ATF4

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/ATF4 latin yazuında])
ATF4
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген ATF4[d][1]
Молекулярная функция ДНК-связывающий[d][2], sequence-specific DNA binding[d][2], DNA-binding transcription factor activity[d][2][2], DNA-binding transcription activator activity, RNA polymerase II-specific[d][2][3][4], transcription factor binding[d][2][4], RNA polymerase II cis-regulatory region sequence-specific DNA binding[d][2][4], core promoter sequence-specific DNA binding[d][2], protein C-terminus binding[d][2][4], связывание с белками плазмы[d][5][6][7][…], leucine zipper domain binding[d][8], protein heterodimerization activity[d][9], DNA-binding transcription factor activity[d][10][4][4][…], ДНК-связывающий[d][4][4][4][…], core promoter sequence-specific DNA binding[d][3][3], sequence-specific DNA binding[d][11], protein kinase binding[d][12], DNA-binding transcription factor activity, RNA polymerase II-specific[d][13][13][3][…], RNA polymerase II cis-regulatory region sequence-specific DNA binding[d][4][4], RNA polymerase II transcription regulatory region sequence-specific DNA binding[d][14] һәм DNA-binding transcription factor activity, RNA polymerase II-specific[d][15][15][4][…]
Күзәнәк компоненты цитоплазма[2][2], ATF1-ATF4 transcription factor complex[d][2], ATF4-CREB1 transcription factor complex[d][2], transcription regulator complex[d][2][4], dendrite membrane[d][2][4], төш[2][2], Lewy body core[d][16], nuclear periphery[d][16], мембрана[d][4], күзәнәк мембраны[d][4], нуклеоплазма[d][4], центр организации микротрубочек[d][4], neuron projection[d][16], цитоскелет[d][4], CHOP-ATF4 complex[d][9][7][8], ATF4-CREB1 transcription factor complex[d][4][17], цитоплазма[4][4][4][…], төш[3][3][3][…], ATF1-ATF4 transcription factor complex[d][4][17], центросома[d][12], protein-containing complex[d][12], төш[4][4][4][…] һәм RNA polymerase II transcription regulator complex[d][4]
Биологический процесс gamma-aminobutyric acid signaling pathway[d][2][4], глюконеогенез[d][2], ДНК-зависимая регуляция транскрипции[d][2][2], positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress[d][2], regulation of transcription by RNA polymerase II[d][2][2][3][…], negative regulation of oxidative stress-induced neuron death[d][2], cellular response to amino acid starvation[d][2], mRNA transcription by RNA polymerase II[d][2], circadian regulation of gene expression[d][2], response to endoplasmic reticulum stress[d][2], PERK-mediated unfolded protein response[d][2], response to manganese-induced endoplasmic reticulum stress[d][2][4], ДНК-зависимая позитивная регуляция транскрипции[d][2], positive regulation of neuron apoptotic process[d][2], intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress[d][2], positive regulation of gene expression[d][2], positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress[d][2], циркадный ритм[d][2][4], negative regulation of potassium ion transport[d][2][4], положительная регуляция транскрипции РНК полимеразой II промотор[d][2], positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance[d][18], cellular response to glucose starvation[d][11], negative regulation of translational initiation in response to stress[d][4], ритмический процесс[d][4], cellular response to UV[d][4], positive regulation of transcription from RNA polymerase II promoter in response to stress[d][19], cellular amino acid metabolic process[d][10], transcription by RNA polymerase II[d][4], транскрипция, ДНК-зависимая[d][3], positive regulation of gene expression[d][20][21][4], positive regulation of apoptotic process[d][16], positive regulation of vascular endothelial growth factor production[d][11], positive regulation of transcription by RNA polymerase I[d][11], положительная регуляция транскрипции РНК полимеразой II промотор[d][4][22][4][…], positive regulation of neuron apoptotic process[d][4][4], positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress[d][23][24][3], intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress[d][4][4], positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress[d][24][3][25], глюконеогенез[d][4][4], PERK-mediated unfolded protein response[d][4][26][27][…], ДНК-зависимая регуляция транскрипции[d][4][4][4], negative regulation of oxidative stress-induced neuron death[d][16][4], cellular response to amino acid