FMR1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/FMR1 latin yazuında])
FMR1
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген FMR1[d][1]
Молекулярная функция гомодимеризация белка[d][2], poly(U) RNA binding[d][3][4], ribosome binding[d][5], poly(G) binding[d][4], связывание с белками плазмы[d][6][7][8][…], protein heterodimerization activity[d][9], nucleic acid binding[d][10], translation initiation factor binding[d][5], mRNA binding[d][11][12][13][…], G-quadruplex RNA binding[d][14][15], RNA strand annealing activity[d][16], siRNA binding[d][16], miRNA binding[d][16], mRNA 3'-UTR binding[d][17], mRNA 5'-UTR binding[d][18], translation repressor activity[d][7], microtubule binding[d][10], chromatin binding[d][10], methylated histone binding[d][19], sequence-specific mRNA binding[d][20][21], transmembrane transporter binding[d][22], RNA stem-loop binding[d][23][18], dynein complex binding[d][10], RNA binding[d][24][25][26][…], связывание похожих белков[d][27][28][7], RNA binding[d][3][29][30][…], mRNA binding[d][31][10][22][…], mRNA 3'-UTR binding[d][32][33], гомодимеризация белка[d][9][33] һәм translation regulator activity[d][33]
Күзәнәк компоненты Цитоплазма[34][35][36][…], axon terminus[d][10], Дендритный шипик[d][35][35], нуклеоплазма[d][37][38], SMN complex[d][39], mRNA cap binding complex[d][10], дендрит[d][10][10], ядрышко[d][40][10][38][…], neuron projection[d][10][39], cytoplasmic ribonucleoprotein granule[d][41][42][43], Төш[35][35][44][…], polysomal ribosome[d][6], Перикарион[d][10][10][8][…], perinuclear region of cytoplasm[d][10][5], рибонуклеопротеин[d][45][46], Постсинаптическое уплотнение[d][35], chromocenter[d][10], аксон[d][35][35], Межклеточные контакты[d][10], neuronal ribonucleoprotein granule[d][35], filopodium tip[d][10][10], postsynaptic membrane[d][10], Полисома[d][35][47][12][…], Тельце Кахаля[d][35][48], Хромосома[10][10], Конус роста[d][35][41], центромера[d][10], growth cone filopodium[d][10], viral replication complex[d][49], күзәнәк мембраны[d][10], extrinsic component of plasma membrane[d][10], glial cell projection[d][10], cell projection[d][10][8], мембрана[d][35][50], dendritic filopodium[d][35], presynaptic membrane[d][10], пресинапс[d][35], постсинапс[d][10], Синапс[10][10], цитозоль[d][10], messenger ribonucleoprotein complex[d][30], Төш[10][10][51][…], Цитоплазма[40][10][46][…], Полисома[d][10][45][14][…], cytoplasmic stress granule[d][10], Постсинаптическое уплотнение[d][10][33], Тельце Кахаля[d][10], мембрана[d][10][52], аксон[d][10][10][33], Конус роста[d][10][8][33], ribonucleoprotein granule[d][33], cytoplasmic ribonucleoprotein granule[d][10][8][39][…], neuronal cell body[d][33], Дендритный шипик[d][10][10][33], dendritic spine neck[d][33], neuronal ribonucleoprotein granule[d][10][33], пресинапс[d][10][33], dendritic filopodium[d][10][33] һәм axon cytoplasm[d][10]
Биологический процесс Lua хатасы: too many expensive function calls.
