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Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (Beta-2 adrenoceptor)

 ADRB2_HUMAN             Reviewed;         413 AA.
P07550; B0LPE4; B2R7X2; O14823; O14824; O14825; O14826; Q4JG18;
Q53GA6; Q6GMT4; Q6P4D8; Q8NEQ9; Q96EC3; Q9UCZ0; Q9UCZ1; Q9UCZ2;
Q9UCZ3; Q9UH95; Q9UHA1; Q9UMZ5;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
05-DEC-2018, entry version 218.
RecName: Full=Beta-2 adrenergic receptor;
AltName: Full=Beta-2 adrenoreceptor;
Short=Beta-2 adrenoceptor;
Name=ADRB2; Synonyms=ADRB2R, B2AR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-27.
TISSUE=Brain;
PubMed=3026848; DOI=10.1016/0014-5793(87)81436-9;
Chung F.-Z., Lentes K.-U., Gocayne J.D., Fitzgerald M.G.,
Robinson D.A., Kerlavage A.R., Fraser C.M., Venter J.C.;
"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. 211:200-206(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-16 AND GLN-27.
PubMed=3034889;
Kobilka B.K., Frielle T., Dohlman H.G., Bolanowski M.A., Dixon R.A.F.,
Keller P., Caron M.G., Lefkowitz R.J.;
"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. 262:7321-7327(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-16 AND GLN-27.
PubMed=3033609; DOI=10.1093/nar/15.8.3636;
Schofield P.R., Rhee L.M., Peralta E.G.;
"Primary structure of the human beta-adrenergic receptor gene.";
Nucleic Acids Res. 15:3636-3636(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-16 AND GLN-27.
PubMed=3025863; DOI=10.1073/pnas.84.1.46;
Kobilka B.K., Dixon R.A.F., Frielle T., Dohlman H.G., Bolanowski M.A.,
Sigal I.S., Yang-Feng T.L., Francke U., Caron M.G., Lefkowitz R.J.;
"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. 84:46-50(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-27.
PubMed=2823249; DOI=10.1073/pnas.84.20.6995;
Emorine L.J., Marullo S., Delavier-Klutchko C., Kaveri S.V.,
Durieu-Trautmann O., Strosberg A.D.;
"Structure of the gene for human beta 2-adrenergic receptor:
expression and promoter characterization.";
Proc. Natl. Acad. Sci. U.S.A. 84:6995-6999(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-16; GLN-27; MET-34
AND ILE-164.
PubMed=8383511; DOI=10.1165/ajrcmb/8.3.334;
Reihsaus E., Innis M., Macintyre N., Liggett S.B.;
"Mutations in the gene encoding for the beta 2-adrenergic receptor in
normal and asthmatic subjects.";
Am. J. Respir. Cell Mol. Biol. 8:334-339(1993).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-27; LEU-159;
PHE-159 AND ARG-375.
TISSUE=Blood;
PubMed=11246467; DOI=10.1046/j.1469-1809.2000.6420135.x;
Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W.;
"Beta2-adrenergic receptor allele frequencies in the Quechua, a high
altitude native population.";
Ann. Hum. Genet. 64:135-143(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-16 AND
GLN-27.
TISSUE=Heart;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-27.
TISSUE=Thyroid;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-27 AND CYS-220.
SeattleSNPs variation discovery resource;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-27.
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-16 AND
GLN-27.
TISSUE=Fetal brain, Leukocyte, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
MUTAGENESIS OF ASP-79, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=2831218;
Chung F.-Z., Wang C.-D., Potter P.C., Venter J.C., Fraser C.M.;
"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. 263:4052-4055(1988).
[16]
PALMITOYLATION AT CYS-341, AND MUTAGENESIS OF CYS-341.
PubMed=2540197;
O'Dowd B.F., Hnatowich M., Caron M.G., Lefkowitz R.J., 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. 264:7564-7569(1989).
[17]
MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, AND
PHOSPHORYLATION AT TYR-141.
PubMed=8521811;
Valiquette M., Parent S., Loisel T.P., Bouvier M.;
"Mutation of tyrosine-141 inhibits insulin-promoted tyrosine
phosphorylation and increased responsiveness of the human beta 2-
adrenergic receptor.";
EMBO J. 14:5542-5549(1995).
[18]
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=7822302; DOI=10.1074/jbc.270.2.720;
Gurevich V.V., Dion S.B., Onorato J.J., Ptasienski J., Kim C.M.,
Sterne-Marr R., Hosey M.M., Benovic J.L.;
"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. 270:720-731(1995).
