TRIM5

TRIM5
Рәсем
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген TRIM5[d][1]
Молекуляр функция protein-macromolecule adaptor activity[d][2], гомодимеризация белка[d][3], pattern recognition receptor activity[d][4], zinc ion binding[d][5], связывание с ионом металла[d][5], связывание с белками плазмы[d][6][7][4][…], связывание похожих белков[d][8][9], protein kinase binding[d][2], трансферазная активность[d][5] һәм ubiquitin-protein transferase activity[d][5][4]
Күзәнәк компоненты цитоплазма[5][10][2], цитозоль[d][5], omegasome[d][2], внутренний компонент клетки[d][11], төш[5] һәм P-body[d][7]
Биологик процесс regulation of lipopolysaccharide-mediated signaling pathway[d][4], interferon-gamma-mediated signaling pathway[d][5], protein K63-linked ubiquitination[d][4], процесс иммунной системы[d][5], protein trimerization[d][12], positive regulation of DNA-binding transcription factor activity[d][13], regulation of protein localization[d][2], аутофагия[d][5][5][2], positive regulation of NF-kappaB transcription factor activity[d][13][4], defense response to virus[d][14][4][5][…], protein ubiquitination[d][5], activation of innate immune response[d][4], positive regulation of I-kappaB kinase/NF-kappaB signaling[d][4][13], врождённый иммунитет[d][5][5][10], вирусный процесс[d][5], positive regulation of MAPK cascade[d][4], pattern recognition receptor signaling pathway[d][5] һәм negative regulation of viral entry into host cell[d][10]
Изображение Gene Atlas

TRIM5 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[15][16]

Искәрмәләр

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 2,3 2,4 2,5 Levine B., Dinkins C., Chauhan S. et al. TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition // Developmental Cell — Elsevier, 2014. — 16 p. — ISSN 1534-5807; 1878-1551 — doi:10.1016/J.DEVCEL.2014.06.013 — PMID:25127057
  3. ↑ S Cairo, A Reymond The tripartite motif family identifies cell compartments // EMBO J. — NPG, 2001. — ISSN 0261-4189; 1460-2075 — doi:10.1093/EMBOJ/20.9.2140 — PMID:11331580
  4. ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 Pertel T., Strambio-De-Castillia C., Luban J. et al. TRIM5 is an innate immune sensor for the retrovirus capsid lattice // Nature / M. Skipper — NPG, Springer Science+Business Media, 2011. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE09976 — PMID:21512573
  5. ↑ 5,00 5,01 5,02 5,03 5,04 5,05 5,06 5,07 5,08 5,09 5,10 5,11 5,12 5,13 5,14 5,15 5,16 GOA
  6. ↑ Luban J. TRIM5α associates with proteasomal subunits in cells while in complex with HIV-1 virions // Retrovirology — BMC, Springer Science+Business Media, 2011. — ISSN 1742-4690 — doi:10.1186/1742-4690-8-93 — PMID:22078707
  7. ↑ 7,0 7,1 Pertel T., Luban J. p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha // J. Virol. — ASM, 2010. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.02412-09 — PMID:20357094
  8. ↑ Schoultz I., Kufer T. A. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation // PLOS ONE / PLOS ONE Editors — PLoS, 2012. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0041255 — PMID:22829933
  9. ↑ Woodsmith J., Jenn R. C., Sanderson C. M. Systematic analysis of dimeric E3-RING interactions reveals increased combinatorial complexity in human ubiquitination networks, Systematic Analysis of Dimeric E3-RING Interactions Reveals Increased Combinatorial Complexity in Human Ubiquitination Networks // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2012. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M111.016162 — PMID:22493164
  10. ↑ 10,0 10,1 10,2 Uchil P. D., Luna J. M., Quinlan B. D. et al. TRIM E3 ligases interfere with early and late stages of the retroviral life cycle // PLoS Pathog. — PLoS, 2008. — ISSN 1553-7366; 1553-7374 — doi:10.1371/JOURNAL.PPAT.0040016 — PMID:18248090
  11. ↑ GOA
  12. ↑ Dean M., Sodroski J., Winkler C. et al. Unique features of TRIM5alpha among closely related human TRIM family members // Virology — Elsevier, 2007. — ISSN 0042-6822; 1096-0341; 1089-862X — doi:10.1016/J.VIROL.2006.10.035 — PMID:17156811
  13. ↑ 13,0 13,1 13,2 Pertel T., Uchil P. D., Siegel S. J. et al. TRIM protein-mediated regulation of inflammatory and innate immune signaling and its association with antiretroviral activity // J. Virol. — ASM, 2012. — 16 p. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.01804-12 — PMID:23077300
  14. ↑ Nakayama E. E., Shioda T. TRIM5α and Species Tropism of HIV/SIV // Frontiers in microbiology — Frontiers Media, 2012. — ISSN 1664-302X — doi:10.3389/FMICB.2012.00013 — PMID:22291694
  15. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  16. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • 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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