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P07550 (ADRB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-2 adrenergic receptor
Alternative name(s):
Beta-2 adrenoreceptor
Short name=Beta-2 adrenoceptor
Gene names
Name:ADRB2
Synonyms:ADRB2R, B2AR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Colocalizes with VHL at the cell membrane. Ref.26

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 Ref.30 Ref.31

Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK. Ref.17 Ref.22

Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor.

Polyubiquitinated. 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. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent.

Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2.

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. Adrenergic receptor subfamily. ADRB2 sub-subfamily.

Sequence caution

The sequence BAD96745.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of adenylate cyclase activity

Inferred from direct assay PubMed 15123695. Source: HGNC

activation of transmembrane receptor protein tyrosine kinase activity

Traceable author statement PubMed 10734107. Source: ProtInc

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement Ref.5. Source: ProtInc

adrenergic receptor signaling pathway

Inferred from direct assay PubMed 15123695. Source: GOC

bone resorption

Inferred from electronic annotation. Source: Ensembl

brown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 1371121. Source: ProtInc

desensitization of G-protein coupled receptor protein signaling pathway by arrestin

Inferred from direct assay PubMed 15123695. Source: HGNC

diet induced thermogenesis

Inferred from electronic annotation. Source: Ensembl

endosome to lysosome transport

Traceable author statement PubMed 9507004. Source: ProtInc

heat generation

Inferred from electronic annotation. Source: Ensembl

negative regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from direct assay PubMed 15123695. Source: HGNC

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination

Inferred from mutant phenotype PubMed 19372219. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from direct assay PubMed 15123695. Source: HGNC

regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of vasodilation

Inferred from electronic annotation. Source: InterPro

response to cold

Inferred from electronic annotation. Source: Ensembl

vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

endosome

Traceable author statement PubMed 10734107. Source: ProtInc

integral component of plasma membrane

Inferred from direct assay PubMed 12297500. Source: BHF-UCL

lysosome

Traceable author statement PubMed 9507004. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 9235896. Source: MGI

receptor complex

Inferred from direct assay PubMed 15123695. Source: HGNC

   Molecular_functionbeta2-adrenergic receptor activity

Inferred from direct assay PubMed 15123695. Source: HGNC

norepinephrine binding

Inferred from direct assay PubMed 15123695. Source: HGNC

potassium channel regulator activity

Inferred from direct assay PubMed 12297500. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.25Ref.26Ref.27PubMed 9560162. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 15123695. Source: HGNC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Beta-2 adrenergic receptor
PRO_0000069130

Regions

Topological domain1 – 3434Extracellular Ref.29 Ref.30 Ref.31
Transmembrane35 – 5824Helical; Name=1
Topological domain59 – 7113Cytoplasmic Ref.29 Ref.30 Ref.31
Transmembrane72 – 9524Helical; Name=2
Topological domain96 – 10611Extracellular Ref.29 Ref.30 Ref.31
Transmembrane107 – 12923Helical; Name=3
Topological domain130 – 15021Cytoplasmic Ref.29 Ref.30 Ref.31
Transmembrane151 – 17424Helical; Name=4
Topological domain175 – 19622Extracellular Ref.29 Ref.30 Ref.31
Transmembrane197 – 22024Helical; Name=5
Topological domain221 – 27454Cytoplasmic Ref.29 Ref.30 Ref.31
Transmembrane275 – 29824Helical; Name=6
Topological domain299 – 3057Extracellular Ref.29 Ref.30 Ref.31
Transmembrane306 – 32924Helical; Name=7
Topological domain330 – 41384Cytoplasmic Ref.29 Ref.30 Ref.31
Region193 – 20715Agonist and antagonist binding
Region286 – 2938Agonist and antagonist binding
Region312 – 3165Agonist and antagonist binding
Motif410 – 4134PDZ-binding

Sites

Binding site1131Agonist or antagonist
Binding site1181Agonist or antagonist

Amino acid modifications

Modified residue1411Phosphotyrosine Ref.17
Modified residue2461Phosphoserine Ref.24
Modified residue2611Phosphoserine; by PKA Potential
Modified residue2621Phosphoserine; by PKA Potential
Modified residue3451Phosphoserine; by PKA Ref.22
Modified residue3461Phosphoserine; by PKA Ref.22
Modified residue3551Phosphoserine; by BARK Probable
Modified residue3561Phosphoserine; by BARK Probable
Modified residue38214-hydroxyproline Ref.26
Modified residue39514-hydroxyproline Ref.26
Lipidation3411S-palmitoyl cysteine Ref.16 Ref.22 Ref.30 Ref.31
Glycosylation61N-linked (GlcNAc...) Probable
Glycosylation151N-linked (GlcNAc...) Probable
Disulfide bond106 ↔ 191 Ref.30 Ref.31
Disulfide bond184 ↔ 190 Ref.30 Ref.31

Natural variations

Natural variant151N → S.
Corresponds to variant rs33973603 [ dbSNP | Ensembl ].
VAR_049373
Natural variant161G → R Common polymorphism. Ref.2 Ref.3 Ref.4 Ref.6 Ref.8 Ref.14 Ref.32 Ref.33
Corresponds to variant rs1042713 [ dbSNP | Ensembl ].
VAR_003452
Natural variant271E → Q. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.32
Corresponds to variant rs1042714 [ dbSNP | Ensembl ].
VAR_003453
Natural variant341V → M. Ref.6
VAR_003454
Natural variant1591I → F. Ref.7
VAR_009125
Natural variant1591I → L. Ref.7
VAR_009124
Natural variant1641T → I. Ref.6
Corresponds to variant rs1800888 [ dbSNP | Ensembl ].
VAR_003455
Natural variant2201S → C. Ref.11
Corresponds to variant rs3729943 [ dbSNP | Ensembl ].
VAR_025101
Natural variant3751K → R. Ref.7
VAR_009394

