Beta-2 adrenergic receptor

Details

Name
Beta-2 adrenergic receptor
Synonyms
  • ADRB2R
  • B2AR
  • Beta-2 adrenoceptor
  • Beta-2 adrenoreceptor
Gene Name
ADRB2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037061|Beta-2 adrenergic receptor
MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAK
FERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTAS
IETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQE
AINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRF
HVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQD
NLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNT
GEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL
Number of residues
413
Molecular Weight
46458.32
Theoretical pI
7.44
GO Classification
Functions
beta2-adrenergic receptor activity / dopamine binding / drug binding / epinephrine binding / norepinephrine binding / potassium channel regulator activity / protein homodimerization activity
Processes
activation of adenylate cyclase activity / activation of transmembrane receptor protein tyrosine kinase activity / adenylate cyclase-activating adrenergic receptor signaling pathway / adenylate cyclase-modulating G-protein coupled receptor signaling pathway / aging / associative learning / bone resorption / brown fat cell differentiation / cell surface receptor signaling pathway / cell-cell signaling / cellular response to hypoxia / desensitization of G-protein coupled receptor protein signaling pathway by arrestin / diaphragm contraction / diet induced thermogenesis / endosome to lysosome transport / estrous cycle / excitatory postsynaptic potential / female pregnancy / heat generation / liver regeneration / mitophagy in response to mitochondrial depolarization / negative regulation of angiogenesis / negative regulation of inflammatory response / negative regulation of multicellular organism growth / negative regulation of ossification / negative regulation of platelet aggregation / negative regulation of smooth muscle contraction / negative regulation of urine volume / positive regulation of apoptotic process / positive regulation of ATPase activity / positive regulation of autophagosome maturation / positive regulation of bone mineralization / positive regulation of cell proliferation / positive regulation of lipophagy / positive regulation of MAPK cascade / positive regulation of potassium ion transport / positive regulation of protein ubiquitination / positive regulation of skeletal muscle tissue growth / positive regulation of sodium ion transport / positive regulation of the force of heart contraction by epinephrine / positive regulation of transcription from RNA polymerase II promoter / positive regulation of vasodilation / receptor-mediated endocytosis / regulation of calcium ion transport / regulation of sensory perception of pain / response to cold / response to dexamethasone / response to estrogen / response to monoamine / response to progesterone / response to testosterone / synaptic transmission, glutamatergic / vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure / wound healing
Components
apical plasma membrane / axon / dendritic spine / early endosome / endosome / integral component of plasma membrane / lysosome / neuronal cell body membrane / nucleus / plasma membrane / receptor complex / sarcolemma
General Function
Protein homodimerization activity
Specific Function
Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
Pfam Domain Function
Transmembrane Regions
35-58 72-95 107-129 151-174 197-220 275-298 306-329
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0020478|Beta-2 adrenergic receptor (ADRB2)
