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Эчтәлеккә күчү

PAK1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/PAK1 latin yazuında])
PAK1
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген PAK1[d][1]
Молекуляр функция АТФ-связанные[d][2][2], collagen binding[d][3], связывание с белками плазмы[d][4][5][6][…], kinase activity[d][2], активность катализатора[d][2], нуклеотид-связывающий[d][2], трансферазная активность[d][2], protein serine/threonine kinase activity[d][7][7][7][…], protein kinase activity[d][2][2][8][…], связывание похожих белков[d][9][10], protein kinase binding[d][2] һәм protein serine/threonine kinase activity[d][2][2][2][…]
Күзәнәк компоненты cell projection[d][2], ruffle membrane[d][2], мембрана[d][2][2], filamentous actin[d][11], cell-cell junction[d][12], межклеточные контакты[d][2], фокальные контакты[d][2], цитоплазма[7][13][14], intercalated disc[d][2][2], дендрит[d][2][2], күзәнәк мембранасы[d][2][2][2][…], Z discdkac[d][2][2], аксон[d][2][2], ядерная мембрана[d][2][2], ruffle[d][2][12], цитозоль[d][2][2][2], lamellipodium[d][2], protein-containing complex[d][15][4], цитоплазма[2][16][5][…], микрофиламент[d][17], нуклеоплазма[d][18], төш[2], нуклеоплазма[d][2][16] һәм Хромосома[2]
Биологик процесс positive regulation of protein phosphorylation[d][19], cellular response to insulin stimulus[d][2], negative regulation of cell proliferation involved in contact inhibition[d][12], response to hypoxia[d][2], Экзоцитоз[d][2], positive regulation of JUN kinase activity[d][8], MAPK cascade[d][8], regulation of actin cytoskeleton organization[d][2], positive regulation of intracellular estrogen receptor signaling pathway[d][20], branching morphogenesis of an epithelial tube[d][21], ephrin receptor signaling pathway[d][2], positive regulation of stress fiber assembly[d][4], T cell costimulation[d][2], Заживление ран[d][12], positive regulation of cell migration[d][5], апоптоз[d][2], Fc-gamma receptor signaling pathway involved in phagocytosis[d][2], Fc-epsilon receptor signaling pathway[d][2], фосфорилирование[d][2], Метаболизм[2], stimulatory C-type lectin receptor signaling pathway[d][2], response to organic substance[d][2], T cell receptor signaling pathway[d][2], neuron projection morphogenesis[d][2][2], позитивная регуляция пролиферации клеток[d][22], protein autophosphorylation[d][2][8], actin cytoskeleton reorganization[d][20][17], фосфорилация белка[d][2][2][16][…], Rho protein signal transduction[d][7], regulation of mitotic cell cycle[d][7], positive regulation of fibroblast migration[d][2], cerebellum development[d][2], establishment of cell polarity[d][2], positive regulation of microtubule polymerization[d][23], activation of protein kinase activity[d][24], positive regulation of peptidyl-serine phosphorylation[d][2][25], regulation of apoptotic process[d][7], positive regulation of axon extension[d][2], hepatocyte growth factor receptor signaling pathway[d][23], regulation of axonogenesis[d][24], negative regulation of cell growth involved in cardiac muscle cell development[d][2], positive regulation of protein targeting to membrane[d][2], positive regulation of vascular associated smooth muscle cell proliferation[d][2], positive regulation of vascular associated smooth muscle cell migration[d][2], передача сигнала[d][24], stress-activated protein kinase signaling cascade[d][24], regulation of MAPK cascade[d][24], positive regulation of insulin receptor signaling pathway[d][2], cellular response to DNA damage stimulus[d][16], миграция клеток[d][24] һәм ремоделирование хроматина[d][16]
Изображение Gene Atlas

PAK1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[26][27]

