ARRB1

ARRB1
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген ARRB1[d][1]
Молекуляр функция GTPase activator activity[d][2], histone acetyltransferase activity[d][3], enzyme inhibitor activity[d][4], связывание с рецептором инсулино-подобного фактора роста[d][5], transcription factor binding[d][3], mitogen-activated protein kinase kinase binding[d][6], clathrin adaptor activity[d][6], protein phosphorylated amino acid binding[d][6], cysteine-type endopeptidase inhibitor activity involved in apoptotic process[d][6], связывание с белками плазмы[d][7][8][9][…], AP-2 adaptor complex binding[d][6], alpha-1B adrenergic receptor binding[d][6], Связывание с рецептором вазопрессина V2[d][6], phosphoprotein binding[d][6], angiotensin receptor binding[d][2], ubiquitin protein ligase binding[d][5], arrestin family protein binding[d][10][6], signaling receptor binding[d][6], enzyme binding[d][6], estrogen receptor binding[d][6], alpha-1A adrenergic receptor binding[d][6], follicle-stimulating hormone receptor binding[d][6], transmembrane transporter binding[d][6], clathrin binding[d][6] һәм G protein-coupled receptor binding[d][11]
Күзәнәк компоненты цитоплазма[6][6][2][…], цитозоль[d][6][6], postsynaptic membrane[d][6], мембрана[d][6], төш[6][6][3], cell projection[d][6], дендритный шипик[d][6], heterotrimeric G-protein complex[d][12], хроматин[d][3], күзәнәк мембранасы[d][13][6], внутренний компонент клетки[d][14], нуклеоплазма[d][6], clathrin-coated pit[d][6], псевдоподия[d][6][6], постсинаптическое уплотнение[d][6], Golgi membrane[d][6], lysosomal membrane[d][6], basolateral plasma membrane[d][6], cytoplasmic vesicle membrane[d][6], цитоплазматическая везикула[d][6][2], ядерные тельца[d][6], эндосома[d][6], төш[6][6][3][…], цитоплазма[6][6][15][…], цитозоль[d][6][6][11], күзәнәк мембранасы[d][13][6][11] һәм цитоплазматическая везикула[d][6][2][11]
Биологик процесс positive regulation of Rho protein signal transduction[d][2], regulation of G protein-coupled receptor signaling pathway[d][6], positive regulation of receptor internalization[d][9], transcription by RNA polymerase II[d][3][6], stress fiber assembly[d][2], follicle-stimulating hormone signaling pathway[d][6], platelet activation[d][6], positive regulation of cysteine-type endopeptidase activity involved in apoptotic process[d][6], negative regulation of GTPase activity[d][6], positive regulation of ERK1 and ERK2 cascade[d][6][16], positive regulation of insulin secretion involved in cellular response to glucose stimulus[d][6], proteasome-mediated ubiquitin-dependent protein catabolic process[d][5], фототрансдукция[d][6], ДНК-зависимая регуляция транскрипции[d][14], транскрипция, ДНК-зависимая[d][14], positive regulation of peptidyl-serine phosphorylation[d][6], negative regulation of interleukin-8 production[d][17], protein ubiquitination[d][5], protein transport[d][6], negative regulation of protein phosphorylation[d][6], positive regulation of smooth muscle cell apoptotic process[d][6], positive regulation of histone H4 acetylation[d][3], positive regulation of protein binding[d][6], negative regulation of NF-kappaB transcription factor activity[d][17], positive regulation of protein ubiquitination[d][6], G protein-coupled receptor internalization[d][18][19], negative regulation of cysteine-type endopeptidase activity involved in apoptotic process[d][6], эндоцитоз[d][6], negative regulation of interleukin-6 production[d][17], positive regulation of histone acetylation[d][3], negative regulation of protein ubiquitination[d][17], negative regulation of ERK1 and ERK2 cascade[d][6], negative regulation of signal transduction[d][6], положительная регуляция транскрипции РНК полимеразой II промотор[d][3][6], передача сигнала[d][6], positive regulation of GTPase activity[d][6], апоптоз[d][6], membrane organization[d][6], regulation of apoptotic process[d][6], ubiquitin-dependent protein catabolic process[d][10][6], negative regulation of Notch signaling pathway[d][10][6], G protein-coupled receptor signaling pathway[d][6][6], positive regulation of protein phosphorylation[d][20][6], позитивная регуляция пролиферации клеток[d][6], негативная регуляция апоптоза[d][6], negative regulation of neuron apoptotic process[d][6], histone acetylation[d][6], G protein-coupled receptor internalization[d][19][18][11], negative regulation of Notch signaling pathway[d][10][6][11] һәм positive regulation of ERK1 and ERK2 cascade[d][6][16][11]

