TSC1 |
Нинди таксонда бар |
H. sapiens[d][1] |
Кодлаучы ген |
TSC1[d][1] |
Молекуляр функция |
chaperone binding[d][2], связывание с белками плазмы[d][3][4][5][…], protein N-terminus binding[d][6][7][8], Hsp70 protein binding[d][9], ATPase inhibitor activity[d][8][9], Hsp90 protein binding[d][9] һәм GTPase activating protein binding[d][8] |
Күзәнәк компоненты |
цитоплазма[8][8][4], cell cortex[d][6], Конус роста[d][8], intracellular membrane-bounded organelle[d][8], lamellipodium[d][6], мембрана[d][8][10], микрофиламент[d][6], TSC1-TSC2 complex[d][11], цитоскелет[d][8], цитозоль[d][8][8][2][…], төш[8][8], perinuclear region of cytoplasm[d][8][8], lipid droplet[d][8], күзәнәк мембранасы[d][8], cell projection[d][8], protein-containing complex[d][8][2], chaperone complex[d][9], постсинаптическое уплотнение[d][8] һәм TSC1-TSC2 complex[d][4][12] |
Биологик процесс |
rRNA export from nucleus[d][13], regulation of cell cycle[d][12], neural tube closure[d][8], cerebral cortex development[d][8], memory T cell differentiation[d][8], regulation of protein kinase activity[d][8], positive regulation of focal adhesion assembly[d][6], myelination[d][8], negative regulation of insulin receptor signaling pathway[d][12], synapse organization[d][8], regulation of translation[d][13], развитие гиппокампа[d][8], regulation of phosphoprotein phosphatase activity[d][13], cell-matrix adhesion[d][6], potassium ion transport[d][8], adaptive immune response[d][8], protein heterooligomerization[d][8], нефрогенез[d][8], нерв системасы үсеше[d][8], cell projection organization[d][8], activation of GTPase activity[d][6], regulation of focal adhesion assembly[d][8], glucose import[d][8], regulation of cell-matrix adhesion[d][6], negative regulation of cell size[d][8], response to insulin[d][14], cardiac muscle cell differentiation[d][8], negative regulation of translation[d][13], негативная регуляция пролиферации клеток[d][15][8], cellular response to oxygen-glucose deprivation[d][8][8], adult locomotory behavior[d][8][8], negative regulation of TOR signaling[d][16][17][18][…], regulation of neuron death[d][8][8], negative regulation of macroautophagy[d][8][8], negative regulation of neuron projection development[d][8], positive regulation of macroautophagy[d][8], negative regulation of GTPase activity[d][8], regulation of stress fiber assembly[d][6], positive regulation of stress fiber assembly[d][8], negative regulation of oxidative stress-induced neuron death[d][8], negative regulation of ATP-dependent activity[d][8][9], protein stabilization[d][9][8][19] һәм negative regulation of TOR signaling[d][8][13][20][…] |
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TSC1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[21][22]
- ↑ 1,0 1,1 UniProt
- ↑ 2,0 2,1 2,2 M Nellist, M A van Slegtenhorst, M Goedbloed et al. Characterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartin // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1999. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.274.50.35647 — PMID:10585443
- ↑ He Y. J., Duronio R. J. WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase // Genes Dev. — Cold Spring Harbor Laboratory Press, 2008. — ISSN 0890-9369; 1549-5477 — doi:10.1101/GAD.1624008 — PMID:18381890
- ↑ 4,0 4,1 4,2 Snell R. G. Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products // Human Molecular Genetics — OUP, 1998. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/7.6.1053 — PMID:9580671
- ↑ Nakashima A., Yoshino K., Miyamoto T. et al. Identification of TBC7 having TBC domain as a novel binding protein to TSC1-TSC2 complex // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 2007. — ISSN 0006-291X; 1090-2104 — doi:10.1016/J.BBRC.2007.07.011 — PMID:17658474
- ↑ 6,0 6,1 6,2 6,3 6,4 6,5 6,6 6,7 6,8 Lamb R. F., C Roy, Diefenbach T. J. et al. The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho // Nat. Cell Biol. — NPG, 2000. — ISSN 1465-7392; 1476-4679 — doi:10.1038/35010550 — PMID:10806479
- ↑ Haddad L. A., Smith N., Bowser M. et al. The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton // 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.M207211200 — PMID:12226091
- ↑ 8,00 8,01 8,02 8,03 8,04 8,05 8,06 8,07 8,08 8,09 8,10 8,11 8,12 8,13 8,14 8,15 8,16 8,17 8,18 8,19 8,20 8,21 8,22 8,23 8,24 8,25 8,26 8,27 8,28 8,29 8,30 8,31 8,32 8,33 8,34 8,35 8,36 8,37 8,38 8,39 8,40 8,41 8,42 8,43 8,44 8,45 8,46 8,47 8,48 8,49 8,50 8,51 8,52 8,53 GOA
- ↑ 9,0 9,1 9,2 9,3 9,4 9,5 Woodford M. R., Dunn D. M., Prodromou C. et al. Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients // EMBO J. — NPG, 2017. — ISSN 0261-4189; 1460-2075 — doi:10.15252/EMBJ.201796700 — PMID:29127155
- ↑ Tee A. R. Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2006. — 11 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200507119 — PMID:16636147
- ↑ Snell R. G. Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products // Human Molecular Genetics — OUP, 1998. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/7.6.1053 — PMID:9580671
- ↑ 12,0 12,1 12,2 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
- ↑ 13,0 13,1 13,2 13,3 13,4 Maggi L. B., Gutmann D. H. TSC1 sets the rate of ribosome export and protein synthesis through nucleophosmin translation // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2007. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-06-2875 — PMID:17308101
- ↑ Wan M., Wu X., Guan K. et al. Muscle atrophy in transgenic mice expressing a human TSC1 transgene // FEBS Letters — Elsevier BV, 2006. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2006.09.008 — PMID:16996505
- ↑ A Miloloza, M Rosner, M Nellist et al. The TSC1 gene product, hamartin, negatively regulates cell proliferation // Human Molecular Genetics — OUP, 2000. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/9.12.1721 — PMID:10915759
- ↑ GOA
- ↑ Park S. M., Kim S., Kim H. H. et al. Somatic Mutations in TSC1 and TSC2 Cause Focal Cortical Dysplasia // Am. J. Hum. Genet. — Cell Press, Elsevier BV, 2017. — ISSN 0002-9297; 1537-6605 — doi:10.1016/J.AJHG.2017.01.030 — PMID:28215400
- ↑ Maggi L. B., Gutmann D. H. TSC1 sets the rate of ribosome export and protein synthesis through nucleophosmin translation // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2007. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-06-2875 — PMID:17308101
- ↑ G Benvenuto The tuberous sclerosis-1 (TSC1) gene product hamartin suppresses cell growth and augments the expression of the TSC2 product tuberin by inhibiting its ubiquitination // Oncogene — NPG, 2000. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1204009 — PMID:11175345
- ↑ Park S. M., Kim S., Kim H. H. et al. Somatic Mutations in TSC1 and TSC2 Cause Focal Cortical Dysplasia // Am. J. Hum. Genet. — Cell Press, Elsevier BV, 2017. — ISSN 0002-9297; 1537-6605 — doi:10.1016/J.AJHG.2017.01.030 — PMID:28215400
- ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
- ↑ 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.)