starvation[d][4][4], circadian regulation of gene expression[d][4][4], ДНК-зависимая позитивная регуляция транскрипции[d][28][4][29][…], mRNA transcription by RNA polymerase II[d][4][4], response to endoplasmic reticulum stress[d][20][4][30], cellular response to dopamine[d][21], response to toxic substance[d][4], neuron differentiation[d][4], cellular response to oxygen-glucose deprivation[d][4], positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway[d][3], regulation of transcription by RNA polymerase II[d][4][4][14], cellular calcium ion homeostasis[d][4], positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress[d][16][31][4][…], positive regulation of biomineral tissue development[d][4], negative regulation of cold-induced thermogenesis[d][32][4], positive regulation of vascular associated smooth muscle cell apoptotic process[d][4], positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress[d][31][4][17][…] һәм positive regulation of sodium-dependent phosphate transport[d][4]

ATF4 (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 GOA
  3. ↑ 3,00 3,01 3,02 3,03 3,04 3,05 3,06 3,07 3,08 3,09 3,10 3,11 GOA
  4. ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 4,12 4,13 4,14 4,15 4,16 4,17 4,18 4,19 4,20 4,21 4,22 4,23 4,24 4,25 4,26 4,27 4,28 4,29 4,30 4,31 4,32 4,33 4,34 4,35 4,36 4,37 4,38 4,39 4,40 4,41 4,42 4,43 4,44 4,45 4,46 4,47 4,48 4,49 4,50 4,51 4,52 4,53 4,54 4,55 4,56 4,57 4,58 4,59 4,60 4,61 4,62 4,63 4,64 4,65 4,66 4,67 4,68 4,69 GOA
  5. ↑ Dricot A., Barabási A., Tavernier J. et al. A proteome-scale map of the human interactome network // Cell — Cell Press, Elsevier BV, 2014. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2014.10.050 — PMID:25416956
  6. ↑ Bosak S., Hirozane-Kishikawa T., Dricot A. et al. Towards a proteome-scale map of the human protein–protein interaction network, Towards a proteome-scale map of the human protein-protein interaction network // Nature / M. Skipper — NPG, Springer Science+Business Media, 2005. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE04209 — PMID:16189514
  7. ↑ 7,0 7,1 Su N., Kilberg M. S. C/EBP homology protein (CHOP) interacts with activating transcription factor 4 (ATF4) and negatively regulates the stress-dependent induction of the asparagine synthetase gene // 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.M806874200 — PMID:18940792
  8. ↑ 8,0 8,1 F Gachon, G Gaudray, S Thébault et al. The cAMP response element binding protein-2 (CREB-2) can interact with the C/EBP-homologous protein (CHOP) // FEBS Letters — Elsevier BV, 2001. — ISSN 0014-5793; 1873-3468 — doi:10.1016/S0014-5793(01)02646-1 — PMID:11478948
  9. ↑ 9,0 9,1 Hattori T., Ohoka N. TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death // EMBO J. — NPG, 2005. — ISSN 0261-4189; 1460-2075 — doi:10.1038/SJ.EMBOJ.7600596 — PMID:15775988
  10. ↑ 10,0 10,1 Rutkowski T. All roads lead to ATF4 // Developmental Cell — Elsevier BV, 2003. — 3 p. — ISSN 1534-5807; 1878-1551 — doi:10.1016/S1534-5807(03)00100-X — PMID:12689582
  11. ↑ 11,0 11,1 11,2 11,3 Wang Y., Alam G. N., Ning Y. et al. The unfolded protein response induces the angiogenic switch in human tumor cells through the PERK/ATF4 pathway // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2012. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-12-0474 — PMID:22915762
  12. ↑ 12,0 12,1 12,2 Meirelles G. V., Silva J. C. d., Adriana Franco Paes Leme et al. Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome // J. Proteome Res. / J. Yates — ACS, 2010. — ISSN 1535-3893; 1535-3907 — doi:10.1021/PR100562W — PMID:20873783
  13. ↑ 13,0 13,1 Vaquerizas J. M., Teichmann S., Kummerfeld S. K. A census of human transcription factors: function, expression and evolution // Nature reviews. Genetics — UK: NPG, 2009. — ISSN 1471-0056; 1471-0064 — doi:10.1038/NRG2538 — PMID:19274049
  14. ↑ 14,0 14,1 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
  15. ↑ 15,0 15,1 Vaquerizas J. M., Teichmann S., Kummerfeld S. K. A census of human transcription factors: function, expression and evolution // Nature reviews. Genetics — UK: NPG, 2009. — ISSN 1471-0056; 1471-0064 — doi:10.1038/NRG2538 — PMID:19274049
  16. ↑ 16,0 16,1 16,2 16,3 16,4 16,5 Sulzer D. ATF4 protects against neuronal death in cellular Parkinson's disease models by maintaining levels of parkin // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2013. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.2292-12.2013 — PMID:23392669
