SMURF2 |
Нинди таксонда бар |
H. sapiens[d][1] |
Кодлаучы ген |
SMURF2[d][1] |
Молекуляр функция |
связывание с белками плазмы[d][2][3][4][…], связывание похожих белков[d][5][6], ubiquitin-protein transferase activity[d][7][7][8][…], трансферазная активность[d][9], ubiquitin protein ligase activity[d][9][9][10], transforming growth factor beta receptor binding[d][9], SMAD binding[d][11][9] һәм ubiquitin-protein transferase activity[d][9][9][12] |
Күзәнәк компоненты |
цитозоль[d][9], мембрана[d][9], ubiquitin ligase complex[d][12], күзәнәк мембранасы[d][9], нуклеоплазма[d][9], липидный рафт[d][9], ядерные спеклы[d][9], төш[13][9] һәм цитоплазма[9][10] |
Биологик процесс |
positive regulation of canonical Wnt signaling pathway[d][9], negative regulation of transcription by RNA polymerase II[d][9], negative regulation of transforming growth factor beta receptor signaling pathway[d][9][14], BMP signaling pathway[d][9], positive regulation of trophoblast cell migration[d][14], ubiquitin-dependent SMAD protein catabolic process[d][15], regulation of transforming growth factor beta receptor signaling pathway[d][16], protein ubiquitination[d][7], negative regulation of transcription, DNA-templated[d][17], protein polyubiquitination[d][7], Wnt signaling pathway, planar cell polarity pathway[d][9], protein deubiquitination[d][9], ubiquitin-dependent protein catabolic process[d][7][8], negative regulation of BMP signaling pathway[d][10], protein polyubiquitination[d][9][10], ubiquitin-dependent protein catabolic process[d][9][12][10], protein ubiquitination[d][9][10], ubiquitin-dependent SMAD protein catabolic process[d][11][10], proteasome-mediated ubiquitin-dependent protein catabolic process[d][10] һәм positive regulation of protein catabolic process[d][10] |
SMURF2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[18][19]
- ↑ 1,0 1,1 UniProt
- ↑ Meng A., Zhang L. SCFFBXL¹⁵ regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1, SCFFBXL15regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1 // EMBO J. — NPG, 2011. — ISSN 0261-4189; 1460-2075 — doi:10.1038/EMBOJ.2011.155 — PMID:21572392
- ↑ Pietenpol J. A., Moses H. L. Identification of novel Smad2 and Smad3 associated proteins in response to TGF-beta1 // J. Cell. Biochem. — Wiley, 2008. — ISSN 0730-2312; 1097-4644; 0733-1959 — doi:10.1002/JCB.21860 — PMID:18729074
- ↑ Tafforeau L., Mangeot P., Jacob Y. et al. Hepatitis C virus infection protein network // Mol. Syst. Biol. / R. Aebersold — EMBO, Wiley, 2008. — ISSN 1744-4292 — doi:10.1038/MSB.2008.66 — PMID:18985028
- ↑ Sicheri F., Rotin D., Wiesner S. et al. Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain // Cell — Cell Press, Elsevier BV, 2007. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2007.06.050 — PMID:17719543
- ↑ Wojcik J., Meil A. Functional proteomics mapping of a human signaling pathway // Genome Res. — Cold Spring Harbor Laboratory Press, 2004. — ISSN 1549-5469; 1088-9051; 1054-9803 — doi:10.1101/GR.2334104 — PMID:15231748
- ↑ 7,0 7,1 7,2 7,3 7,4 GOA
- ↑ 8,0 8,1 Li H., Seth A. An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein // Oncogene — NPG, 2004. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1207319 — PMID:14755250
- ↑ 9,00 9,01 9,02 9,03 9,04 9,05 9,06 9,07 9,08 9,09 9,10 9,11 9,12 9,13 9,14 9,15 9,16 9,17 9,18 9,19 9,20 9,21 9,22 9,23 GOA
- ↑ 10,0 10,1 10,2 10,3 10,4 10,5 10,6 10,7 10,8 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
- ↑ 11,0 11,1 Miyazawa K., Uchida T., Matsumoto T. Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — 7 p. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M804659200 — PMID:19122240
- ↑ 12,0 12,1 12,2 Li H., Seth A. An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein // Oncogene — NPG, 2004. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1207319 — PMID:14755250
- ↑ P Kavsak, Rasmussen R. K., Causing C. G. et al. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation // Mol. Cell — Cell Press, Elsevier BV, 2000. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(00)00134-9 — PMID:11163210
- ↑ 14,0 14,1 Yang Q., Chen S., Zhang X. et al. Smurf2 participates in human trophoblast cell invasion by inhibiting TGF-beta type I receptor // J. Histochem. Cytochem. — SAGE Publishing, 2009. — ISSN 0022-1554; 1551-5044 — doi:10.1369/JHC.2009.953166 — PMID:19255252
- ↑ Miyazawa K., Uchida T., Matsumoto T. Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — 7 p. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M804659200 — PMID:19122240
- ↑ A Hemmati-Brivanlou Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2001. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.98.3.974 — PMID:11158580
- ↑ X Lin, M Liang, Feng X. H. Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.C000580200 — PMID:11016919
- ↑ 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.)