[19]
INTERACTION WITH ARRB1.
PubMed=9388255; DOI=10.1074/jbc.272.49.31051;
Lin F.-T., Krueger K.M., Kendall H.E., Daaka Y., Fredericks Z.L.,
Pitcher J.A., Lefkowitz R.J.;
"Clathrin-mediated endocytosis of the beta-adrenergic receptor is
regulated by phosphorylation/dephosphorylation of beta-arrestin1.";
J. Biol. Chem. 272:31051-31057(1997).
[20]
INTERACTION WITH SLC9A3R1.
PubMed=10499588; DOI=10.1038/45816;
Cao T.T., Deacon H.W., Reczek D., Bretscher A., von Zastrow M.;
"A kinase-regulated PDZ-domain interaction controls endocytic sorting
of the beta2-adrenergic receptor.";
Nature 401:286-290(1999).
[21]
INTERACTION WITH SRC AND ARRB1.
PubMed=9924018; DOI=10.1126/science.283.5402.655;
Luttrell L.M., Ferguson S.S.G., Daaka Y., Miller W.E., Maudsley S.,
Della Rocca G.J., Lin F.-T., Kawakatsu H., Owada K., Luttrell D.K.,
Caron M.G., Lefkowitz R.J.;
"Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src
protein kinase complexes.";
Science 283:655-661(1999).
[22]
EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, AND
MUTAGENESIS OF 345-SER-SER-346.
PubMed=11146000; DOI=10.1046/j.1471-4159.2001.00005.x;
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. 76:269-279(2001).
[23]
INTERACTION WITH GPRASP1.
PubMed=12142540; DOI=10.1126/science.1073308;
Whistler J.L., Enquist J., Marley A., Fong J., Gladher F., Tsuruda P.,
Murray S.R., Von Zastrow M.;
"Modulation of postendocytic sorting of G protein-coupled receptors.";
Science 297:615-620(2002).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[25]
UBIQUITINATION, DEUBIQUITINATION BY USP20 AND USP33, AND INTERACTION
WITH USP20 AND USP33.
PubMed=19424180; DOI=10.1038/emboj.2009.128;
Berthouze M., Venkataramanan V., Li Y., Shenoy S.K.;
"The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic
receptor recycling and resensitization.";
EMBO J. 28:1684-1696(2009).
[26]
INTERACTION WITH EGLN3 AND VHL, SUBCELLULAR LOCATION, INDUCTION,
UBIQUITINATION, HYDROXYLATION AT PRO-382 AND PRO-395, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19584355; DOI=10.1126/scisignal.2000444;
Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G.,
Gygi S.P., Lefkowitz R.J., Stamler J.S.;
"Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3
and ubiquitylation by pVHL.";
Sci. Signal. 2:RA33-RA33(2009).
[27]
UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARRDC3.
PubMed=20559325; DOI=10.1038/embor.2010.80;
Nabhan J.F., Pan H., Lu Q.;
"Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to
mediate ubiquitination of the beta2-adrenergic receptor.";
EMBO Rep. 11:605-611(2010).
[28]
INTERACTION WITH SNX27.
PubMed=20733053; DOI=10.1083/jcb.201004060;
Lauffer B.E., Melero C., Temkin P., Lei C., Hong W., Kortemme T.,
von Zastrow M.;
"SNX27 mediates PDZ-directed sorting from endosomes to the plasma
membrane.";
J. Cell Biol. 190:565-574(2010).
[29]
INTERACTION WITH SNX27.
PubMed=21602791; DOI=10.1038/ncb2252;
Temkin P., Lauffer B., Jager S., Cimermancic P., Krogan N.J.,
von Zastrow M.;
"SNX27 mediates retromer tubule entry and endosome-to-plasma membrane
trafficking of signalling receptors.";
Nat. Cell Biol. 13:715-721(2011).
[30]
SUBCELLULAR LOCATION, AND INTERACTION WITH ARRDC3.
PubMed=25220262; DOI=10.1002/pro.2549;
Qi S., O'Hayre M., Gutkind J.S., Hurley J.H.;
"Insights into beta2-adrenergic receptor binding from structures of
the N-terminal lobe of ARRDC3.";
Protein Sci. 23:1708-1716(2014).
[31]
INTERACTION WITH CNIH4.
PubMed=24405750; DOI=10.1111/tra.12148;
Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y.,
Simpson J.C., Pepperkok R., Bouvier M.;
"CNIH4 interacts with newly synthesized GPCR and controls their export
from the endoplasmic reticulum.";
Traffic 15:383-400(2014).