Experimental info

Mutagenesis791D → N: Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins. Ref.15 Ref.22
Mutagenesis1411Y → F: Abolishes insulin-induced tyrosine phosphorylation and insulin-induced receptor supersensitization. Ref.17 Ref.22
Mutagenesis3411C → G: Uncoupled receptor. Ref.16 Ref.22
Mutagenesis345 – 3462SS → AA: Delayed agonist-promoted desensitization. Ref.22
Mutagenesis3501Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. Ref.17 Ref.22
Mutagenesis3541Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. Ref.17 Ref.22
Mutagenesis3661Y → F: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. Ref.17 Ref.22
Sequence conflict711F → L in BAG35969. Ref.9
Sequence conflict2161V → A in AAN01267. Ref.8
Sequence conflict2611S → P in BAD96745. Ref.10
Sequence conflict4021Q → P in AAH12481. Ref.14

Secondary structure

......................................... 413
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07550 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 408C22731C6EDFBE

FASTA41346,459
        10         20         30         40         50         60 
MGQPGNGSAF LLAPNGSHAP DHDVTQERDE 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 SQGRNCSTND SLL 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-27.
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-16 AND GLN-27.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-27.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLN-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27; 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], VARIANTS ARG-16 AND GLN-27.
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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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], VARIANT GLN-27.
Tissue: Thyroid.
[11]SeattleSNPs variation discovery resource
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-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], VARIANT GLN-27.
[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. expand/collapse author list , 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].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-16 AND GLN-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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[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] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP20 AND USP33, INTERACTION WITH USP20 AND USP33.
[26]"Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL."
Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., Gygi S.P., Lefkowitz R.J., Stamler J.S.
Sci. Signal. 2:RA33-RA33(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGLN3 AND VHL, SUBCELLULAR LOCATION, INDUCTION, UBIQUITINATION, HYDROXYLATION AT PRO-382 AND PRO-395, IDENTIFICATION BY MASS SPECTROMETRY.
[27]"SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane."
Lauffer B.E., Melero C., Temkin P., Lei C., Hong W., Kortemme T., von Zastrow M.
J. Cell Biol. 190:565-574(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
[28]"SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors."
Temkin P., Lauffer B., Jager S., Cimermancic P., Krogan N.J., von Zastrow M.
Nat. Cell Biol. 13:715-721(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY.
[30]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
[31]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
[32]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-16 AND GLN-27, CHARACTERIZATION.
[33]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-16, POLYMORPHISM.
+Additional computationally mapped references.

Web resources

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.
CCDSCCDS4292.1.
PIRQRHUB2. A27525.
RefSeqNP_000015.1. NM_000024.5.
UniGeneHs.2551.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQ4X-ray1.90A409-413[»]
2R4RX-ray3.40A1-365[»]
2R4SX-ray3.40A24-365[»]
2RH1X-ray2.40A1-230[»]
A263-365[»]
3D4SX-ray2.80A1-230[»]
A263-348[»]
3KJ6X-ray3.40A2-365[»]
3NY8X-ray2.84A1-230[»]
A263-348[»]
3NY9X-ray2.84A1-230[»]
A263-348[»]
3NYAX-ray3.16A1-230[»]
A263-348[»]
3P0GX-ray3.50A1-230[»]
A263-365[»]
3PDSX-ray3.50A25-230[»]
A264-348[»]
3SN6X-ray3.20R29-365[»]
4GBRX-ray3.99A29-365[»]
4LDEX-ray2.79A29-348[»]
4LDLX-ray3.10A29-348[»]
4LDOX-ray3.20A29-348[»]
ProteinModelPortalP07550.
SMRP07550. Positions 29-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106663. 186 interactions.
DIPDIP-33948N.
IntActP07550. 11 interactions.
MINTMINT-148142.

Chemistry

BindingDBP07550.
ChEMBLCHEMBL2096974.
DrugBankDB00866. 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.
GuidetoPHARMACOLOGY29.

Protein family/group databases

TCDB9.A.14.3.5. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP07550.

Polymorphism databases

DMDM296439450.

Proteomic databases

MaxQBP07550.
PaxDbP07550.
PRIDEP07550.

Protocols and materials databases

DNASU154.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305988; ENSP00000305372; ENSG00000169252.
GeneID154.
KEGGhsa:154.
UCSCuc003lpr.2. human.

Organism-specific databases

CTD154.
GeneCardsGC05P148186.
HGNCHGNC:286. ADRB2.
HPAHPA003431.
MIM109690. gene+phenotype.
neXtProtNX_P07550.
PharmGKBPA39.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262978.
HOVERGENHBG106962.
InParanoidP07550.
KOK04142.
OMARVFQVAK.
OrthoDBEOG7BS4BS.
PhylomeDBP07550.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP07550.

Gene expression databases

ArrayExpressP07550.
BgeeP07550.
GenevestigatorP07550.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24248:SF21. PTHR24248:SF21. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07550.
GeneWikiBeta-2_adrenergic_receptor.
GenomeRNAi154.
NextBio613.
PROP07550.
SOURCESearch...

Entry information

Entry nameADRB2_HUMAN
AccessionPrimary (citable) accession number: P07550
Secondary accession number(s): B0LPE4 expand/collapse secondary AC list , 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 18, 2010
Last modified: July 9, 2014
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries