test/P07550.xml

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<entry dataset="Swiss-Prot" created="1988-04-01" modified="2025-02-05" version="255" xmlns="http://uniprot.org/uniprot">
  <accession>P07550</accession>
  <accession>B0LPE4</accession>
  <accession>B2R7X2</accession>
  <accession>O14823</accession>
  <accession>O14824</accession>
  <accession>O14825</accession>
  <accession>O14826</accession>
  <accession>Q4JG18</accession>
  <accession>Q53GA6</accession>
  <accession>Q6GMT4</accession>
  <accession>Q6P4D8</accession>
  <accession>Q8NEQ9</accession>
  <accession>Q96EC3</accession>
  <accession>Q9UCZ0</accession>
  <accession>Q9UCZ1</accession>
  <accession>Q9UCZ2</accession>
  <accession>Q9UCZ3</accession>
  <accession>Q9UH95</accession>
  <accession>Q9UHA1</accession>
  <accession>Q9UMZ5</accession>
  <name>ADRB2_HUMAN</name>
  <protein>
    <recommendedName>
      <fullName>Beta-2 adrenergic receptor</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Beta-2 adrenoreceptor</fullName>
      <shortName>Beta-2 adrenoceptor</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ADRB2</name>
    <name type="synonym">ADRB2R</name>
    <name type="synonym">B2AR</name>
  </gene>
  <organism>
    <name type="scientific">Homo sapiens</name>
    <name type="common">Human</name>
    <dbReference type="NCBI Taxonomy" id="9606"/>
    <lineage>
      <taxon>Eukaryota</taxon>
      <taxon>Metazoa</taxon>
      <taxon>Chordata</taxon>
      <taxon>Craniata</taxon>
      <taxon>Vertebrata</taxon>
      <taxon>Euteleostomi</taxon>
      <taxon>Mammalia</taxon>
      <taxon>Eutheria</taxon>
      <taxon>Euarchontoglires</taxon>
      <taxon>Primates</taxon>
      <taxon>Haplorrhini</taxon>
      <taxon>Catarrhini</taxon>
      <taxon>Hominidae</taxon>
      <taxon>Homo</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1987" name="FEBS Lett." volume="211" first="200" last="206">
      <title>Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors.</title>
      <authorList>
        <person name="Chung F.-Z."/>
        <person name="Lentes K.-U."/>
        <person name="Gocayne J.D."/>
        <person name="Fitzgerald M.G."/>
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        <person name="Fraser C.M."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="3026848"/>
      <dbReference type="DOI" id="10.1016/0014-5793(87)81436-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
    <scope>VARIANT GLN-27</scope>
    <source>
      <tissue>Brain</tissue>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1987" name="J. Biol. Chem." volume="262" first="7321" last="7327">
      <title>Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions.</title>
      <authorList>
        <person name="Kobilka B.K."/>
        <person name="Frielle T."/>
        <person name="Dohlman H.G."/>
        <person name="Bolanowski M.A."/>
        <person name="Dixon R.A.F."/>
        <person name="Keller P."/>
        <person name="Caron M.G."/>
        <person name="Lefkowitz R.J."/>
      </authorList>
      <dbReference type="PubMed" id="3034889"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)48239-7"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANTS ARG-16 AND GLN-27</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1987" name="Nucleic Acids Res." volume="15" first="3636" last="3636">
      <title>Primary structure of the human beta-adrenergic receptor gene.</title>
      <authorList>
        <person name="Schofield P.R."/>
        <person name="Rhee L.M."/>
        <person name="Peralta E.G."/>
      </authorList>
      <dbReference type="PubMed" id="3033609"/>
      <dbReference type="DOI" id="10.1093/nar/15.8.3636"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANTS ARG-16 AND GLN-27</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1987" name="Proc. Natl. Acad. Sci. U.S.A." volume="84" first="46" last="50">
      <title>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.</title>
      <authorList>
        <person name="Kobilka B.K."/>
        <person name="Dixon R.A.F."/>
        <person name="Frielle T."/>
        <person name="Dohlman H.G."/>
        <person name="Bolanowski M.A."/>
        <person name="Sigal I.S."/>
        <person name="Yang-Feng T.L."/>
        <person name="Francke U."/>
        <person name="Caron M.G."/>
        <person name="Lefkowitz R.J."/>
      </authorList>
      <dbReference type="PubMed" id="3025863"/>
      <dbReference type="DOI" id="10.1073/pnas.84.1.46"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
    <scope>VARIANTS ARG-16 AND GLN-27</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="1987" name="Proc. Natl. Acad. Sci. U.S.A." volume="84" first="6995" last="6999">