[32]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH
CARAZOLOL, AND TOPOLOGY.
PubMed=17952055; DOI=10.1038/nature06325;
Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S.,
Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P.,
Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I.,
Kobilka B.K.;
"Crystal structure of the human beta2 adrenergic G-protein-coupled
receptor.";
Nature 450:383-387(2007).
[33]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH
CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, AND
PALMITOYLATION AT CYS-341.
PubMed=17962520; DOI=10.1126/science.1150577;
Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F.,
Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I.,
Kobilka B.K., Stevens R.C.;
"High-resolution crystal structure of an engineered human beta2-
adrenergic G protein-coupled receptor.";
Science 318:1258-1265(2007).
[34]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL
AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, AND PALMITOYLATION AT
CYS-341.
PubMed=18547522; DOI=10.1016/j.str.2008.05.001;
Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P.,
Chien E.Y., Velasquez J., Kuhn P., Stevens R.C.;
"A specific cholesterol binding site is established by the 2.8 A
structure of the human beta2-adrenergic receptor.";
Structure 16:897-905(2008).
[35]
VARIANTS ARG-16 AND GLN-27, CHARACTERIZATION, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=7915137; DOI=10.1021/bi00198a006;
Green S.A., Turki J., Innis M., Ligget S.B.;
"Amino-terminal polymorphisms of the human beta 2-adrenergic receptor
impart distinct agonist-promoted regulatory properties.";
Biochemistry 33:9414-9419(1994).
[36]
VARIANT ARG-16, AND POLYMORPHISM.
PubMed=7706471; DOI=10.1172/JCI117838;
Turki J., Pak J., Green S.A., Martin R.J., Liggett S.B.;
"Genetic polymorphisms of the beta 2-adrenergic receptor in nocturnal
and nonnocturnal asthma. Evidence that Gly16 correlates with the
nocturnal phenotype.";
J. Clin. Invest. 95:1635-1641(1995).
-!- 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. {ECO:0000269|PubMed:2831218,
ECO:0000269|PubMed:7915137}.
-!- SUBUNIT: Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and
ARRB2. Interacts with SRC, USP20 and USP33. Interacts with VHL;
the interaction, which is increased on hydroxylation of ADRB2,
ubiquitinates ADRB2 leading to its degradation. Interacts with
EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3
ligase-mediated ubiquitination. Interacts (via PDZ-binding motif)
with SNX27 (via PDZ domain); the interaction is required when
endocytosed to prevent degradation in lysosomes and promote
recycling to the plasma membrane. Interacts with CNIH4
(PubMed:24405750). Interacts with ARRDC3 (PubMed:20559325,
PubMed:25220262). {ECO:0000269|PubMed:10499588,
ECO:0000269|PubMed:12142540, ECO:0000269|PubMed:17952055,
ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522,
ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:19584355,
ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:20733053,
ECO:0000269|PubMed:21602791, ECO:0000269|PubMed:24405750,
ECO:0000269|PubMed:25220262, ECO:0000269|PubMed:7822302,
ECO:0000269|PubMed:9388255, ECO:0000269|PubMed:9924018}.
-!- INTERACTION:
P32121:ARRB2; NbExp=3; IntAct=EBI-491169, EBI-714559;
Q96B67:ARRDC3; NbExp=6; IntAct=EBI-491169, EBI-2875665;
Q5TCQ9:MAGI3; NbExp=9; IntAct=EBI-491169, EBI-310506;
O14745:SLC9A3R1; NbExp=6; IntAct=EBI-491169, EBI-349787;
P12931:SRC; NbExp=3; IntAct=EBI-491169, EBI-621482;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19584355,
ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:25220262,
ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}; Multi-
pass membrane protein {ECO:0000269|PubMed:19584355}. Early
endosome {ECO:0000269|PubMed:20559325}. Note=Colocalizes with VHL
at the cell membrane (PubMed:19584355). Activated receptors are
internalized into endosomes prior to their degradation in
lysosomes (PubMed:20559325). {ECO:0000269|PubMed:19584355,
ECO:0000269|PubMed:20559325}.
-!- PTM: Palmitoylated; may reduce accessibility of Ser-345 and Ser-
346 by anchoring Cys-341 to the plasma membrane. Agonist
stimulation promotes depalmitoylation and further allows Ser-345
and Ser-346 phosphorylation. {ECO:0000269|PubMed:11146000,
ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522,
ECO:0000269|PubMed:2540197}.