ARRB1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[21][22]

  1. 1,0 1,1 UniProt
  2. 2,0 2,1 2,2 2,3 2,4 2,5 2,6 Milligan G., Lefkowitz R. J. beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2005. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M412924200PMID:15611106
  3. 3,0 3,1 3,2 3,3 3,4 3,5 3,6 3,7 3,8 Ma L. A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription // CellCell Press, Elsevier BV, 2005. — ISSN 0092-8674; 1097-4172doi:10.1016/J.CELL.2005.09.011PMID:16325578
  4. Lohse M. J., Lefkowitz R. J., Caron M. G. beta-Arrestin: a protein that regulates beta-adrenergic receptor function // Science / H. ThorpNorthern America: AAAS, 1990. — ISSN 0036-8075; 1095-9203doi:10.1126/SCIENCE.2163110PMID:2163110
  5. 5,0 5,1 5,2 5,3 Lefkowitz R. J. {beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2005. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M501129200PMID:15878855
  6. 6,00 6,01 6,02 6,03 6,04 6,05 6,06 6,07 6,08 6,09 6,10 6,11 6,12 6,13 6,14 6,15 6,16 6,17 6,18 6,19 6,20 6,21 6,22 6,23 6,24 6,25 6,26 6,27 6,28 6,29 6,30 6,31 6,32 6,33 6,34 6,35 6,36 6,37 6,38 6,39 6,40 6,41 6,42 6,43 6,44 6,45 6,46 6,47 6,48 6,49 6,50 6,51 6,52 6,53 6,54 6,55 6,56 6,57 6,58 6,59 6,60 6,61 6,62 6,63 6,64 6,65 6,66 6,67 6,68 6,69 6,70 6,71 6,72 6,73 6,74 6,75 6,76 6,77 6,78 6,79 6,80 6,81 6,82 GOA
  7. Berthouze M., Lefkowitz R. J. Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2 // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2009. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.0901083106PMID:19363159
  8. Innamorati G., Piccirillo R., Bagnato P. et al. The melanosomal/lysosomal protein OA1 has properties of a G protein-coupled receptor // Pigment Cell Melanoma Res.Wiley-Blackwell, 2006. — ISSN 1755-1471; 1755-148X; 0893-5785; 1600-0749doi:10.1111/J.1600-0749.2006.00292.XPMID:16524428
  9. 9,0 9,1 Scholten D. J., Canals M. Ubiquitination of CXCR7 controls receptor trafficking // PLOS ONE / PLOS ONE EditorsPLoS, 2012. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0034192PMID:22457824
  10. 10,0 10,1 10,2 10,3 Puca L., Brou C., Israël A. Α-arrestin 1 (ARRDC1) and β-arrestins cooperate to mediate Notch degradation in mammals // J. Cell Sci.The Company of Biologists, 2013. — ISSN 0021-9533; 1477-9137doi:10.1242/JCS.130500PMID:23886940
  11. 11,0 11,1 11,2 11,3 11,4 11,5 11,6 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; 1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  12. Prossnitz E. R. Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.C000314200PMID:10823817
  13. 13,0 13,1 Miller W. E., Lefkowitz R. J., Caron M. G. Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes // Science / H. ThorpNorthern America: AAAS, 1999. — ISSN 0036-8075; 1095-9203doi:10.1126/SCIENCE.283.5402.655PMID:9924018
  14. 14,0 14,1 14,2 GOA
  15. Prossnitz E. R. Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.C000314200PMID:10823817
  16. 16,0 16,1 J Zhao beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4 // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.275.4.2479PMID:10644702
  17. 17,0 17,1 17,2 17,3 Wang Y., Tang Y., Teng L. et al. Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling // Nat. Immunol.USA: NPG, 2006. — ISSN 1529-2908; 1529-2916doi:10.1038/NI1294PMID:16378096
  18. 18,0 18,1 Orsini M. J., Parent J. L., Mundell S. J. et al. Trafficking of the HIV coreceptor CXCR4. Role of arrestins and identification of residues in the c-terminal tail that mediate receptor internalization // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1999. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.274.43.31076PMID:10521508
  19. 19,0 19,1 Lefkowitz R. J. Desensitization, internalization, and signaling functions of beta-arrestins demonstrated by RNA interference // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2003. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.262789099PMID:12582207
  20. 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; 1937-9145doi:10.1126/SCISIGNAL.2003627PMID:23633677
  21. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  22. 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.)