Wikipedia

PAK1

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

PAK1
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген PAK1[d][1]
Молекулярная 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 мембраны[d][2][2][2][…], Z disc[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][…], Микрофиламенты[d][17], нуклеоплазма[d][18], Төш[2], нуклеоплазма[d][2][16] һәм Хромосома[2]
Биологический 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

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 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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M206650200 — PMID: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. — UK: Cell Press, Elsevier BV, 2002. — ISSN 0960-9822; 1879-0445 — doi:10.1016/S0960-9822(02)00652-8 — PMID: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 2041-4889 — doi:10.1038/CDDIS.2015.50 — PMID:25766321
  6. ↑ Ijuin T. Glucose-regulated protein 78 (GRP78) binds directly to PIP3 phosphatase SKIP and determines its localization // Genes Cells / M. Yanagida — Wiley-Blackwell, 2016. — ISSN 1356-9597; 1365-2443 — doi:10.1111/GTC.12353 — PMID: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. — UK: Cell Press, Elsevier BV, 1996. — ISSN 0960-9822; 1879-0445 — doi:10.1016/S0960-9822(02)00546-8 — PMID:8805275
  9. ↑ Wang J., Wu J., Wang Z. Structural insights into the autoactivation mechanism of p21-activated protein kinase // Structure / C. D. Lima — Cell Press, Elsevier BV, 2011. — ISSN 0969-2126; 1878-4186 — doi:10.1016/J.STR.2011.10.013 — PMID: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; 1091-6490 — doi:10.1073/PNAS.0701065104 — PMID:17389360
  11. ↑ Knaus U. G. Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells // Curr. Biol. — UK: Cell Press, Elsevier BV, 1997. — ISSN 0960-9822; 1879-0445 — doi:10.1016/S0960-9822(97)70091-5 — PMID: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; 1460-2075 — doi:10.1093/EMBOJ/CDG398 — PMID: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 2041-4889 — doi:10.1038/CDDIS.2015.50 — PMID:25766321
  14. ↑ Talukder A. H., Q Meng, R Kumar CRIPak, a novel endogenous Pak1 inhibitor // Oncogene — NPG, 2006. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1209172 — PMID: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; 1878-5875 — doi:10.1016/S1357-2725(02)00008-0 — PMID: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 Reports — Cell Press, Elsevier BV, 2012. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2012.11.018 — PMID:23260667
  17. ↑ 17,0 17,1 Knaus U. G. Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells // Curr. Biol. — UK: Cell Press, Elsevier BV, 1997. — ISSN 0960-9822; 1879-0445 — doi:10.1016/S0960-9822(97)70091-5 — PMID:9395435
  18. ↑ L Aravind MORC2 signaling integrates phosphorylation-dependent, ATPase-coupled chromatin remodeling during the DNA damage response // Cell Reports — Cell Press, Elsevier BV, 2012. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2012.11.018 — PMID: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; 1937-9145 — doi:10.1126/SCISIGNAL.2003627 — PMID:23633677
  20. ↑ 20,0 20,1 Talukder A. H., Q Meng, R Kumar CRIPak, a novel endogenous Pak1 inhibitor // Oncogene — NPG, 2006. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1209172 — PMID: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; 1522-1563 — doi:10.1152/AJPCELL.00543.2009 — PMID: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; 1090-2104 — doi:10.1016/J.BBRC.2012.12.157 — PMID: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 Editors — PLoS, 2014. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0105912 — PMID: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; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID: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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.010702 — PMID: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.

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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