-!- PTM: Phosphorylated by PKA and BARK upon agonist stimulation,
which mediates homologous desensitization of the receptor. PKA-
mediated phosphorylation seems to facilitate phosphorylation by
BARK.
-!- PTM: Phosphorylation of Tyr-141 is induced by insulin and leads to
supersensitization of the receptor. {ECO:0000269|PubMed:8521811}.
-!- PTM: Polyubiquitinated. Agonist-induced ubiquitination leads to
sort internalized receptors to the lysosomes for degradation
(PubMed:19424180, PubMed:20559325). Deubiquitination by USP20 and
USP33, leads to ADRB2 recycling and resensitization after
prolonged agonist stimulation. USP20 and USP33 are constitutively
associated and are dissociated immediately after agonist
stimulation. Ubiquitination by the VHL-E3 ligase complex is
oxygen-dependent. {ECO:0000269|PubMed:19424180,
ECO:0000269|PubMed:20559325}.
-!- PTM: Hydroxylation by EGLN3 occurs only under normoxia and
increases the interaction with VHL and the subsequent
ubiquitination and degradation of ADRB2.
{ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:19584355}.
-!- POLYMORPHISM: The Gly-16 allele is overrepresented in individuals
affected by nocturnal asthma as compared to controls, and appears
to be an important genetic factor in the expression of this
asthmatic phenotype.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Adrenergic receptor subfamily. ADRB2 sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=BAD96745.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/adrb2/";
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EMBL; X04827; CAA28511.1; -; mRNA.
EMBL; Y00106; CAA68289.1; -; Genomic_DNA.
EMBL; M15169; AAA88015.1; -; mRNA.
EMBL; J02960; AAA88017.1; -; Genomic_DNA.
EMBL; AF022953; AAB82148.1; -; Genomic_DNA.
EMBL; AF022954; AAB82149.1; -; Genomic_DNA.
EMBL; AF022955; AAB82150.1; -; Genomic_DNA.
EMBL; AF022956; AAB82151.1; -; Genomic_DNA.
EMBL; AF169225; AAD48036.1; -; Genomic_DNA.
EMBL; AF202305; AAF17569.1; -; Genomic_DNA.
EMBL; AF203386; AAF20199.1; -; Genomic_DNA.
EMBL; AY136741; AAN01267.1; -; mRNA.
EMBL; AK313151; BAG35969.1; -; mRNA.
EMBL; AK223025; BAD96745.1; ALT_INIT; mRNA.
EMBL; DQ094845; AAY88739.1; -; Genomic_DNA.
EMBL; EU332834; ABY87523.1; -; Genomic_DNA.
EMBL; CH471062; EAW61798.1; -; Genomic_DNA.
EMBL; BC012481; AAH12481.3; -; mRNA.
EMBL; BC063486; AAH63486.2; -; mRNA.
EMBL; BC073856; AAH73856.1; -; mRNA.
CCDS; CCDS4292.1; -.
PIR; A27525; QRHUB2.
RefSeq; NP_000015.1; NM_000024.5.
UniGene; Hs.2551; -.
PDB; 1GQ4; X-ray; 1.90 A; A=409-413.
PDB; 2R4R; X-ray; 3.40 A; A=1-365.
PDB; 2R4S; X-ray; 3.40 A; A=24-365.
PDB; 2RH1; X-ray; 2.40 A; A=1-230, A=263-365.
PDB; 3D4S; X-ray; 2.80 A; A=1-230, A=263-348.
PDB; 3KJ6; X-ray; 3.40 A; A=2-365.
PDB; 3NY8; X-ray; 2.84 A; A=1-230, A=263-348.
PDB; 3NY9; X-ray; 2.84 A; A=1-230, A=263-348.
PDB; 3NYA; X-ray; 3.16 A; A=1-230, A=263-348.
PDB; 3P0G; X-ray; 3.50 A; A=1-230, A=263-365.
PDB; 3PDS; X-ray; 3.50 A; A=25-230, A=264-348.
PDB; 3SN6; X-ray; 3.20 A; R=29-365.
PDB; 4GBR; X-ray; 3.99 A; A=29-365.
PDB; 4LDE; X-ray; 2.79 A; A=29-348.
PDB; 4LDL; X-ray; 3.10 A; A=29-348.
PDB; 4LDO; X-ray; 3.20 A; A=29-348.
PDB; 4QKX; X-ray; 3.30 A; A=29-348.
PDB; 5D5A; X-ray; 2.48 A; A=1-230, A=263-365.