      <title>Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization.</title>
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        <person name="Emorine L.J."/>
        <person name="Marullo S."/>
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      </authorList>
      <dbReference type="PubMed" id="2823249"/>
      <dbReference type="DOI" id="10.1073/pnas.84.20.6995"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANT GLN-27</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="1993" name="Am. J. Respir. Cell Mol. Biol." volume="8" first="334" last="339">
      <title>Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects.</title>
      <authorList>
        <person name="Reihsaus E."/>
        <person name="Innis M."/>
        <person name="Macintyre N."/>
        <person name="Liggett S.B."/>
      </authorList>
      <dbReference type="PubMed" id="8383511"/>
      <dbReference type="DOI" id="10.1165/ajrcmb/8.3.334"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANTS ARG-16; GLN-27; MET-34 AND ILE-164</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2000" name="Ann. Hum. Genet." volume="64" first="135" last="143">
      <title>Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population.</title>
      <authorList>
        <person name="Rupert J.L."/>
        <person name="Monsalve M.V."/>
        <person name="Devine D.V."/>
        <person name="Hochachka P.W."/>
      </authorList>
      <dbReference type="PubMed" id="11246467"/>
      <dbReference type="DOI" id="10.1017/s0003480000008009"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANTS GLN-27; LEU-159; PHE-159 AND ARG-375</scope>
    <source>
      <tissue>Blood</tissue>
    </source>
  </reference>
  <reference key="8">
    <citation type="submission" date="2002-07" db="EMBL/GenBank/DDBJ databases">
      <title>cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).</title>
      <authorList>
        <person name="Puhl H.L. III"/>
        <person name="Ikeda S.R."/>
        <person name="Aronstam R.S."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
    <scope>VARIANTS ARG-16 AND GLN-27</scope>
    <source>
      <tissue>Heart</tissue>
    </source>
  </reference>
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      <title>Complete sequencing and characterization of 21,243 full-length human cDNAs.</title>
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        <person name="Kawakami T."/>
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        <person name="Hata H."/>
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        <person name="Komatsu T."/>
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        <person name="Yamashita R."/>
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        <person name="Sugano S."/>
      </authorList>
      <dbReference type="PubMed" id="14702039"/>
      <dbReference type="DOI" id="10.1038/ng1285"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
    <source>
      <tissue>Brain</tissue>
    </source>
  </reference>
  <reference key="10">
    <citation type="submission" date="2005-04" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Suzuki Y."/>
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    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
    <scope>VARIANT GLN-27</scope>
    <source>
      <tissue>Thyroid</tissue>
    </source>
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    <citation type="submission" date="2005-06" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <consortium name="SeattleSNPs variation discovery resource"/>
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    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANTS GLN-27 AND CYS-220</scope>
  </reference>
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      <authorList>
        <consortium name="NHLBI resequencing and genotyping service (RS&amp;G)"/>
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    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>VARIANT GLN-27</scope>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <authorList>
        <consortium name="The MGC Project Team"/>
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      <dbReference type="DOI" id="10.1101/gr.2596504"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
    <scope>VARIANTS ARG-16 AND GLN-27</scope>
    <source>
      <tissue>Fetal brain</tissue>
      <tissue>Leukocyte</tissue>
      <tissue>Prostate</tissue>
    </source>
  </reference>
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        <person name="Chung F.-Z."/>
