Reviewed, UniProtKB/Swiss-Prot P07550 (ADRB2_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-2 adrenergic receptor
Alternative name(s):
    Beta-2 adrenoreceptor
      Short name=Beta-2 adrenoceptor

Gene names

Name:	ADRB2
Synonyms:	ADRB2R, B2AR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Subunit structure	Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC, USP20 and USP33. Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	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. Ref.16 Ref.22 Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.22 Ref.17 Ref.24 Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor. Ubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. 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 By similarity. Ref.25
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.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of transmembrane receptor protein tyrosine kinase activity Traceable author statement. Source: ProtInc desensitization of G-protein coupled receptor protein signaling pathway by arrestin Inferred from direct assay. Source: HGNC endosome to lysosome transport Traceable author statement. Source: ProtInc positive regulation of MAPKKK cascade Inferred from direct assay. Source: HGNC receptor-mediated endocytosis Inferred from direct assay. Source: HGNC
Cellular component	endosome Traceable author statement. Source: ProtInc integral to plasma membrane Inferred from direct assay. Source: UniProtKB lysosome Traceable author statement. Source: ProtInc nucleus Inferred from direct assay. Source: HPA receptor complex Inferred from direct assay. Source: HGNC
Molecular function	beta2-adrenergic receptor activity Inferred from direct assay. Source: HGNC norepinephrine binding Inferred from direct assay. Source: HGNC potassium channel regulator activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2B1	Q14232	1	EBI-491169,EBI-491065

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 413

413

Beta-2 adrenergic receptor

PRO_0000069130

Regions

Topological domain

1 – 34

34

Extracellular Ref.26 Ref.27 Ref.28

Transmembrane

35 – 58

24

1

Topological domain

59 – 71

13

Cytoplasmic Ref.26 Ref.27 Ref.28

Transmembrane

72 – 95

24

2

Topological domain

96 – 106

11

Extracellular Ref.26 Ref.27 Ref.28

Transmembrane

107 – 129

23

3

Topological domain

130 – 150

21

Cytoplasmic Ref.26 Ref.27 Ref.28

Transmembrane

151 – 174

24

4

Topological domain

175 – 196

22

Extracellular Ref.26 Ref.27 Ref.28

Transmembrane

197 – 220

24

5

Topological domain

221 – 274

54

Cytoplasmic Ref.26 Ref.27 Ref.28

Transmembrane

275 – 298

24

6

Topological domain

299 – 305

7

Extracellular Ref.26 Ref.27 Ref.28

Transmembrane

306 – 329

24

7

Topological domain

330 – 413

84

Cytoplasmic Ref.26 Ref.27 Ref.28

Region

193 – 207

15

Agonist and antagonist binding

Region

286 – 293

8

Agonist and antagonist binding

Region

312 – 316

5

Agonist and antagonist binding

Sites

Binding site

113

1

Agonist or antagonist

Binding site

118

1

Agonist or antagonist

Amino acid modifications

Modified residue

141

1

Phosphotyrosine Ref.17

Modified residue

246

1

Phosphoserine Ref.24

Modified residue

261

1

Phosphoserine; by PKA Potential

Modified residue

262

1

Phosphoserine; by PKA Potential

Modified residue

345

1

Phosphoserine; by PKA Ref.22

Modified residue

346

1

Phosphoserine; by PKA Ref.22

Modified residue

355

1

Phosphoserine; by BARK Probable

Modified residue

356

1

Phosphoserine; by BARK Probable

Lipidation

341

1

S-palmitoyl cysteine Ref.16 Ref.22

Glycosylation

6

1

N-linked (GlcNAc...) Probable

Glycosylation

15

1

N-linked (GlcNAc...) Probable

Disulfide bond

106 ↔ 191

Ref.27 Ref.28

Disulfide bond

184 ↔ 190

Ref.27 Ref.28

Natural variations

Natural variant

15

1

N → S: dbSNP rs33973603.

VAR_049373

Natural variant

16

1

G → R Common polymorphism. dbSNP rs1042713.