PDB; 5D5B; X-ray; 3.80 A; A=1-230, A=263-365.
PDB; 5D6L; X-ray; 3.20 A; A=1-223, A=264-365.
PDB; 5JQH; X-ray; 3.20 A; A/B=30-348.
PDB; 5X7D; X-ray; 2.70 A; A=1-230, A=264-365.
PDB; 6CSY; X-ray; 2.96 A; A=29-365.
PDBsum; 1GQ4; -.
PDBsum; 2R4R; -.
PDBsum; 2R4S; -.
PDBsum; 2RH1; -.
PDBsum; 3D4S; -.
PDBsum; 3KJ6; -.
PDBsum; 3NY8; -.
PDBsum; 3NY9; -.
PDBsum; 3NYA; -.
PDBsum; 3P0G; -.
PDBsum; 3PDS; -.
PDBsum; 3SN6; -.
PDBsum; 4GBR; -.
PDBsum; 4LDE; -.
PDBsum; 4LDL; -.
PDBsum; 4LDO; -.
PDBsum; 4QKX; -.
PDBsum; 5D5A; -.
PDBsum; 5D5B; -.
PDBsum; 5D6L; -.
PDBsum; 5JQH; -.
PDBsum; 5X7D; -.
PDBsum; 6CSY; -.
ProteinModelPortal; P07550; -.
SMR; P07550; -.
BioGrid; 106663; 246.
CORUM; P07550; -.
DIP; DIP-33948N; -.
ELM; P07550; -.
IntAct; P07550; 15.
MINT; P07550; -.
STRING; 9606.ENSP00000305372; -.
BindingDB; P07550; -.
ChEMBL; CHEMBL210; -.
DrugBank; DB07543; (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol.
DrugBank; DB01193; Acebutolol.
DrugBank; DB00866; Alprenolol.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00182; Amphetamine.
DrugBank; DB01102; Arbutamine.
DrugBank; DB01274; Arformoterol.
DrugBank; DB06216; Asenapine.
DrugBank; DB00335; Atenolol.
DrugBank; DB01408; Bambuterol.
DrugBank; DB00195; Betaxolol.
DrugBank; DB00217; Bethanidine.
DrugBank; DB01295; Bevantolol.
DrugBank; DB00612; Bisoprolol.
DrugBank; DB00901; Bitolterol.
DrugBank; DB08807; Bopindolol.
DrugBank; DB06726; Bufuralol.
DrugBank; DB08808; Bupranolol.
DrugBank; DB00248; Cabergoline.
DrugBank; DB00521; Carteolol.
DrugBank; DB01136; Carvedilol.
DrugBank; DB04846; Celiprolol.
DrugBank; DB01407; Clenbuterol.
DrugBank; DB01151; Desipramine.
DrugBank; DB00449; Dipivefrin.
DrugBank; DB00841; Dobutamine.
DrugBank; DB06262; Droxidopa.
DrugBank; DB01363; Ephedra.
DrugBank; DB00668; Epinephrine.
DrugBank; DB01288; Fenoterol.
DrugBank; DB00983; Formoterol.
DrugBank; DB05039; Indacaterol.
DrugBank; DB00221; Isoetarine.
DrugBank; DB01064; Isoprenaline.
DrugBank; DB00598; Labetalol.
DrugBank; DB01210; Levobunolol.
DrugBank; DB13139; Levosalbutamol.
DrugBank; DB01365; Mephentermine.
DrugBank; DB01214; Metipranolol.
DrugBank; DB00264; Metoprolol.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB01203; Nadolol.
DrugBank; DB05849; NCX 950.
DrugBank; DB04861; Nebivolol.
DrugBank; DB00368; Norepinephrine.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00334; Olanzapine.
DrugBank; DB09080; Olodaterol.
DrugBank; DB00816; Orciprenaline.
DrugBank; DB01580; Oxprenolol.
DrugBank; DB01359; Penbutolol.
DrugBank; DB00925; Phenoxybenzamine.
DrugBank; DB00397; Phenylpropanolamine.
DrugBank; DB00960; Pindolol.
DrugBank; DB01291; Pirbuterol.
DrugBank; DB01366; Procaterol.
DrugBank; DB00571; Propranolol.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB00867; Ritodrine.
DrugBank; DB01001; Salbutamol.
DrugBank; DB00938; Salmeterol.
DrugBank; DB00489; Sotalol.
DrugBank; DB00871; Terbutaline.
DrugBank; DB00373; Timolol.