  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 GOA
  3. Knaus U. G. A p21-activated kinase-controlled metabolic switch up-regulates phagocyte NADPH oxidase // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M206650200PMID:12189148
  4. 4,0 4,1 4,2 Koh C., Tan E., Manser E. et al. The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family // Curr. Biol.United Kingdom: Cell Press, Elsevier BV, 2002. — ISSN 0960-9822; 1879-0445doi:10.1016/S0960-9822(02)00652-8PMID:11864573
  5. 5,0 5,1 5,2 G Wang, Q Zhang, Y Song et al. PAK1 regulates RUFY3-mediated gastric cancer cell migration and invasion // Cell Death Dis.London: Nature Publishing Group, 2015. — ISSN 2041-4889doi:10.1038/CDDIS.2015.50PMID:25766321
  6. Ijuin T. Glucose-regulated protein 78 (GRP78) binds directly to PIP3 phosphatase SKIP and determines its localization // Genes Cells / M. YanagidaWiley-Blackwell, 2016. — ISSN 1356-9597; 1365-2443doi:10.1111/GTC.12353PMID:26940976
  7. 7,0 7,1 7,2 7,3 7,4 7,5 7,6 GOA
  8. 8,0 8,1 8,2 8,3 Brown J. L., L Stowers, M Baer et al. Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway // Curr. Biol.United Kingdom: Cell Press, Elsevier BV, 1996. — ISSN 0960-9822; 1879-0445doi:10.1016/S0960-9822(02)00546-8PMID:8805275
  9. Wang J., Wu J., Wang Z. Structural insights into the autoactivation mechanism of p21-activated protein kinase // Structure / C. D. LimaCell Press, Elsevier BV, 2011. — ISSN 0969-2126; 1878-4186doi:10.1016/J.STR.2011.10.013PMID:22153498
  10. Rayala S. K., Bert W O'Malley Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1 // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2007. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.0701065104PMID:17389360
  11. Knaus U. G. Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells // Curr. Biol.United Kingdom: Cell Press, Elsevier BV, 1997. — ISSN 0960-9822; 1879-0445doi:10.1016/S0960-9822(97)70091-5PMID:9395435
  12. 12,0 12,1 12,2 12,3 Zegers M. M., Chernoff J. Pak1 and PIX regulate contact inhibition during epithelial wound healing // EMBO J.NPG, 2003. — ISSN 0261-4189; 1460-2075doi:10.1093/EMBOJ/CDG398PMID:12912914
  13. G Wang, Q Zhang, Y Song et al. PAK1 regulates RUFY3-mediated gastric cancer cell migration and invasion // Cell Death Dis.London: Nature Publishing Group, 2015. — ISSN 2041-4889doi:10.1038/CDDIS.2015.50PMID:25766321
  14. Talukder A. H., Q Meng, R Kumar CRIPak, a novel endogenous Pak1 inhibitor // OncogeneNPG, 2006. — ISSN 0950-9232; 1476-5594doi:10.1038/SJ.ONC.1209172PMID:16278681
  15. Curtis I. D. Analysis of the subcellular distribution of avian p95-APP2, an ARF-GAP orthologous to mammalian paxillin kinase linker // Int. J. Biochem. Cell Biol.Elsevier BV, 2002. — ISSN 1357-2725; 0020-711X; 1878-5875doi:10.1016/S1357-2725(02)00008-0PMID:11950598
  16. 16,0 16,1 16,2 16,3 16,4 L Aravind MORC2 signaling integrates phosphorylation-dependent, ATPase-coupled chromatin remodeling during the DNA damage response // Cell ReportsCell Press, Elsevier BV, 2012. — ISSN 2211-1247; 2639-1856doi:10.1016/J.CELREP.2012.11.018PMID:23260667
  17. 17,0 17,1 Knaus U. G. Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells // Curr. Biol.United Kingdom: Cell Press, Elsevier BV, 1997. — ISSN 0960-9822; 1879-0445doi:10.1016/S0960-9822(97)70091-5PMID:9395435
  18. L Aravind MORC2 signaling integrates phosphorylation-dependent, ATPase-coupled chromatin remodeling during the DNA damage response // Cell ReportsCell Press, Elsevier BV, 2012. — ISSN 2211-1247; 2639-1856doi:10.1016/J.CELREP.2012.11.018PMID:23260667
  19. Mantovani A., Arenzana-Seisdedos F., Cancellieri C. et al. β-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6 // Sci. Signal.AAAS, 2013. — ISSN 1945-0877; 1937-9145doi:10.1126/SCISIGNAL.2003627PMID:23633677
  20. 20,0 20,1 Talukder A. H., Q Meng, R Kumar CRIPak, a novel endogenous Pak1 inhibitor // OncogeneNPG, 2006. — ISSN 0950-9232; 1476-5594doi:10.1038/SJ.ONC.1209172PMID:16278681
  21. Zegers M. M. Pak1 regulates branching morphogenesis in 3D MDCK cell culture by a PIX and beta1-integrin-dependent mechanism // American Journal of Physiology: Cell Physiology — 2010. — ISSN 0363-6143; 1522-1563doi:10.1152/AJPCELL.00543.2009PMID:20457839
  22. Zhang X., Mao H., Chen J. et al. Increased expression of microRNA-221 inhibits PAK1 in endothelial progenitor cells and impairs its function via c-Raf/MEK/ERK pathway // Biochem. Biophys. Res. Commun.Academic Press, Elsevier BV, 2013. — ISSN 0006-291X; 1090-2104doi:10.1016/J.BBRC.2012.12.157PMID:23333386
  23. 23,0 23,1 Tian X., Tian Y., Moldobaeva N. et al. Microtubule dynamics control HGF-induced lung endothelial barrier enhancement // PLOS ONE / PLOS ONE EditorsPLoS, 2014. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0105912PMID:25198505
  24. 24,0 24,1 24,2 24,3 24,4 24,5 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; 1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  25. Sickmann A., Benz R., Polzien L. et al. Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M109.010702PMID:19667065
  26. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  27. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
  • 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.)