VAR_003452

Natural variant

27

1

Q → E: dbSNP rs1042714. Ref.14 Ref.29 Ref.6 Ref.9 Ref.11 Ref.13

VAR_003453

Natural variant

34

1

V → M

VAR_003454

Natural variant

159

1

I → F

VAR_009125

Natural variant

159

1

I → L

VAR_009124

Natural variant

164

1

T → I: dbSNP rs1800888. Ref.6

VAR_003455

Natural variant

220

1

S → C: dbSNP rs3729943. Ref.11

VAR_025101

Natural variant

375

1

K → R

VAR_009394

Experimental info

Mutagenesis

79

1

D → N: Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins. Ref.22 Ref.15

Mutagenesis

141

1

Y → F: Abolishes insulin-induced tyrosine phosphorylation and insulin-induced receptor supersensitization. Ref.22 Ref.17

Mutagenesis

341

1

C → G: Uncoupled receptor. Ref.16 Ref.22

Mutagenesis

345 – 346

2

SS → AA: Delayed agonist-promoted desensitization. Ref.22

Mutagenesis

350

1

Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. Ref.22 Ref.17

Mutagenesis

354

1

Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. Ref.22 Ref.17

Mutagenesis

366

1

Y → F: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. Ref.22 Ref.17

Sequence conflict

71

1

F → L in BAG35969. Ref.9

Sequence conflict

216

1

V → A Ref.7

Sequence conflict

216

1

V → A Ref.8

Sequence conflict

261

1

S → P in BAD96745. Ref.10

Sequence conflict

402

1

P → Q in CAA28511. Ref.1

Sequence conflict

402

1

P → Q Ref.2

Sequence conflict

402

1

P → Q in CAA68289. Ref.3

Sequence conflict

402

1

P → Q in AAA88015. Ref.4

Sequence conflict

402

1

P → Q in AAA88017. Ref.5

Sequence conflict

402

1

P → Q in AAB82148. Ref.6

Sequence conflict

402

1

P → Q in AAB82149. Ref.6

Sequence conflict

402

1

P → Q in AAB82150. Ref.6

Sequence conflict

402

1

P → Q in AAB82151. Ref.6

Sequence conflict

402

1

P → Q in AAD48036. Ref.7

Sequence conflict

402

1

P → Q in AAF17569. Ref.7

Sequence conflict

402

1

P → Q in AAF20199. Ref.7

Sequence conflict

402

1

P → Q in AAN01267. Ref.8

Sequence conflict

402

1

P → Q in BAG35969. Ref.9

Sequence conflict

402

1

P → Q in BAD96745. Ref.10

Sequence conflict

402

1

P → Q in AAY88739. Ref.11

Sequence conflict

402

1

P → Q in ABY87523. Ref.12

Sequence conflict

402

1

P → Q in EAW61798. Ref.13

Sequence conflict

402

1

P → Q in AAH63486. Ref.14

Sequence conflict

402

1

P → Q in AAH73856. Ref.14

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

413

Helix Strand Turn

Details...

