PMID:27664052
  28. ↑ Armitage J. O., Vose J. M., Bierman P. J. et al. ATM, CTLA4, MNDA, and HEM1 in high versus low CD38 expressing B-cell chronic lymphocytic leukemia // Clin. Cancer Res. / K. Flaherty — American Association for Cancer Research, 2007. — ISSN 1078-0432; 1557-3265 — doi:10.1158/1078-0432.CCR-07-0283 — PMID:17875758
  29. ↑ Huggins D., Jeyasekharan A. D. PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2014. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1317585111 — PMID:24550317
  30. ↑ Lee J., Paull T. T. ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex // Science / H. Thorp — AAAS, 2005. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.1108297 — PMID:15790808
  31. ↑ 31,0 31,1 31,2 31,3 31,4 31,5 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
  32. ↑ 32,0 32,1 Chen S., Zhang J., Chen J. et al. The over expression of long non-coding RNA ANRIL promotes epithelial-mesenchymal transition by activating the ATM-E2F1 signaling pathway in pancreatic cancer: An in vivo and in vitro study. // Int. J. Biol. Macromolec. — Elsevier BV, 2017. — ISSN 0141-8130; 1879-0003 — doi:10.1016/J.IJBIOMAC.2017.03.123 — PMID:28344092
  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 | вики-текстны 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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