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P07550

- ADRB2_HUMAN

UniProt

P07550 - ADRB2_HUMAN

Protein

Beta-2 adrenergic receptor

Gene

ADRB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei113 – 1131Agonist or antagonist
    Binding sitei118 – 1181Agonist or antagonist

    GO - Molecular functioni

    1. beta2-adrenergic receptor activity Source: HGNC
    2. norepinephrine binding Source: HGNC
    3. potassium channel regulator activity Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: HGNC

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: HGNC
    2. activation of transmembrane receptor protein tyrosine kinase activity Source: ProtInc
    3. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
    4. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: ProtInc
    5. adrenergic receptor signaling pathway Source: GOC
    6. bone resorption Source: Ensembl
    7. brown fat cell differentiation Source: Ensembl
    8. cell surface receptor signaling pathway Source: ProtInc
    9. desensitization of G-protein coupled receptor protein signaling pathway by arrestin Source: HGNC
    10. diet induced thermogenesis Source: Ensembl
    11. endosome to lysosome transport Source: ProtInc
    12. heat generation Source: Ensembl
    13. negative regulation of multicellular organism growth Source: Ensembl
    14. negative regulation of smooth muscle contraction Source: Ensembl
    15. positive regulation of bone mineralization Source: Ensembl
    16. positive regulation of MAPK cascade Source: HGNC
    17. positive regulation of protein ubiquitination Source: BHF-UCL
    18. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    19. receptor-mediated endocytosis Source: HGNC
    20. regulation of sodium ion transport Source: Ensembl
    21. regulation of vasodilation Source: InterPro
    22. response to cold Source: Ensembl
    23. vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_16927. Adrenoceptors.
    REACT_19327. G alpha (s) signalling events.
    SignaLinkiP07550.

    Protein family/group databases

    TCDBi9.A.14.3.5. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-2 adrenergic receptor
    Alternative name(s):
    Beta-2 adrenoreceptor
    Short name:
    Beta-2 adrenoceptor
    Gene namesi
    Name:ADRB2
    Synonyms:ADRB2R, B2AR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:286. ADRB2.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Colocalizes with VHL at the cell membrane.

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. endosome Source: ProtInc
    3. integral component of plasma membrane Source: BHF-UCL
    4. lysosome Source: ProtInc
    5. nucleus Source: Ensembl
    6. plasma membrane Source: MGI
    7. receptor complex Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791D → N: Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins. 2 Publications
    Mutagenesisi141 – 1411Y → F: Abolishes insulin-induced tyrosine phosphorylation and insulin-induced receptor supersensitization. 2 Publications
    Mutagenesisi341 – 3411C → G: Uncoupled receptor. 2 Publications
    Mutagenesisi345 – 3462SS → AA: Delayed agonist-promoted desensitization. 1 Publication
    Mutagenesisi350 – 3501Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 2 Publications
    Mutagenesisi354 – 3541Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 2 Publications
    Mutagenesisi366 – 3661Y → F: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 2 Publications

    Organism-specific databases

    MIMi109690. gene+phenotype.
    PharmGKBiPA39.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 413413Beta-2 adrenergic receptorPRO_0000069130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi6 – 61N-linked (GlcNAc...)Curated
    Glycosylationi15 – 151N-linked (GlcNAc...)Curated
    Disulfide bondi106 ↔ 191
    Modified residuei141 – 1411Phosphotyrosine1 Publication
    Disulfide bondi184 ↔ 190
    Modified residuei246 – 2461Phosphoserine1 Publication
    Modified residuei261 – 2611Phosphoserine; by PKASequence Analysis
    Modified residuei262 – 2621Phosphoserine; by PKASequence Analysis
    Lipidationi341 – 3411S-palmitoyl cysteine3 Publications
    Modified residuei345 – 3451Phosphoserine; by PKA1 Publication
    Modified residuei346 – 3461Phosphoserine; by PKA1 Publication
    Modified residuei355 – 3551Phosphoserine; by BARKCurated
    Modified residuei356 – 3561Phosphoserine; by BARKCurated
    Modified residuei382 – 38214-hydroxyproline1 Publication
    Modified residuei395 – 39514-hydroxyproline1 Publication

    Post-translational modificationi

    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.4 Publications
    Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.
    Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor.1 Publication
    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.1 Publication
    Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP07550.
    PaxDbiP07550.
    PRIDEiP07550.

    PTM databases

    PhosphoSiteiP07550.

    Expressioni

    Gene expression databases

    ArrayExpressiP07550.
    BgeeiP07550.
    GenevestigatoriP07550.

    Organism-specific databases

    HPAiHPA003431.

    Interactioni

    Subunit structurei

    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.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAGI3Q5TCQ99EBI-491169,EBI-310506
    SLC9A3R1O147456EBI-491169,EBI-349787
    SRCP129313EBI-491169,EBI-621482

    Protein-protein interaction databases

    BioGridi106663. 237 interactions.
    DIPiDIP-33948N.
    IntActiP07550. 12 interactions.
    MINTiMINT-148142.