        <person name="Wang C.-D."/>
        <person name="Potter P.C."/>
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    <scope>MUTAGENESIS OF ASP-79</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="16">
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        <person name="O'Dowd B.F."/>
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        <person name="Caron M.G."/>
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      <dbReference type="PubMed" id="2540197"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)83271-9"/>
    </citation>
    <scope>PALMITOYLATION AT CYS-341</scope>
    <scope>MUTAGENESIS OF CYS-341</scope>
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      <authorList>
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    </citation>
    <scope>MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366</scope>
    <scope>PHOSPHORYLATION AT TYR-141</scope>
  </reference>
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      </authorList>
      <dbReference type="PubMed" id="7822302"/>
      <dbReference type="DOI" id="10.1074/jbc.270.2.720"/>
    </citation>
    <scope>INTERACTION WITH ARRB1 AND ARRB2</scope>
  </reference>
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      <title>Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1.</title>
      <authorList>
        <person name="Lin F.-T."/>
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      </authorList>
      <dbReference type="PubMed" id="9388255"/>
      <dbReference type="DOI" id="10.1074/jbc.272.49.31051"/>
    </citation>
    <scope>INTERACTION WITH ARRB1</scope>
  </reference>
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      <title>A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor.</title>
      <authorList>
        <person name="Cao T.T."/>
        <person name="Deacon H.W."/>
        <person name="Reczek D."/>
        <person name="Bretscher A."/>
        <person name="von Zastrow M."/>
      </authorList>
      <dbReference type="PubMed" id="10499588"/>
      <dbReference type="DOI" id="10.1038/45816"/>
    </citation>
    <scope>INTERACTION WITH NHERF1</scope>
  </reference>
  <reference key="21">
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      <title>Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes.</title>
      <authorList>
        <person name="Luttrell L.M."/>
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        <person name="Miller W.E."/>
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        <person name="Lin F.-T."/>
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      </authorList>
      <dbReference type="PubMed" id="9924018"/>
      <dbReference type="DOI" id="10.1126/science.283.5402.655"/>
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    <scope>INTERACTION WITH SRC AND ARRB1</scope>
  </reference>
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        <person name="Rousseau G."/>
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      </authorList>
      <dbReference type="PubMed" id="11146000"/>
      <dbReference type="DOI" id="10.1046/j.1471-4159.2001.00005.x"/>
    </citation>
    <scope>EFFECT OF PALMITOYLATION</scope>
    <scope>PHOSPHORYLATION AT SER-345 AND SER-346</scope>
    <scope>MUTAGENESIS OF 345-SER-SER-346</scope>
  </reference>
  <reference key="23">
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      <authorList>
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        <person name="Marley A."/>
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        <person name="Gladher F."/>
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        <person name="Von Zastrow M."/>
      </authorList>
      <dbReference type="PubMed" id="12142540"/>
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    </citation>
    <scope>INTERACTION WITH GPRASP1</scope>
  </reference>
  <reference key="24">
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      <authorList>
        <person name="Matsuoka S."/>
        <person name="Ballif B.A."/>
        <person name="Smogorzewska A."/>
        <person name="McDonald E.R. III"/>
        <person name="Hurov K.E."/>
        <person name="Luo J."/>
        <person name="Bakalarski C.E."/>
        <person name="Zhao Z."/>
        <person name="Solimini N."/>
        <person name="Lerenthal Y."/>
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        <person name="Gygi S.P."/>
        <person name="Elledge S.J."/>
      </authorList>
      <dbReference type="PubMed" id="17525332"/>
      <dbReference type="DOI" id="10.1126/science.1140321"/>
    </citation>