Изображение Gene Atlas
 FMR1 Викиҗыентыкта

FMR1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[55][56]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. ↑ 1,0 1,1 UniProt
  2. ↑ Y Zhang, J P O'Connor, Siomi M. C. et al. The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2 // EMBO J. — NPG, 1995. — ISSN 0261-4189; 1460-2075 — doi:10.1002/(ISSN)1460-2075 — PMID:7489725
  3. ↑ 3,0 3,1 Siomi H. Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome // Cell — Cell Press, Elsevier BV, 1994. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(94)90232-1 — PMID:8156595
  4. ↑ 4,0 4,1 Siomi H. The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein // Cell — Cell Press, Elsevier BV, 1993. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(93)90420-U — PMID:7688265
  5. ↑ 5,0 5,1 5,2 Nouri K., Brunsveld L., Milroy L. G. Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin // PLOS ONE / PLOS ONE Editors — PLoS, 2014. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0091465 — PMID:24658146
  6. ↑ 6,0 6,1 Mandel J., Adinolfi S., Schenck A. et al. 82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization // Human Molecular Genetics — OUP, 2003. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDG181 — PMID:12837692
  7. ↑ 7,0 7,1 7,2 Fischer U. Evidence that fragile X mental retardation protein is a negative regulator of translation // Human Molecular Genetics — OUP, 2001. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/10.4.329 — PMID:11157796
  8. ↑ 8,0 8,1 8,2 8,3 8,4 Oostra B. A. Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells // Exp. Neurol. — Elsevier BV, 2004. — ISSN 0014-4886; 1090-2430; 1055-8330; 1522-9661 — doi:10.1016/J.EXPNEUROL.2004.05.039 — PMID:15380484
  9. ↑ 9,0 9,1 Y Zhang, J P O'Connor, Siomi M. C. et al. The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2 // EMBO J. — NPG, 1995. — ISSN 0261-4189; 1460-2075 — doi:10.1002/(ISSN)1460-2075 — PMID:7489725
  10. ↑ 10,00 10,01 10,02 10,03 10,04 10,05 10,06 10,07 10,08 10,09 10,10 10,11 10,12 10,13 10,14 10,15 10,16 10,17 10,18 10,19 10,20 10,21 10,22 10,23 10,24 10,25 10,26 10,27 10,28 10,29 10,30 10,31 10,32 10,33 10,34 10,35 10,36 10,37 10,38 10,39 10,40 10,41 10,42 10,43 10,44 10,45 10,46 10,47 10,48 10,49 10,50 10,51 10,52 10,53 10,54 10,55 10,56 10,57 10,58 10,59 10,60 10,61 10,62 10,63 10,64 10,65 GOA
  11. ↑ Ashley C. T., Wilkinson K. D., D Reines et al. FMR1 protein: conserved RNP family domains and selective RNA binding // Science / H. Thorp — AAAS, 1993. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.7692601 — PMID:7692601
  12. ↑ 12,0 12,1 Hashimoto H., Visootsak J. Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2015. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1423094112 — PMID:25561520
  13. ↑ Fischer U. Evidence that fragile X mental retardation protein is a negative regulator of translation // Human Molecular Genetics — OUP, 2001. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/10.4.329 — PMID:11157796
  14. ↑ 14,0 14,1 14,2 Zhou H., Khetani R. S., Kosik K. S. et al. MOV10 and FMRP regulate AGO2 association with microRNA recognition elements // Cell Reports — Cell Press, Elsevier BV, 2014. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2014.10.054 — PMID:25464849
  15. ↑ Mandel J., Schaeffer C., Moine H. et al. The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer // Nucleic Acids Res. — OUP, University of Oxford, 2008. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKN472 — PMID:18653529
  16. ↑ 16,0 16,1 16,2 16,3 Provost P. Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs // Journal of Biomedicine and Biotechnology — Hindawi Publishing Corporation, 2006. — ISSN 1110-7243; 1110-7251 — doi:10.1155/JBB/2006/64347 — PMID:17057366
  17. ↑ Zalfa F., Rubeis S. D., Grant S. G. et al. A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability // Nat. Neurosci. — NPG, 2007. — ISSN 1097-6256; 1546-1726 — doi:10.1038/NN1893 — PMID:17417632