  17. ↑ 17,0 17,1 17,2 Abcouwer S. F., Lee A. S. Induction of Grp78/BiP by translational block: activation of the Grp78 promoter by ATF4 through and upstream ATF/CRE site independent of the endoplasmic reticulum stress elements // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M303619200 — PMID:12871976
  18. ↑ S Oyadomari, M Mori Roles of CHOP/GADD153 in endoplasmic reticulum stress // Cell Death & Differentiation — NPG, 2004. — ISSN 1350-9047; 1476-5403 — doi:10.1038/SJ.CDD.4401373 — PMID:14685163
  19. ↑ Klinkenberg M. Loss of lysosome-associated membrane protein 3 (LAMP3) enhances cellular vulnerability against proteasomal inhibition // Eur. J. Cell Biol. — Elsevier BV, 2015. — ISSN 0171-9335; 0070-2463 — doi:10.1016/J.EJCB.2015.01.003 — PMID:25681212
  20. ↑ 20,0 20,1 Maehara Y. Role of activating transcription factor 3 (ATF3) in endoplasmic reticulum (ER) stress-induced sensitization of p53-deficient human colon cancer cells to tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis through up-regulation of death receptor 5 (DR5) by zerumbone and celecoxib // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2014. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M114.558890 — PMID:24939851
  21. ↑ 21,0 21,1 Minchin R. F., Butcher N. J. Cytosolic sulfotransferase 1A3 is induced by dopamine and protects neuronal cells from dopamine toxicity: role of D1 receptor-N-methyl-D-aspartate receptor coupling // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M113.493239 — PMID:24136195
  22. ↑ Abcouwer S. F. The oxidative stressor arsenite activates vascular endothelial growth factor mRNA transcription by an ATF4-dependent mechanism // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2005. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M411275200 — PMID:15788408
  23. ↑ Sulzer D. ATF4 protects against neuronal death in cellular Parkinson's disease models by maintaining levels of parkin // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2013. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.2292-12.2013 — PMID:23392669
  24. ↑ 24,0 24,1 J Tatzelt, Park D. S., Winklhofer K. F. et al. Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress // Cell Death & Differentiation — NPG, 2011. — ISSN 1350-9047; 1476-5403 — doi:10.1038/CDD.2010.142 — PMID:21113145
  25. ↑ Abcouwer S. F., Lee A. S. Induction of Grp78/BiP by translational block: activation of the Grp78 promoter by ATF4 through and upstream ATF/CRE site independent of the endoplasmic reticulum stress elements // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M303619200 — PMID:12871976
  26. ↑ Brown M. K., Naidoo N. The endoplasmic reticulum stress response in aging and age-related diseases // Frontiers in Physiology — Frontiers Media, 2012. — ISSN 1664-042X — doi:10.3389/FPHYS.2012.00263 — PMID:22934019
  27. ↑ Martinon F., Glimcher L. H. The unfolded protein response: integrating stress signals through the stress sensor IRE1α // Physiological Reviews / D. Brown — USA: American Physiological Society, 2011. — 680 p. — ISSN 0031-9333; 1522-1210 — doi:10.1152/PHYSREV.00001.2011 — PMID:22013210
  28. ↑ F Wong-Staal Functional interaction of the HTLV-1 transactivator Tax with activating transcription factor-4 (ATF4) // Oncogene — NPG, 1997. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1201119 — PMID:9190894
  29. ↑ Siu F., Bain P. J., LeBlanc-Chaffin R. et al. ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M201959200 — PMID:11960987
  30. ↑ Chami M., Oulès B., Rizzuto R. et al. Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress // Mol. Cell — Cell Press, Elsevier BV, 2008. — 11 p. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2008.11.014 — PMID:19061639
  31. ↑ 31,0 31,1 J Tatzelt, Park D. S., Winklhofer K. F. et al. Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress // Cell Death & Differentiation — NPG, 2011. — ISSN 1350-9047; 1476-5403 — doi:10.1038/CDD.2010.142 — PMID:21113145
  32. ↑ Wang C., Xia T., Du Y. et al. Effects of ATF4 on PGC1α expression in brown adipose tissue and metabolic responses to cold stress // Metabolism: clinical and experimental — Elsevier BV, 2012. — ISSN 0026-0495; 1532-8600 — doi:10.1016/J.METABOL.2012.07.017 — PMID:22980225
  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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