Helix

31 – 60

30

Helix

62 – 64

3

Helix

67 – 85

19

Helix

87 – 96

10

Helix

102 – 136

35

Beta strand

137 – 139

3

Helix

147 – 170

24

Turn

171 – 174

4

Helix

179 – 186

8

Helix

197 – 207

11

Helix

209 – 229

21

Helix

231 – 237

7

Helix

240 – 243

4

Helix

245 – 260

16

Helix

267 – 298

32

Helix

305 – 317

13

Helix

318 – 320

3

Helix

322 – 325

4

Helix

326 – 328

3

Helix

330 – 339

10

Sequences

	Sequence		Length	Mass (Da)
	P07550-1 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: FB17B56DC1EAD8A4	FASTA	413	46,427
	10 20 30 40 50 60 MGQPGNGSAF LLAPNGSHAP DHDVTQQRDE VWVVGMGIVM SLIVLAIVFG NVLVITAIAK 70 80 90 100 110 120 FERLQTVTNY FITSLACADL VMGLAVVPFG AAHILMKMWT FGNFWCEFWT SIDVLCVTAS 130 140 150 160 170 180 IETLCVIAVD RYFAITSPFK YQSLLTKNKA RVIILMVWIV SGLTSFLPIQ MHWYRATHQE 190 200 210 220 230 240 AINCYANETC CDFFTNQAYA IASSIVSFYV PLVIMVFVYS RVFQEAKRQL QKIDKSEGRF 250 260 270 280 290 300 HVQNLSQVEQ DGRTGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD 310 320 330 340 350 360 NLIRKEVYIL LNWIGYVNSG FNPLIYCRSP DFRIAFQELL CLRRSSLKAY GNGYSSNGNT 370 380 390 400 410 GEQSGYHVEQ EKENKLLCED LPGTEDFVGH QGTVPSDNID SPGRNCSTND SLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors." Chung F.-Z., Lentes K.-U., Gocayne J.D., Fitzgerald M.G., Robinson D.A., Kerlavage A.R., Fraser C.M., Venter J.C. FEBS Lett. 211:200-206(1987) [PubMed: 3026848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions." Kobilka B.K., Frielle T., Dohlman H.G., Bolanowski M.A., Dixon R.A.F., Keller P., Caron M.G., Lefkowitz R.J. J. Biol. Chem. 262:7321-7327(1987) [PubMed: 3034889] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-16.
[3]	"Primary structure of the human beta-adrenergic receptor gene." Schofield P.R., Rhee L.M., Peralta E.G. Nucleic Acids Res. 15:3636-3636(1987) [PubMed: 3033609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-16.
[4]	"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." 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. Proc. Natl. Acad. Sci. U.S.A. 84:46-50(1987) [PubMed: 3025863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-16.
[5]	"Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization." Emorine L.J., Marullo S., Delavier-Klutchko C., Kaveri S.V., Durieu-Trautmann O., Strosberg A.D. Proc. Natl. Acad. Sci. U.S.A. 84:6995-6999(1987) [PubMed: 2823249] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects." Reihsaus E., Innis M., Macintyre N., Liggett S.B. Am. J. Respir. Cell Mol. Biol. 8:334-339(1993) [PubMed: 8383511] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-27; MET-34 AND ILE-164.
[7]	"Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population." Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W. Ann. Hum. Genet. 64:135-143(2000) [PubMed: 11246467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-159; PHE-159 AND ARG-375. Tissue: Blood.
[8]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-16. Tissue: Heart.
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-27. Tissue: Brain.
[10]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thyroid.
[11]	SeattleSNPs variation discovery resource Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-27 AND CYS-220.
[12]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[13]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-27.
[14]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-16 AND GLU-27. Tissue: Fetal brain, Leukocyte and Prostate.
[15]	"Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation." Chung F.-Z., Wang C.-D., Potter P.C., Venter J.C., Fraser C.M. J. Biol. Chem. 263:4052-4055(1988) [PubMed: 2831218] [Abstract] Cited for: MUTAGENESIS OF ASP-79.
[16]	"Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor." O'Dowd B.F., Hnatowich M., Caron M.G., Lefkowitz R.J., Bouvier M. J. Biol. Chem. 264:7564-7569(1989) [PubMed: 2540197] [Abstract] Cited for: PALMITOYLATION AT CYS-341, MUTAGENESIS OF CYS-341.
[17]	"Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor." Valiquette M., Parent S., Loisel T.P., Bouvier M. EMBO J. 14:5542-5549(1995) [PubMed: 8521811] [Abstract] Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141.
[18]	"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." Gurevich V.V., Dion S.B., Onorato J.J., Ptasienski J., Kim C.M., Sterne-Marr R., Hosey M.M., Benovic J.L. J. Biol. Chem. 270:720-731(1995) [PubMed: 7822302] [Abstract] Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[19]	"Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1." Lin F.-T., Krueger K.M., Kendall H.E., Daaka Y., Fredericks Z.L., Pitcher J.A., Lefkowitz R.J. J. Biol. Chem. 272:31051-31057(1997) [PubMed: 9388255] [Abstract] Cited for: INTERACTION WITH ARRB1.
[20]	"A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor." Cao T.T., Deacon H.W., Reczek D., Bretscher A., von Zastrow M. Nature 401:286-290(1999) [PubMed: 10499588] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[21]	"Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes." 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. Science 283:655-661(1999) [PubMed: 9924018] [Abstract] Cited for: INTERACTION WITH SRC AND ARRB1.
[22]	"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." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed: 11146000] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
[23]	"Modulation of postendocytic sorting of G protein-coupled receptors." Whistler J.L., Enquist J., Marley A., Fong J., Gladher F., Tsuruda P., Murray S.R., Von Zastrow M. Science 297:615-620(2002) [PubMed: 12142540] [Abstract] Cited for: INTERACTION WITH GPRASP1.
[24]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, MASS SPECTROMETRY.
[25]	"The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization." Berthouze M., Venkataramanan V., Li Y., Shenoy S.K. EMBO J. 28:1684-1696(2009) [PubMed: 19424180] [Abstract] Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP20 AND USP33, INTERACTION WITH USP20 AND USP33.
[26]	"Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." 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. Nature 450:383-387(2007) [PubMed: 17952055] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY.
[27]	"High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." 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. Science 318:1258-1265(2007) [PubMed: 17962520] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMYTOYLATION AT CYS-341.
[28]	"A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed: 18547522] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMYTOYLATION AT CYS-341.
[29]	"Amino-terminal polymorphisms of the human beta 2-adrenergic receptor impart distinct agonist-promoted regulatory properties." Green S.A., Turki J., Innis M., Ligget S.B. Biochemistry 33:9414-9419(1994) [PubMed: 7915137] [Abstract] Cited for: VARIANTS ARG-16 AND GLU-27, CHARACTERIZATION.
[30]	"Genetic polymorphisms of the beta 2-adrenergic receptor in nocturnal and nonnocturnal asthma. Evidence that Gly16 correlates with the nocturnal phenotype." Turki J., Pak J., Green S.A., Martin R.J., Liggett S.B. J. Clin. Invest. 95:1635-1641(1995) [PubMed: 7706471] [Abstract] Cited for: VARIANT ARG-16, ASSOCIATION OF GLY-16 WITH NOCTURNAL ASTHMA.
+	Additional computationally mapped references.