  18. ↑ 18,0 18,1 Moine H., Bardoni B. A novel function for fragile X mental retardation protein in translational activation // PLoS Biol. / J. A. Eisen — PLoS, 2009. — ISSN 1544-9173; 1545-7885 — doi:10.1371/JOURNAL.PBIO.1000016 — PMID:19166269
  19. ↑ 19,0 19,1 Xu C., Prisic S., Kutateladze T. G. et al. A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response // Cell — Cell Press, Elsevier BV, 2014. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2014.03.040 — PMID:24813610
  20. ↑ L. Chen, Yun S. W., J. Seto et al. The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences // Neuroscience / J. L. Gómez — Elsevier BV, 2003. — ISSN 0306-4522; 1873-7544 — doi:10.1016/S0306-4522(03)00406-8 — PMID:12927206
  21. ↑ Mukherjee N., Corcoran D. L., Hafner M. et al. FMRP targets distinct mRNA sequence elements to regulate protein expression // Nature / M. Skipper — NPG, Springer Science+Business Media, 2012. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE11737 — PMID:23235829
  22. ↑ 22,0 22,1 Hashimoto H., Visootsak J. Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2015. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1423094112 — PMID:25561520
  23. ↑ Eddy S., Stefani G., Darnell R. B. Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes // Genes Dev. — Cold Spring Harbor Laboratory Press, 2005. — ISSN 0890-9369; 1549-5477 — doi:10.1101/GAD.1276805 — PMID:15805463
  24. ↑ Siomi H. Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome // Cell — Cell Press, Elsevier BV, 1994. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(94)90232-1 — PMID:8156595
  25. ↑ C Bagni Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains // RNA — Cold Spring Harbor Laboratory Press, 1999. — ISSN 1355-8382; 1469-9001 — doi:10.1017/S1355838299990647 — PMID:10496225
  26. ↑ Stoecklin G. Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins // Mol. Cell. Biol. — ASM, 2014. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.00766-14 — PMID:25225333
  27. ↑ Pastore A., Pauwels K. On the aggregation properties of FMRP--a link with the FXTAS syndrome? // FEBS J. — Wiley-Blackwell, 2011. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033 — doi:10.1111/J.1742-4658.2011.08108.X — PMID:21446998
  28. ↑ Regan L. Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein // Structure / C. D. Lima — Cell Press, Elsevier BV, 2007. — ISSN 0969-2126; 1878-4186 — doi:10.1016/J.STR.2007.06.022 — PMID:17850748
  29. ↑ C Bagni Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains // RNA — Cold Spring Harbor Laboratory Press, 1999. — ISSN 1355-8382; 1469-9001 — doi:10.1017/S1355838299990647 — PMID:10496225
  30. ↑ 30,0 30,1 Stoecklin G. Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins // Mol. Cell. Biol. — ASM, 2014. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.00766-14 — PMID:25225333
  31. ↑ Ashley C. T., Wilkinson K. D., D Reines et al. FMR1 protein: conserved RNP family domains and selective RNA binding // Science / H. Thorp — AAAS, 1993. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.7692601 — PMID:7692601
  32. ↑ Zalfa F., Rubeis S. D., Grant S. G. et al. A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability // Nat. Neurosci. — NPG, 2007. — ISSN 1097-6256; 1546-1726 — doi:10.1038/NN1893 — PMID:17417632
  33. ↑ 33,00 33,01 33,02 33,03 33,04 33,05 33,06 33,07 33,08 33,09 33,10 33,11 33,12 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
  34. ↑ Hollingworth D., Pastore A., Adinolfi S. et al. The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction // Structure / C. D. Lima — Cell Press, Elsevier BV, 2006. — ISSN 0969-2126; 1878-4186 — doi:10.1016/J.STR.2005.09.018 — PMID:16407062
  35. ↑ 35,00 35,01 35,02 35,03 35,04 35,05 35,06 35,07 35,08 35,09 35,10 35,11 35,12 35,13 35,14 35,15 GOA
  36. ↑ Bardoni B. The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons // Human Molecular Genetics — OUP, 2006. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDL074 — PMID:16571602