DrugBank; DB00726; Trimipramine.
DrugBank; DB09082; Vilanterol.
GuidetoPHARMACOLOGY; 29; -.
MoonDB; P07550; Predicted.
TCDB; 9.A.14.3.5; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P07550; -.
PhosphoSitePlus; P07550; -.
SwissPalm; P07550; -.
BioMuta; ADRB2; -.
DMDM; 296439450; -.
EPD; P07550; -.
PaxDb; P07550; -.
PeptideAtlas; P07550; -.
PRIDE; P07550; -.
ProteomicsDB; 52013; -.
DNASU; 154; -.
Ensembl; ENST00000305988; ENSP00000305372; ENSG00000169252.
GeneID; 154; -.
KEGG; hsa:154; -.
CTD; 154; -.
DisGeNET; 154; -.
EuPathDB; HostDB:ENSG00000169252.5; -.
GeneCards; ADRB2; -.
HGNC; HGNC:286; ADRB2.
HPA; HPA003431; -.
HPA; HPA075322; -.
MalaCards; ADRB2; -.
MIM; 109690; gene+phenotype.
neXtProt; NX_P07550; -.
OpenTargets; ENSG00000169252; -.
PharmGKB; PA39; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00940000159538; -.
HOVERGEN; HBG106962; -.
InParanoid; P07550; -.
KO; K04142; -.
OMA; KETCCDF; -.
OrthoDB; EOG091G06VI; -.
PhylomeDB; P07550; -.
TreeFam; TF316350; -.
Reactome; R-HSA-390696; Adrenoceptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SignaLink; P07550; -.
SIGNOR; P07550; -.
ChiTaRS; ADRB2; human.
EvolutionaryTrace; P07550; -.
GeneWiki; Beta-2_adrenergic_receptor; -.
GenomeRNAi; 154; -.
PRO; PR:P07550; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000169252; Expressed in 181 organ(s), highest expression level in squamous epithelium.
ExpressionAtlas; P07550; baseline and differential.
Genevisible; P07550; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; TAS:ProtInc.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0016020; C:membrane; NAS:ARUK-UCL.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; IDA:HGNC.
GO; GO:0008179; F:adenylate cyclase binding; IEA:Ensembl.
GO; GO:0004935; F:adrenergic receptor activity; IBA:GO_Central.
GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
GO; GO:0004941; F:beta2-adrenergic receptor activity; IDA:HGNC.
GO; GO:0051379; F:epinephrine binding; IBA:GO_Central.
GO; GO:0051380; F:norepinephrine binding; IDA:HGNC.
GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:HGNC.
GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0071875; P:adrenergic receptor signaling pathway; IDA:CAFA.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0002032; P:desensitization of G protein-coupled receptor signaling pathway by arrestin; IDA:HGNC.
GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
GO; GO:0008333; P:endosome to lysosome transport; TAS:ProtInc.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0031649; P:heat generation; IEA:Ensembl.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IBA:GO_Central.
GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IBA:GO_Central.
GO; GO:2000969; P:positive regulation of AMPA receptor activity; IGI:ARUK-UCL.
GO; GO:1901098; P:positive regulation of autophagosome maturation; IDA:GO_Central.
GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; TAS:ARUK-UCL.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:1904504; P:positive regulation of lipophagy; IDA:GO_Central.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:HGNC.
GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; IGI:ARUK-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IGI:ARUK-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:HGNC.
GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:1990911; P:response to psychosocial stress; TAS:ARUK-UCL.
CDD; cd15957; 7tmA_Beta2_AR; 1.
InterPro; IPR002233; ADR_fam.
InterPro; IPR000332; ADRB2_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24248:SF21; PTHR24248:SF21; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01103; ADRENERGICR.
PRINTS; PR00562; ADRENRGCB2AR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Endosome; G-protein coupled receptor; Glycoprotein; Hydroxylation;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 413 Beta-2 adrenergic receptor.
/FTId=PRO_0000069130.
TOPO_DOM 1 34 Extracellular.
TRANSMEM 35 58 Helical; Name=1.
TOPO_DOM 59 71 Cytoplasmic.
TRANSMEM 72 95 Helical; Name=2.
TOPO_DOM 96 106 Extracellular.
TRANSMEM 107 129 Helical; Name=3.
TOPO_DOM 130 150 Cytoplasmic.
TRANSMEM 151 174 Helical; Name=4.
TOPO_DOM 175 196 Extracellular.
TRANSMEM 197 220 Helical; Name=5.
