Wikipedia

ADRB2

ADRB2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[44][45]

ADRB2
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген бета-2 адренорецептор[d][1]
Молекуляр функция adenylate cyclase binding[d][2], adrenergic receptor activity[d][3], beta2-adrenergic receptor activity[d][3][3][4][…], enzyme binding[d][2], гомодимеризация белка[d][5], potassium channel regulator activity[d][6], связывание с белками плазмы[d][7][8][9][…], G protein-coupled receptor activity[d][2][2], signal transducer activity[d][3], norepinephrine binding[d][5], epinephrine binding[d][10], amyloid-beta binding[d][11], adrenergic receptor activity[d][2][10], beta2-adrenergic receptor activity[d][11][2][2][…] һәм protein-containing complex binding[d][11]
Күзәнәк компоненты мембрана[d][3][3]
Биологик процесс positive regulation of autophagosome maturation[d][12], adenylate cyclase-activating G protein-coupled receptor signaling pathway[d][2][2], regulation of sodium ion transport[d][2], endosome to lysosome transport[d][13], рецепторно-опосредованный эндоцитоз[d][5], cell surface receptor signaling pathway[d][14], regulation of systemic arterial blood pressure by norepinephrine-epinephrine[d][2], negative regulation of smooth muscle contraction[d][2][10], regulation of smooth muscle contraction[d][2], adenylate cyclase-modulating G protein-coupled receptor signaling pathway[d][15], костная резорбция[d][2], adenylate cyclase-activating adrenergic receptor signaling pathway[d][10], heat generation[d][2], desensitization of G protein-coupled receptor signaling pathway by arrestin[d][5], positive regulation of MAPK cascade[d][5], G protein-coupled receptor signaling pathway[d][3][3], positive regulation of bone mineralization[d][2], activation of adenylate cyclase activity[d][5], brown fat cell differentiation[d][2], activation of transmembrane receptor protein tyrosine kinase activity[d][16], positive regulation of protein ubiquitination[d][17], negative regulation of multicellular organism growth[d][2], передача сигнала между клетками[d][3], diet induced thermogenesis[d][2], norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure[d][2][10], positive regulation of lipophagy[d][12], response to cold[d][2], положительная регуляция транскрипции РНК полимеразой II промотор[d][2], передача сигнала[d][2], protein deubiquitination[d][2], membrane organization[d][2], adrenergic receptor signaling pathway[d][18], blood vessel diameter maintenance[d][2], G protein-coupled receptor signaling pathway[d][2][2][2], adenylate cyclase-modulating G protein-coupled receptor signaling pathway[d][19][10], positive regulation of protein kinase A signaling[d][11][2], positive regulation of mini excitatory postsynaptic potential[d][2], positive regulation of protein serine/threonine kinase activity[d][11], positive regulation of cold-induced thermogenesis[d][20][2], cellular response to amyloid-beta[d][11][2], response to psychosocial stress[d][11], positive regulation of cAMP-dependent protein kinase activity[d][11] һәм positive regulation of AMPA receptor activity[d][11]
Тәэсир итешә arformoterol[d][21], фенотерол[d][21], формотерол[d][21], indacaterol[d][21], mirabegron[d][21], olodaterol[d][21], орципреналин[d][21], vilanterol[d][21], zinterol[d][21], адреналин[d][21], изопреналин[d][21], сальметерол[d][21], Добутамин[d][21], (−)-эфедрин[d][21], пиндолол[d][21], сальбутамол[d][21], тербуталин[d][21], алпренолол[d][21], атенолол[d][21], бетаксолол[d][21], bupranolol[d][21], carazolol[d][21], карведилол[d][21], cicloprolol[d][21], лабеталол[d][21], levobetaxolol[d][21], levobunolol[d][21], метопролол[d][21], надолол[d][21], пропафенон[d][21], пропранолол[d][21], соталол[d][21], sr-59230a free base[d][21], isoxsuprine[d][22], pirbuterol[d][23], reproterol[d][24], адреналин[d][25], vilanterol[d][26], норадреналин[d][27], (−)-эфедрин[d][28], кленбутерол[d][29], carmoterol[d][30], PF-610355[d][31], isoproterenol hydrochloride[d][32], procaterol[d][33], bitolterol mesylate[d][34], carteolol hydrochloride[d][35], dipivefrin hydrochloride[d][36], DL-dobutamine hydrochloride[d][37], esmolol hydrochloride[d][38], levobunolol hydrochloride[d][39], propafenone hydrochloride[d][40], propranolol hydrochloride[d][41], sotalol hydrochloride[d][42] һәм timolol maleate[d][43]
Изображение Gene Atlas