  37. ↑ F Tamanini, Kirkpatrick L. L., J Schonkeren et al. The fragile X-related proteins FXR1P and FXR2P contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins // Human Molecular Genetics — OUP, 2000. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/9.10.1487 — PMID:10888599
  38. ↑ 38,0 38,1 Bardoni B. The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons // Human Molecular Genetics — OUP, 2006. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDL074 — PMID:16571602
  39. ↑ 39,0 39,1 39,2 Branlant C. In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2008. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M707304200 — PMID:18093976
  40. ↑ 40,0 40,1 Hollingworth D., Pastore A., Adinolfi S. et al. The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction // Structure / C. D. Lima — Cell Press, Elsevier BV, 2006. — ISSN 0969-2126; 1878-4186 — doi:10.1016/J.STR.2005.09.018 — PMID:16407062
  41. ↑ 41,0 41,1 Oostra B. A. Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells // Exp. Neurol. — Elsevier BV, 2004. — ISSN 0014-4886; 1090-2430; 1055-8330; 1522-9661 — doi:10.1016/J.EXPNEUROL.2004.05.039 — PMID:15380484
  42. ↑ Branlant C. In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2008. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M707304200 — PMID:18093976
  43. ↑ Villacé P., Marión R. M., Ortín J. The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs // Nucleic Acids Res. — OUP, University of Oxford, 2004. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKH552 — PMID:15121898
  44. ↑ Ceman S. Fragile X mental retardation protein FMRP binds mRNAs in the nucleus // Mol. Cell. Biol. — ASM, 2009. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.01377-08 — PMID:18936162
  45. ↑ 45,0 45,1 Mrowka R., Meier J. C. Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2008. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M807354200 — PMID:19097999
  46. ↑ 46,0 46,1 Y. Feng, D. Absher, Eberhart D. E. et al. FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association // Mol. Cell — Cell Press, Elsevier BV, 1997. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(00)80012-X — PMID:9659908
  47. ↑ Y. Feng, D. Absher, Eberhart D. E. et al. FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association // Mol. Cell — Cell Press, Elsevier BV, 1997. — ISSN 1097-2765; 1097-4164 — doi:10.1016/S1097-2765(00)80012-X — PMID:9659908
  48. ↑ Fatimy R. E., Côté J. Nuclear Fragile X Mental Retardation Protein is localized to Cajal bodies // PLOS Genetics — PLoS, 2013. — ISSN 1553-7390; 1553-7404 — doi:10.1371/JOURNAL.PGEN.1003890 — PMID:24204304
  49. ↑ 49,0 49,1 49,2 Cui S., Gabriel G. Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus // Nat. Commun. / J. D. Heber — NPG, 2014. — ISSN 2041-1723 — doi:10.1038/NCOMMS4259 — PMID:24514761
  50. ↑ Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom. — Wiley, 2010. — ISSN 1076-5174; 1096-9888 — doi:10.1002/JMS.1696 — PMID:19946888
  51. ↑ Ceman S. Fragile X mental retardation protein FMRP binds mRNAs in the nucleus // Mol. Cell. Biol. — ASM, 2009. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.01377-08 — PMID:18936162
  52. ↑ Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom. — Wiley, 2010. — ISSN 1076-5174; 1096-9888 — doi:10.1002/JMS.1696 — PMID:19946888
  53. ↑ 53,0 53,1 Antar L. N., Li C., Zhang H. et al. Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses // Mol. Cell. Neurosci. — Elsevier BV, 2017. — ISSN 1044-7431; 1095-9327 — doi:10.1016/J.MCN.2006.02.001 — PMID:16631377
  54. ↑ Xu C., Prisic S., Kutateladze T. G. et al. A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response // Cell — Cell Press, Elsevier BV, 2014. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2014.03.040 — PMID:24813610
  55. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  56. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар[үзгәртү | вики-текстны 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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Чыганак — https://tt.wikipedia.org/w/index.php?title=FMR1&oldid=4128569