TOPO_DOM 221 274 Cytoplasmic.
TRANSMEM 275 298 Helical; Name=6.
TOPO_DOM 299 305 Extracellular.
TRANSMEM 306 329 Helical; Name=7.
TOPO_DOM 330 413 Cytoplasmic.
REGION 193 207 Agonist and antagonist binding.
REGION 286 293 Agonist and antagonist binding.
REGION 312 316 Agonist and antagonist binding.
MOTIF 410 413 PDZ-binding.
BINDING 113 113 Agonist or antagonist.
BINDING 118 118 Agonist or antagonist.
MOD_RES 141 141 Phosphotyrosine.
{ECO:0000269|PubMed:8521811}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 261 261 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 262 262 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 345 345 Phosphoserine; by PKA.
{ECO:0000269|PubMed:11146000}.
MOD_RES 346 346 Phosphoserine; by PKA.
{ECO:0000269|PubMed:11146000}.
MOD_RES 355 355 Phosphoserine; by BARK. {ECO:0000305}.
MOD_RES 356 356 Phosphoserine; by BARK. {ECO:0000305}.
MOD_RES 382 382 4-hydroxyproline.
{ECO:0000269|PubMed:19584355}.
MOD_RES 395 395 4-hydroxyproline.
{ECO:0000269|PubMed:19584355}.
LIPID 341 341 S-palmitoyl cysteine.
{ECO:0000269|PubMed:17962520,
ECO:0000269|PubMed:18547522,
ECO:0000269|PubMed:2540197}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 106 191
DISULFID 184 190
VARIANT 15 15 N -> S (in dbSNP:rs33973603).
/FTId=VAR_049373.
VARIANT 16 16 G -> R (common polymorphism;
dbSNP:rs1042713).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3025863,
ECO:0000269|PubMed:3033609,
ECO:0000269|PubMed:3034889,
ECO:0000269|PubMed:7706471,
ECO:0000269|PubMed:7915137,
ECO:0000269|PubMed:8383511,
ECO:0000269|Ref.8}.
/FTId=VAR_003452.
VARIANT 27 27 E -> Q (in dbSNP:rs1042714).
{ECO:0000269|PubMed:11246467,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2823249,
ECO:0000269|PubMed:3025863,
ECO:0000269|PubMed:3026848,
ECO:0000269|PubMed:3033609,
ECO:0000269|PubMed:3034889,
ECO:0000269|PubMed:7915137,
ECO:0000269|PubMed:8383511,
ECO:0000269|Ref.10, ECO:0000269|Ref.11,
ECO:0000269|Ref.12, ECO:0000269|Ref.8}.
/FTId=VAR_003453.
VARIANT 34 34 V -> M (in dbSNP:rs990810566).
{ECO:0000269|PubMed:8383511}.
/FTId=VAR_003454.
VARIANT 159 159 I -> F. {ECO:0000269|PubMed:11246467}.
/FTId=VAR_009125.
VARIANT 159 159 I -> L. {ECO:0000269|PubMed:11246467}.
/FTId=VAR_009124.
VARIANT 164 164 T -> I (in dbSNP:rs1800888).
{ECO:0000269|PubMed:8383511}.
/FTId=VAR_003455.
VARIANT 220 220 S -> C (in dbSNP:rs3729943).
{ECO:0000269|Ref.11}.
/FTId=VAR_025101.
VARIANT 375 375 K -> R (in dbSNP:rs771585355).
{ECO:0000269|PubMed:11246467}.
/FTId=VAR_009394.
MUTAGEN 79 79 D->N: Affects binding of catecholamines,
and produces an uncoupling between the
receptor and stimulatory G proteins.
{ECO:0000269|PubMed:2831218}.
MUTAGEN 141 141 Y->F: Abolishes insulin-induced tyrosine
phosphorylation and insulin-induced
receptor supersensitization.
{ECO:0000269|PubMed:8521811}.
MUTAGEN 341 341 C->G: Uncoupled receptor.
{ECO:0000269|PubMed:2540197}.
MUTAGEN 345 346 SS->AA: Delayed agonist-promoted
desensitization.
{ECO:0000269|PubMed:11146000}.
MUTAGEN 350 350 Y->A: Does not affect insulin-induced
tyrosine phosphorylation or insulin-
induced receptor supersensitization.
{ECO:0000269|PubMed:8521811}.
MUTAGEN 354 354 Y->A: Does not affect insulin-induced
tyrosine phosphorylation or insulin-
induced receptor supersensitization.