Web resources

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04827 mRNA. Translation: CAA28511.1.
Y00106 Genomic DNA. Translation: CAA68289.1.
M15169 mRNA. Translation: AAA88015.1.
J02960 Genomic DNA. Translation: AAA88017.1.
AF022953 Genomic DNA. Translation: AAB82148.1.
AF022954 Genomic DNA. Translation: AAB82149.1.
AF022955 Genomic DNA. Translation: AAB82150.1.
AF022956 Genomic DNA. Translation: AAB82151.1.
AF169225 Genomic DNA. Translation: AAD48036.1.
AF202305 Genomic DNA. Translation: AAF17569.1.
AF203386 Genomic DNA. Translation: AAF20199.1.
AY136741 mRNA. Translation: AAN01267.1.
AK313151 mRNA. Translation: BAG35969.1.
AK223025 mRNA. Translation: BAD96745.1. Different initiation.
DQ094845 Genomic DNA. Translation: AAY88739.1.
EU332834 Genomic DNA. Translation: ABY87523.1.
CH471062 Genomic DNA. Translation: EAW61798.1.
BC012481 mRNA. Translation: AAH12481.3.
BC063486 mRNA. Translation: AAH63486.2.
BC073856 mRNA. Translation: AAH73856.1.

IPI

IPI00465066.

PIR

QRHUB2. A27525.

RefSeq

NP_000015.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2R4R	X-ray	3.40	A	1-365	[»]
2R4S	X-ray	3.40	A	24-365	[»]
2RH1	X-ray	2.40	A	1-365	[»]
3D4S	X-ray	2.80	A	1-365	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P07550. 3 interactions.

STRING

P07550.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P07550.

Genome annotation databases

Ensembl

ENST00000305988; ENSP00000305372; ENSG00000169252; Homo sapiens. [Genome view]

GeneID

154.

KEGG

hsa:154.

UCSC

uc003lpr.1. human.

Organism-specific databases

CTD

154.

GeneCards

GC05P148186.

H-InvDB

HIX0032024.

HGNC

HGNC:286. ADRB2.

HPA

HPA003431.

MIM

109690. gene+phenotype.

PharmGKB

PA39.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14235.

HOVERGEN

P07550.

InParanoid

P07550.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6cyclingpathway. Arf6 signaling events.
arf6_traffickingpathway. Arf6 trafficking events.

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

P07550.

Bgee

P07550.

Genevestigator

P07550.

GermOnline

ENSG00000169252. Homo sapiens.

Family and domain databases

InterPro

IPR000276. 7TM_GPCR_Rhodpsn.
IPR000332. Adrgc_rcpt_B2.
IPR002233. Adrnrgc_rcpt.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]

PANTHER

PTHR19266:SF42. Adrgc_rcpt_B2. 1 hit.

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00866. Alprenolol.
DB01274. Arformoterol.
DB01408. Bambuterol.
DB00612. Bisoprolol.
DB00901. Bitolterol.
DB01158. Bretylium.
DB00521. Carteolol.
DB01136. Carvedilol.
DB01407. Clenbuterol.
DB01151. Desipramine.
DB00668. Epinephrine.
DB01288. Fenoterol.
DB00983. Formoterol.
DB01064. Isoproterenol.
DB00598. Labetalol.
DB01210. Levobunolol.
DB01214. Metipranolol.
DB01203. Nadolol.
DB00368. Norepinephrine.
DB00816. Orciprenaline.
DB01580. Oxprenolol.
DB01359. Penbutolol.
DB00960. Pindolol.
DB01291. Pirbuterol.
DB01366. Procaterol.
DB00571. Propranolol.
DB00852. Pseudoephedrine.
DB00867. Ritodrine.
DB01001. Salbutamol.
DB00938. Salmeterol.
DB00871. Terbutaline.
DB00373. Timolol.

NextBio

613.

SOURCE

Search...

Entry information

Entry name

ADRB2_HUMAN

Accession

Primary (citable) accession number: P07550
Secondary accession number(s): B0LPE4 , B2R7X2, O14823, O14824, O14825, O14826, Q4JG18, Q53GA6, Q6GMT4, Q6P4D8, Q8NEQ9, Q96EC3, Q9UCZ0, Q9UCZ1, Q9UCZ2, Q9UCZ3, Q9UH95, Q9UHA1, Q9UMZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	May 26, 2009
Last modified:	January 19, 2010
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.