Искәрмәләр

үзгәртү
  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 GOA
  3. ↑ 3,0 3,1 3,2 3,3 3,4 3,5 3,6 3,7 3,8 GOA
  4. ↑ Bouvier M. Hetero-oligomerization between beta2- and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M313310200 — PMID:15123695
  5. ↑ 5,0 5,1 5,2 5,3 5,4 5,5 Bouvier M. Hetero-oligomerization between beta2- and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M313310200 — PMID:15123695
  6. ↑ Bouvier M. G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase // 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.M205035200 — PMID:12297500
  7. ↑ Berthouze M. The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization // EMBO J. — NPG, 2009. — ISSN 0261-4189; 1460-2075 — doi:10.1038/EMBOJ.2009.128 — PMID:19424180
  8. ↑ Percherancier Y., Simpson J. C., Pepperkok R. et al. CNIH4 interacts with newly synthesized GPCR and controls their export from the endoplasmic reticulum // Traffic — Wiley-Blackwell, 2014. — ISSN 1398-9219; 1600-0854 — doi:10.1111/TRA.12148 — PMID:24405750
  9. ↑ Lefkowitz R. J., Hall R. A., Premont R. T. The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange, The β2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange // Nature / M. Skipper — NPG, Springer Science+Business Media, 1998. — ISSN 1476-4687; 0028-0836 — doi:10.1038/33458 — PMID:9560162
  10. ↑ 10,0 10,1 10,2 10,3 10,4 10,5 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. ↑ 11,0 11,1 11,2 11,3 11,4 11,5 11,6 11,7 11,8 Wang D., G Govindaiah, Liu R. et al. Binding of amyloid beta peptide to beta2 adrenergic receptor induces PKA-dependent AMPA receptor hyperactivity // FASEB J. — FASEB, 2010. — ISSN 0892-6638; 1530-6860 — doi:10.1096/FJ.10-156661 — PMID:20395454
  12. ↑ 12,0 12,1 Lizaso A., Tan K., Lee Y. β-adrenergic receptor-stimulated lipolysis requires the RAB7-mediated autolysosomal lipid degradation // Autophagy — Landes Bioscience, Taylor & Francis, 2013. — ISSN 1554-8627; 1554-8635 — doi:10.4161/AUTO.24893 — PMID:23708524
  13. ↑ Gagnon A. W., L. Kallal, Benovic J. L. Role of clathrin-mediated endocytosis in agonist-induced down-regulation of the beta2-adrenergic receptor, Role of Clathrin-mediated Endocytosis in Agonist-induced Down-regulation of the β2-Adrenergic Receptor // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1998. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.273.12.6976 — PMID:9507004
  14. ↑ Kobilka B. K. Ligand-regulated internalization and recycling of human beta 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1992. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:1371121
  15. ↑ Emorine L. J., S Marullo, C Delavier-Klutchko et al. Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1987. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.84.20.6995 — PMID:2823249
  16. ↑ Luttrell L. M., Lefkowitz R. J. The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor // 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.275.13.9572 — PMID:10734107
  17. ↑ Baillie G., Houslay M. D. Mdm2 directs the ubiquitination of beta-arrestin-sequestered cAMP phosphodiesterase-4D5 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.008078 — PMID:19372219
  18. ↑ Puthenveedu M. A., Zastrow M. v. Structure of an arrestin2-clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.023366 — PMID:19710023
  19. ↑ Emorine L. J., S Marullo, C Delavier-Klutchko et al. Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1987. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.84.20.6995 — PMID:2823249
  20. ↑ Russell A., Léger B. Beta(1)/beta(2)/beta(3)-adrenoceptor knockout mice are obese and cold-sensitive but have normal lipolytic responses to fasting // FEBS Letters — Elsevier BV, 2002. — ISSN 0014-5793; 1873-3468 — doi:10.1016/S0014-5793(02)03387-2 — PMID:12387862
  21. ↑ 21,00 21,01 21,02 21,03 21,04 21,05 21,06 21,07 21,08 21,09 21,10 21,11 21,12 21,13 21,14 21,15 21,16 21,17 21,18 21,19 21,20 21,21 21,22 21,23 21,24 21,25 21,26 21,27 21,28 21,29 21,30 21,31 21,32 IUPHAR/BPS Guide to PHARMACOLOGY
  22. ↑ Open Targets Platform
  23. ↑ Open Targets Platform
  24. ↑ Open Targets Platform
  25. ↑ Open Targets Platform
  26. ↑ Open Targets Platform
  27. ↑ Open Targets Platform
  28. ↑ Open Targets Platform
  29. ↑ Open Targets Platform
  30. ↑ Open Targets Platform
  31. ↑ Open Targets Platform
  32. ↑ Open Targets Platform
  33. ↑ Open Targets Platform
  34. ↑ Open Targets Platform
  35. ↑ Open Targets Platform
  36. ↑ Open Targets Platform
  37. ↑ Open Targets Platform
  38. ↑ Open Targets Platform
  39. ↑ Open Targets Platform
  40. ↑ Open Targets Platform
  41. ↑ Open Targets Platform
  42. ↑ Open Targets Platform
  43. ↑ Open Targets Platform
  44. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  45. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

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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