{ECO:0000269|PubMed:8521811}.
MUTAGEN 366 366 Y->F: Does not affect insulin-induced
tyrosine phosphorylation or insulin-
induced receptor supersensitization.
{ECO:0000269|PubMed:8521811}.
CONFLICT 71 71 F -> L (in Ref. 9; BAG35969).
{ECO:0000305}.
CONFLICT 216 216 V -> A (in Ref. 8; AAN01267).
{ECO:0000305}.
CONFLICT 261 261 S -> P (in Ref. 10; BAD96745).
{ECO:0000305}.
CONFLICT 402 402 Q -> P (in Ref. 14; AAH12481).
{ECO:0000305}.
STRAND 25 27 {ECO:0000244|PDB:3P0G}.
HELIX 31 60 {ECO:0000244|PDB:2RH1}.
HELIX 62 64 {ECO:0000244|PDB:2RH1}.
HELIX 67 85 {ECO:0000244|PDB:2RH1}.
HELIX 87 96 {ECO:0000244|PDB:2RH1}.
HELIX 102 136 {ECO:0000244|PDB:2RH1}.
STRAND 137 139 {ECO:0000244|PDB:2RH1}.
HELIX 147 170 {ECO:0000244|PDB:2RH1}.
TURN 171 174 {ECO:0000244|PDB:2RH1}.
HELIX 179 186 {ECO:0000244|PDB:2RH1}.
STRAND 187 189 {ECO:0000244|PDB:3SN6}.
HELIX 197 207 {ECO:0000244|PDB:2RH1}.
HELIX 209 229 {ECO:0000244|PDB:2RH1}.
TURN 235 239 {ECO:0000244|PDB:2R4R}.
HELIX 267 298 {ECO:0000244|PDB:2RH1}.
STRAND 299 303 {ECO:0000244|PDB:4LDL}.
HELIX 305 317 {ECO:0000244|PDB:2RH1}.
HELIX 318 320 {ECO:0000244|PDB:2RH1}.
HELIX 322 325 {ECO:0000244|PDB:2RH1}.
HELIX 326 328 {ECO:0000244|PDB:2RH1}.
HELIX 330 339 {ECO:0000244|PDB:2RH1}.
TURN 340 342 {ECO:0000244|PDB:5JQH}.
TURN 345 347 {ECO:0000244|PDB:2R4R}.
SEQUENCE 413 AA; 46459 MW; 408C22731C6EDFBE CRC64;
MGQPGNGSAF LLAPNGSHAP DHDVTQERDE VWVVGMGIVM SLIVLAIVFG NVLVITAIAK
FERLQTVTNY FITSLACADL VMGLAVVPFG AAHILMKMWT FGNFWCEFWT SIDVLCVTAS
IETLCVIAVD RYFAITSPFK YQSLLTKNKA RVIILMVWIV SGLTSFLPIQ MHWYRATHQE
AINCYANETC CDFFTNQAYA IASSIVSFYV PLVIMVFVYS RVFQEAKRQL QKIDKSEGRF
HVQNLSQVEQ DGRTGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD
NLIRKEVYIL LNWIGYVNSG FNPLIYCRSP DFRIAFQELL CLRRSSLKAY GNGYSSNGNT
GEQSGYHVEQ EKENKLLCED LPGTEDFVGH QGTVPSDNID SQGRNCSTND SLL


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E1298Rb ELISA kit ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Oryctolagus cuniculus,Rabbit 96T
E1298r ELISA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Rat,Rattus norvegicus 96T
U1298r CLIA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Rat,Rattus norvegicus 96T
U1298b CLIA ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Bos taurus,Bovine 96T
E1298b ELISA ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Bos taurus,Bovine 96T
E1298m ELISA kit Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Mouse,Mus musculus 96T
E1298b ELISA kit ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Bos taurus,Bovine 96T
E1298m ELISA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Mouse,Mus musculus 96T
U1298m CLIA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Mouse,Mus musculus 96T
E1298r ELISA kit Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Rat,Rattus norvegicus 96T
18-461-10500 Alpha-2C adrenergic receptor - Alpha-2C adrenoceptor; Alpha-2C adrenoreceptor; Alpha-2 adrenergic receptor subtype C4 Polyclonal 0.05 ml
18-461-10552 Alpha-2C adrenergic receptor - Alpha-2C adrenoceptor; Alpha-2C adrenoreceptor; Alpha-2 adrenergic receptor subtype C4 Polyclonal 0.05 ml


 

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