    <scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
    <source>
      <tissue>Embryonic kidney</tissue>
    </source>
  </reference>
  <reference key="25">
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      <title>The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization.</title>
      <authorList>
        <person name="Berthouze M."/>
        <person name="Venkataramanan V."/>
        <person name="Li Y."/>
        <person name="Shenoy S.K."/>
      </authorList>
      <dbReference type="PubMed" id="19424180"/>
      <dbReference type="DOI" id="10.1038/emboj.2009.128"/>
    </citation>
    <scope>UBIQUITINATION</scope>
    <scope>DEUBIQUITINATION BY USP20 AND USP33</scope>
    <scope>INTERACTION WITH USP20 AND USP33</scope>
  </reference>
  <reference key="26">
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      <authorList>
        <person name="Xie L."/>
        <person name="Xiao K."/>
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        <person name="Forrester M.T."/>
        <person name="Freeman R.S."/>
        <person name="Fong G."/>
        <person name="Gygi S.P."/>
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        <person name="Stamler J.S."/>
      </authorList>
      <dbReference type="PubMed" id="19584355"/>
      <dbReference type="DOI" id="10.1126/scisignal.2000444"/>
    </citation>
    <scope>INTERACTION WITH EGLN3 AND VHL</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>UBIQUITINATION</scope>
    <scope>HYDROXYLATION AT PRO-382 AND PRO-395</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
  </reference>
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      <authorList>
        <person name="Nabhan J.F."/>
        <person name="Pan H."/>
        <person name="Lu Q."/>
      </authorList>
      <dbReference type="PubMed" id="20559325"/>
      <dbReference type="DOI" id="10.1038/embor.2010.80"/>
    </citation>
    <scope>UBIQUITINATION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INTERACTION WITH ARRDC3</scope>
  </reference>
  <reference key="28">
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        <person name="Lauffer B.E."/>
        <person name="Melero C."/>
        <person name="Temkin P."/>
        <person name="Lei C."/>
        <person name="Hong W."/>
        <person name="Kortemme T."/>
        <person name="von Zastrow M."/>
      </authorList>
      <dbReference type="PubMed" id="20733053"/>
      <dbReference type="DOI" id="10.1083/jcb.201004060"/>
    </citation>
    <scope>INTERACTION WITH SNX27</scope>
  </reference>
  <reference key="29">
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      <title>SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors.</title>
      <authorList>
        <person name="Temkin P."/>
        <person name="Lauffer B."/>
        <person name="Jager S."/>
        <person name="Cimermancic P."/>
        <person name="Krogan N.J."/>
        <person name="von Zastrow M."/>
      </authorList>
      <dbReference type="PubMed" id="21602791"/>
      <dbReference type="DOI" id="10.1038/ncb2252"/>
    </citation>
    <scope>INTERACTION WITH SNX27</scope>
  </reference>
  <reference key="30">
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      <title>MARCH2 promotes endocytosis and lysosomal sorting of carvedilol-bound beta(2)-adrenergic receptors.</title>
      <authorList>
        <person name="Han S.O."/>
        <person name="Xiao K."/>
        <person name="Kim J."/>
        <person name="Wu J.H."/>
        <person name="Wisler J.W."/>
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        <person name="Shenoy S.K."/>
      </authorList>
      <dbReference type="PubMed" id="23166351"/>
      <dbReference type="DOI" id="10.1083/jcb.201208192"/>
    </citation>
    <scope>INTERACTION WITH MARCHF2; NEDD4; USP20 AND USP33</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>UBIQUITINATION</scope>
  </reference>
  <reference key="31">
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        <person name="Qi S."/>
        <person name="O'Hayre M."/>
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        <person name="Hurley J.H."/>
      </authorList>
      <dbReference type="PubMed" id="25220262"/>
      <dbReference type="DOI" id="10.1002/pro.2549"/>
    </citation>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INTERACTION WITH ARRDC3</scope>
  </reference>
  <reference key="32">
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      <title>CNIH4 interacts with newly synthesized GPCR and controls their export from the endoplasmic reticulum.</title>
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        <person name="Sauvageau E."/>