ATGGGGCAACCCGGGAACGGCAGCGCCTTCTTGCTGGCACCCAATAGAAGCCATGCGCCG
GACCACGACGTCACGCAGCAAAGGGACGAGGTGTGGGTGGTGGGCATGGGCATCGTCATG
TCTCTCATCGTCCTGGCCATCGTGTTTGGCAATGTGCTGGTCATCACAGCCATTGCCAAG
TTCGAGCGTCTGCAGACGGTCACCAACTACTTCATCACTTCACTGGCCTGTGCTGATCTG
GTCATGGGCCTGGCAGTGGTGCCCTTTGGGGCCGCCCATATTCTTATGAAAATGTGGACT
TTTGGCAACTTCTGGTGCGAGTTTTGGACTTCCATTGATGTGCTGTGCGTCACGGCCAGC
ATTGAGACCCTGTGCGTGATCGCAGTGGATCGCTACTTTGCCATTACTTCACCTTTCAAG
TACCAGAGCCTGCTGACCAAGAATAAGGCCCGGGTGATCATTCTGATGGTGTGGATTGTG
TCAGGCCTTACCTCCTTCTTGCCCATTCAGATGCACTGGTACCGGGCCACCCACCAGGAA
GCCATCAACTGCTATGCCAATGAGACCTGCTGTGACTTCTTCACGAACCAAGCCTATGCC
ATTGCCTCTTCCATCGTGTCCTTCTACGTTCCCCTGGTGATCATGGTCTTCGTCTACTCC
AGGGTCTTTCAGGAGGCCAAAAGGCAGCTCCAGAAGATTGACAAATCTGAGGGCCGCTTC
CATGTCCAGAACCTTAGCCAGGTGGAGCAGGATGGGCGGACGGGGCATGGACTCCGCAGA
TCTTCCAAGTTCTGCTTGAAGGAGCACAAAGCCCTCAAGACGTTAGGCATCATCATGGGC
ACTTTCACCCTCTGCTGGCTGCCCTTCTTCATCGTTAACATTGTGCATGTGATCCAGGAT
AACCTCATCCGTAAGGAAGTTTACATCCTCCTAAATTGGATAGGCTATGTCAATTCTGGT
TTCAATCCCCTTATCTACTGCCGGAGCCCAGATTTCAGGATTGCCTTCCAGGAGCTTCTG
TGCCTGCGCAGGTCTTCTTTGAAGGCCTATGGGAATGGCTACTCCAGCAACGGCAACACA
GGGGAGCAGAGTGGATATCACGTGGAACAGGAGAAAGAAAATAAACTGCTGTGTGAAGAC
CTCCCAGGCACGGAAGACTTTGTGGGCCATCAAGGTACTGTGCCTAGCGATAACATTGAT
TCACAAGGGAGGAATTGTAGTACAAATGACTCACTGCTGTAA
Chromosome Location
5
Locus
5q31-q32
External Identifiers
ResourceLink
UniProtKB IDP07550
UniProtKB Entry NameADRB2_HUMAN
GenBank Protein ID29371
GenBank Gene IDY00106
GenAtlas IDADRB2
HGNC IDHGNC:286
General References
  1. Chung FZ, Lentes KU, Gocayne J, Fitzgerald M, Robinson D, Kerlavage AR, Fraser CM, Venter JC: Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors. FEBS Lett. 1987 Jan 26;211(2):200-6. [Article]
  2. Kobilka BK, Frielle T, Dohlman HG, Bolanowski MA, Dixon RA, Keller P, Caron MG, Lefkowitz RJ: Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions. J Biol Chem. 1987 May 25;262(15):7321-7. [Article]
  3. Schofield PR, Rhee LM, Peralta EG: Primary structure of the human beta-adrenergic receptor gene. Nucleic Acids Res. 1987 Apr 24;15(8):3636. [Article]
  4. Kobilka BK, Dixon RA, Frielle T, Dohlman HG, Bolanowski MA, Sigal IS, Yang-Feng TL, Francke U, Caron MG, Lefkowitz RJ: cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor. Proc Natl Acad Sci U S A. 1987 Jan;84(1):46-50. [Article]
  5. Emorine LJ, Marullo S, Delavier-Klutchko C, Kaveri SV, Durieu-Trautmann O, Strosberg AD: Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization. Proc Natl Acad Sci U S A. 1987 Oct;84(20):6995-9. [Article]
  6. Reihsaus E, Innis M, MacIntyre N, Liggett SB: Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects. Am J Respir Cell Mol Biol. 1993 Mar;8(3):334-9. [Article]
  7. Rupert JL, Monsalve MV, Devine DV, Hochachka PW: Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population. Ann Hum Genet. 2000 Mar;64(Pt 2):135-43. [Article]
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  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  10. Chung FZ, Wang CD, Potter PC, Venter JC, Fraser CM: Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation. J Biol Chem. 1988 Mar 25;263(9):4052-5. [Article]
  11. O'Dowd BF, Hnatowich M, Caron MG, Lefkowitz RJ, Bouvier M: Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor. J Biol Chem. 1989 May 5;264(13):7564-9. [Article]
  12. Valiquette M, Parent S, Loisel TP, Bouvier M: Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor. EMBO J. 1995 Nov 15;14(22):5542-9. [Article]
  13. Gurevich VV, Dion SB, Onorato JJ, Ptasienski J, Kim CM, Sterne-Marr R, Hosey MM, Benovic JL: Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors. J Biol Chem. 1995 Jan 13;270(2):720-31. [Article]
  14. Lin FT, Krueger KM, Kendall HE, Daaka Y, Fredericks ZL, Pitcher JA, Lefkowitz RJ: Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1. J Biol Chem. 1997 Dec 5;272(49):31051-7. [Article]
  15. Cao TT, Deacon HW, Reczek D, Bretscher A, von Zastrow M: A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature. 1999 Sep 16;401(6750):286-90. [Article]
  16. Luttrell LM, Ferguson SS, Daaka Y, Miller WE, Maudsley S, Della Rocca GJ, Lin F, Kawakatsu H, Owada K, Luttrell DK, Caron MG, Lefkowitz RJ: Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science. 1999 Jan 29;283(5402):655-61. [Article]
  17. Moffett S, Rousseau G, Lagace M, Bouvier M: The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization. J Neurochem. 2001 Jan;76(1):269-79. [Article]
  18. Whistler JL, Enquist J, Marley A, Fong J, Gladher F, Tsuruda P, Murray SR, Von Zastrow M: Modulation of postendocytic sorting of G protein-coupled receptors. Science. 2002 Jul 26;297(5581):615-20. [Article]
  19. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [Article]
  20. Berthouze M, Venkataramanan V, Li Y, Shenoy SK: The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization. EMBO J. 2009 Jun 17;28(12):1684-96. doi: 10.1038/emboj.2009.128. Epub 2009 May 7. [Article]
  21. Xie L, Xiao K, Whalen EJ, Forrester MT, Freeman RS, Fong G, Gygi SP, Lefkowitz RJ, Stamler JS: Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL. Sci Signal. 2009 Jul 7;2(78):ra33. doi: 10.1126/scisignal.2000444. [Article]
  22. Nabhan JF, Pan H, Lu Q: Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to mediate ubiquitination of the beta2-adrenergic receptor. EMBO Rep. 2010 Aug;11(8):605-11. doi: 10.1038/embor.2010.80. Epub 2010 Jun 18. [Article]
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  28. Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Kuhn P, Weis WI, Kobilka BK, Stevens RC: High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science. 2007 Nov 23;318(5854):1258-65. Epub 2007 Oct 25. [Article]
  29. Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EY, Velasquez J, Kuhn P, Stevens RC: A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor. Structure. 2008 Jun;16(6):897-905. doi: 10.1016/j.str.2008.05.001. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00521CarteololapprovedyesantagonistDetails
DB00816OrciprenalineapprovedyesagonistDetails
DB00867Ritodrineapproved, investigationalyesagonistDetails
DB00871TerbutalineapprovedyesagonistDetails
DB00901BitolterolwithdrawnyesDetails
DB00938SalmeterolapprovedyesagonistDetails
DB00983Formoterolapproved, investigationalyesagonistDetails
DB01001Salbutamolapproved, vet_approvedyesagonistDetails
DB00373TimololapprovedyesantagonistDetails
DB00571Propranololapproved, investigationalunknownantagonistDetails
DB00598LabetalolapprovedyesantagonistDetails
DB00612BisoprololapprovednoantagonistDetails
DB00668Epinephrineapproved, vet_approvedyesagonistDetails
DB00852Pseudoephedrineapprovedunknownpartial agonistDetails
DB00866Alprenololexperimental, withdrawnyesantagonistDetails
DB00960Pindololapproved, investigationalyespartial agonistDetails
DB01064Isoprenalineapproved, investigationalyesagonistbinderDetails
DB01151Desipramineapproved, investigationalunknownantagonistDetails
DB01203NadololapprovedunknownantagonistDetails
DB01210LevobunololapprovedyesantagonistDetails
DB01214MetipranololapprovedyesantagonistDetails
DB01274Arformoterolapproved, investigationalyesagonistDetails
DB01366Procaterolapproved, investigationalyesagonistDetails
DB01407Clenbuterolapproved, investigational, vet_approvedyesagonistDetails
DB01136Carvedilolapproved, investigationalunknownantagonistDetails
DB01288Fenoterolapproved, investigationalyesagonistDetails
DB01291PirbuterolapprovedyesagonistDetails
DB01580OxprenololapprovedunknownantagonistDetails
DB01359Penbutololapproved, investigationalyesantagonistpartial agonistDetails
DB00368NorepinephrineapprovedyesagonistDetails
DB01408BambuterolinvestigationalyesagonistDetails
DB05039IndacaterolapprovedyesagonistDetails
DB05849NCX 950investigationalunknownDetails
DB06262Droxidopaapproved, investigationalyesagonistDetails
DB00264Metoprololapproved, investigationalnoantagonistDetails
DB00195Betaxololapproved, investigationalunknownantagonistDetails
DB00489SotalolapprovedyesantagonistDetails
DB01295BevantololexperimentalunknownantagonistDetails
DB01193Acebutololapproved, investigationalunknownpartial agonistDetails
DB01102ArbutamineapprovedunknownagonistDetails
DB00841DobutamineapprovedunknownagonistDetails
DB07543(S)-carazololexperimentalunknownDetails
DB00449DipivefrinapprovedyesagonistDetails
DB08807Bopindololexperimentalunknownpartial agonistDetails
DB08808BupranololexperimentalunknownantagonistDetails
DB04861Nebivololapproved, investigationalunknownantagonistDetails
DB00925PhenoxybenzamineapprovedunknownDetails
DB01363Ephedra sinica rootnutraceuticalyesagonistDetails
DB06216AsenapineapprovedunknownantagonistDetails
DB00248CabergolineapprovedunknownbinderDetails
DB00221IsoetharineapprovedunknownagonistDetails
DB00335AtenololapprovedunknownantagonistDetails
DB00397Phenylpropanolamineapproved, vet_approved, withdrawnunknownagonistDetails
DB09080OlodaterolapprovedyesagonistDetails
DB09082VilanterolapprovedyesagonistDetails
DB04846Celiprololapproved, investigationalyesagonistDetails
DB13139Levosalbutamolapproved, investigationalyesagonistDetails
DB09013BefunololexperimentalunknownDetails
DB12248TulobuterolinvestigationalunknownregulatorDetails
DB01917PutrescineexperimentalunknownDetails
DB03566SpermidineexperimentalunknownDetails
DB00127Spermineexperimental, nutraceuticalunknownDetails
DB01182PropafenoneapprovedunknownantagonistDetails
DB09204ArotinololinvestigationalyesantagonistDetails
DB09273DoxofyllineexperimentalyesagonistDetails
DB06814Protokylolapproved, vet_approvedyesagonistDetails
DB11124RacepinephrineapprovedyesagonistDetails
DB11587EtafedrineapprovedyesagonistDetails
DB05590BedoradrineinvestigationalyesagonistDetails
DB01238Aripiprazoleapproved, investigationalunknownligandDetails
DB01364EphedrineapprovedyesagonistDetails
DB09185Viloxazineapproved, investigational, withdrawnunknownantagonistDetails
DB13624MethoxyphenamineapprovedunknownregulatorDetails
DB01118Amiodaroneapproved, investigationalyesinhibitordownregulatorDetails
DB00182Amphetamineapproved, illicit, investigationalunknownagonistDetails
DB00540NortriptylineapprovedunknownantagonistDetails
DB00726TrimipramineapprovedunknownbinderDetails
DB00334Olanzapineapproved, investigationalnoinhibitorDetails
DB00217BethanidineapprovedunknownantagonistDetails
DB01365MephentermineapprovedunknownagonistDetails
DB06726BufuralolexperimentalunknownantagonistDetails
DB13345Dihydroergocristineapproved, experimentalyesantagonistagonistDetails
DB01049Ergoloid mesylateapprovedyesantagonistagonistDetails
DB11273DihydroergocornineapprovedyesantagonistagonistDetails
DB11278DL-MethylephedrineapprovedyesagonistDetails
DB00715Paroxetineapproved, investigationalunknowninhibitorDetails
DB00785CryptenamineapprovedunknowninhibitorpotentiatorDetails
DB00867Ritodrineapproved, investigationalyesagonistdownregulatorDetails
DB00264Metoprololapproved, investigationalunknowninhibitorDetails