        <person name="Rochdi M.D."/>
        <person name="Oueslati M."/>
        <person name="Hamdan F.F."/>
        <person name="Percherancier Y."/>
        <person name="Simpson J.C."/>
        <person name="Pepperkok R."/>
        <person name="Bouvier M."/>
      </authorList>
      <dbReference type="PubMed" id="24405750"/>
      <dbReference type="DOI" id="10.1111/tra.12148"/>
    </citation>
    <scope>INTERACTION WITH CNIH4</scope>
  </reference>
  <reference key="33">
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      <title>S-Palmitoylation of a Novel Site in the beta2-Adrenergic Receptor Associated with a Novel Intracellular Itinerary.</title>
      <authorList>
        <person name="Adachi N."/>
        <person name="Hess D.T."/>
        <person name="McLaughlin P."/>
        <person name="Stamler J.S."/>
      </authorList>
      <dbReference type="PubMed" id="27481942"/>
      <dbReference type="DOI" id="10.1074/jbc.m116.725762"/>
    </citation>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>PALMITOYLATION AT CYS-265 AND CYS-341</scope>
    <scope>MUTAGENESIS OF CYS-265 AND CYS-341</scope>
  </reference>
  <reference evidence="40 41" key="34">
    <citation type="journal article" date="2007" name="Nature" volume="450" first="383" last="387">
      <title>Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.</title>
      <authorList>
        <person name="Rasmussen S.G.F."/>
        <person name="Choi H.-J."/>
        <person name="Rosenbaum D.M."/>
        <person name="Kobilka T.S."/>
        <person name="Thian F.S."/>
        <person name="Edwards P.C."/>
        <person name="Burghammer M."/>
        <person name="Ratnala V.R.P."/>
        <person name="Sanishvili R."/>
        <person name="Fischetti R.F."/>
        <person name="Schertler G.F.X."/>
        <person name="Weis W.I."/>
        <person name="Kobilka B.K."/>
      </authorList>
      <dbReference type="PubMed" id="17952055"/>
      <dbReference type="DOI" id="10.1038/nature06325"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL</scope>
    <scope>TOPOLOGY</scope>
  </reference>
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      <authorList>
        <person name="Cherezov V."/>
        <person name="Rosenbaum D.M."/>
        <person name="Hanson M.A."/>
        <person name="Rasmussen S.G.F."/>
        <person name="Thian F.S."/>
        <person name="Kobilka T.S."/>
        <person name="Choi H.-J."/>
        <person name="Kuhn P."/>
        <person name="Weis W.I."/>
        <person name="Kobilka B.K."/>
        <person name="Stevens R.C."/>
      </authorList>
      <dbReference type="PubMed" id="17962520"/>
      <dbReference type="DOI" id="10.1126/science.1150577"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL</scope>
    <scope>DISULFIDE BONDS</scope>
    <scope>TOPOLOGY</scope>
    <scope>PALMITOYLATION AT CYS-341</scope>
  </reference>
  <reference evidence="43" key="36">
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      <title>A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor.</title>
      <authorList>
        <person name="Hanson M.A."/>
        <person name="Cherezov V."/>
        <person name="Griffith M.T."/>
        <person name="Roth C.B."/>
        <person name="Jaakola V.P."/>
        <person name="Chien E.Y."/>
        <person name="Velasquez J."/>
        <person name="Kuhn P."/>
        <person name="Stevens R.C."/>
      </authorList>
      <dbReference type="PubMed" id="18547522"/>
      <dbReference type="DOI" id="10.1016/j.str.2008.05.001"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL</scope>
    <scope>DISULFIDE BONDS</scope>
    <scope>TOPOLOGY</scope>
    <scope>PALMITOYLATION AT CYS-341</scope>
  </reference>
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      <title>Amino-terminal polymorphisms of the human beta 2-adrenergic receptor impart distinct agonist-promoted regulatory properties.</title>
      <authorList>
        <person name="Green S.A."/>
        <person name="Turki J."/>
        <person name="Innis M."/>
        <person name="Ligget S.B."/>
      </authorList>
      <dbReference type="PubMed" id="7915137"/>
      <dbReference type="DOI" id="10.1021/bi00198a006"/>
    </citation>
    <scope>VARIANTS ARG-16 AND GLN-27</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="38">
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      <authorList>
        <person name="Turki J."/>
        <person name="Pak J."/>
        <person name="Green S.A."/>
        <person name="Martin R.J."/>
        <person name="Liggett S.B."/>
      </authorList>
      <dbReference type="PubMed" id="7706471"/>
      <dbReference type="DOI" id="10.1172/jci117838"/>
    </citation>
    <scope>VARIANT ARG-16</scope>
    <scope>POLYMORPHISM</scope>
  </reference>
  <comment type="function">
    <text evidence="23 30">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.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4 7 9 10 11 12 13 14 15 16 17 18 19 29 33 34">Binds NHERF1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC (PubMed:9924018). Interacts with USP20 and USP33 (PubMed:19424180, PubMed:23166351). 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). Interacts with NEDD4 (PubMed:23166351). Interacts with MARCHF2 (PubMed:23166351).</text>
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      <label>PARP11</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-491169">
      <id>P07550</id>
    </interactant>
    <interactant intactId="EBI-749039">
      <id>Q8WVD3</id>
      <label>RNF138</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-491169">
      <id>P07550</id>
    </interactant>
    <interactant intactId="EBI-751555">
      <id>Q9H0X6</id>
      <label>RNF208</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-491169">
      <id>P07550</id>
    </interactant>
    <interactant intactId="EBI-632715">
      <id>Q13573</id>
      <label>SNW1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-491169">
      <id>P07550</id>
    </interactant>
    <interactant intactId="EBI-621482">
      <id>P12931</id>
      <label>SRC</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-491169">
      <id>P07550</id>
    </interactant>
    <interactant intactId="EBI-12833746">
      <id>Q5T0J7-2</id>
      <label>TEX35</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-491169">
      <id>P07550</id>
    </interactant>
    <interactant intactId="EBI-25830583">
      <id>Q8N0U2</id>
      <label>TMEM61</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="13 14 17 19 23 30">Cell membrane</location>
      <topology evidence="13">Multi-pass membrane protein</topology>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="14">Early endosome</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="21">Golgi apparatus</location>
    </subcellularLocation>
    <text evidence="13 14 21">Colocalizes with VHL at the cell membrane (PubMed:19584355). Activated receptors are internalized into endosomes prior to their degradation in lysosomes (PubMed:20559325). Activated receptors are also detected within the Golgi apparatus (PubMed:27481942).</text>
  </comment>
  <comment type="PTM">
    <text evidence="5 10 11 20 21">Palmitoylated (PubMed:11146000, PubMed:17962520, PubMed:18547522, PubMed:2540197, PubMed:27481942). Mainly palmitoylated at Cys-341 (PubMed:17962520, PubMed:18547522, PubMed:2540197). Palmitoylation may reduce accessibility of phosphorylation sites by anchoring the receptor to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (PubMed:11146000). Also undergoes transient, ligand-induced palmitoylation at Cys-265 probably by ZDHHC9, ZDHHC14 and ZDHHC18 within the Golgi (PubMed:27481942). Palmitoylation at Cys-265 requires phosphorylation by PKA and receptor internalization and stabilizes the receptor (PubMed:27481942). Could be depalmitoylated by LYPLA1 at the plasma membrane (PubMed:27481942).</text>
  </comment>
  <comment type="PTM">
    <text>Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.</text>
  </comment>
  <comment type="PTM">
    <text evidence="32">Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor.</text>
  </comment>
  <comment type="PTM">
    <text evidence="12 14 17">Polyubiquitinated (PubMed:23166351). Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation (PubMed:19424180, PubMed:20559325, PubMed:23166351). 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.</text>
  </comment>
  <comment type="PTM">
    <text evidence="12 13">Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2.</text>
  </comment>
  <comment type="polymorphism">
    <text>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.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="39">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAD96745" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
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  <feature type="mutagenesis site" description="Uncoupled receptor." evidence="20">
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  <feature type="mutagenesis site" description="Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization." evidence="32">
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</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>