    Structurei

    Secondary structure

    1
    413
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 273
    Helixi31 – 6030
    Helixi62 – 643
    Helixi67 – 8519
    Helixi87 – 9610
    Helixi102 – 13635
    Beta strandi137 – 1393
    Helixi147 – 17024
    Turni171 – 1744
    Helixi179 – 1868
    Beta strandi187 – 1893
    Helixi197 – 20711
    Helixi209 – 22921
    Turni235 – 2395
    Turni263 – 2653
    Helixi267 – 29832
    Beta strandi299 – 3035
    Helixi305 – 31713
    Helixi318 – 3203
    Helixi322 – 3254
    Helixi326 – 3283
    Helixi330 – 33910
    Turni345 – 3473

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP07550.
    SMRiP07550. Positions 29-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07550.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3434ExtracellularAdd
    BLAST
    Topological domaini59 – 7113CytoplasmicAdd
    BLAST
    Topological domaini96 – 10611ExtracellularAdd
    BLAST
    Topological domaini130 – 15021CytoplasmicAdd
    BLAST
    Topological domaini175 – 19622ExtracellularAdd
    BLAST
    Topological domaini221 – 27454CytoplasmicAdd
    BLAST
    Topological domaini299 – 3057Extracellular
    Topological domaini330 – 41384CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei35 – 5824Helical; Name=1Add
    BLAST
    Transmembranei72 – 9524Helical; Name=2Add
    BLAST
    Transmembranei107 – 12923Helical; Name=3Add
    BLAST
    Transmembranei151 – 17424Helical; Name=4Add
    BLAST
    Transmembranei197 – 22024Helical; Name=5Add
    BLAST
    Transmembranei275 – 29824Helical; Name=6Add
    BLAST
    Transmembranei306 – 32924Helical; Name=7Add
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni193 – 20715Agonist and antagonist bindingAdd
    BLAST
    Regioni286 – 2938Agonist and antagonist binding
    Regioni312 – 3165Agonist and antagonist binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi410 – 4134PDZ-binding

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262978.
    HOVERGENiHBG106962.
    InParanoidiP07550.
    KOiK04142.
    OMAiRVFQVAK.
    OrthoDBiEOG7BS4BS.
    PhylomeDBiP07550.
    TreeFamiTF316350.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR002233. ADR_fam.
    IPR000332. ADRB2_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24248:SF21. PTHR24248:SF21. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR01103. ADRENERGICR.
    PR00562. ADRENRGCB2AR.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07550-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQPGNGSAF LLAPNGSHAP DHDVTQERDE VWVVGMGIVM SLIVLAIVFG    50
    NVLVITAIAK FERLQTVTNY FITSLACADL VMGLAVVPFG AAHILMKMWT 100
    FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYFAITSPFK YQSLLTKNKA 150
    RVIILMVWIV SGLTSFLPIQ MHWYRATHQE AINCYANETC CDFFTNQAYA 200
    IASSIVSFYV PLVIMVFVYS RVFQEAKRQL QKIDKSEGRF HVQNLSQVEQ 250
    DGRTGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD 300
    NLIRKEVYIL LNWIGYVNSG FNPLIYCRSP DFRIAFQELL CLRRSSLKAY 350
    GNGYSSNGNT GEQSGYHVEQ EKENKLLCED LPGTEDFVGH QGTVPSDNID 400
    SQGRNCSTND SLL 413
    Length:413
    Mass (Da):46,459
    Last modified:May 18, 2010 - v3
    Checksum:i408C22731C6EDFBE
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711F → L in BAG35969. (PubMed:14702039)Curated
    Sequence conflicti216 – 2161V → A in AAN01267. 1 PublicationCurated
    Sequence conflicti261 – 2611S → P in BAD96745. 1 PublicationCurated
    Sequence conflicti402 – 4021Q → P in AAH12481. (PubMed:15489334)Curated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151N → S.
    Corresponds to variant rs33973603 [ dbSNP | Ensembl ].
    VAR_049373
    Natural varianti16 – 161G → R Common polymorphism. 8 Publications
    Corresponds to variant rs1042713 [ dbSNP | Ensembl ].
    VAR_003452
    Natural varianti27 – 271E → Q.13 Publications
    Corresponds to variant rs1042714 [ dbSNP | Ensembl ].
    VAR_003453
    Natural varianti34 – 341V → M.1 Publication
    VAR_003454
    Natural varianti159 – 1591I → F.1 Publication
    VAR_009125
    Natural varianti159 – 1591I → L.1 Publication
    VAR_009124
    Natural varianti164 – 1641T → I.1 Publication
    Corresponds to variant rs1800888 [ dbSNP | Ensembl ].
    VAR_003455
    Natural varianti220 – 2201S → C.1 Publication
    Corresponds to variant rs3729943 [ dbSNP | Ensembl ].
    VAR_025101
    Natural varianti375 – 3751K → R.1 Publication
    VAR_009394

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4292.1.
    PIRiA27525. QRHUB2.
    RefSeqiNP_000015.1. NM_000024.5.
    UniGeneiHs.2551.

    Genome annotation databases

    EnsembliENST00000305988; ENSP00000305372; ENSG00000169252.
    GeneIDi154.
    KEGGihsa:154.
    UCSCiuc003lpr.2. human.

    Polymorphism databases

    DMDMi296439450.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4292.1.
    PIRi A27525. QRHUB2.
    RefSeqi NP_000015.1. NM_000024.5.
    UniGenei Hs.2551.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GQ4 X-ray 1.90 A 409-413 [» ]
    2R4R X-ray 3.40 A 1-365 [» ]
    2R4S X-ray 3.40 A 24-365 [» ]
    2RH1 X-ray 2.40 A 1-230 [» ]
    A 263-365 [» ]
    3D4S X-ray 2.80 A 1-230 [» ]
    A 263-348 [» ]
    3KJ6 X-ray 3.40 A 2-365 [» ]
    3NY8 X-ray 2.84 A 1-230 [» ]
    A 263-348 [» ]
    3NY9 X-ray 2.84 A 1-230 [» ]
    A 263-348 [» ]
    3NYA X-ray 3.16 A 1-230 [» ]
    A 263-348 [» ]
    3P0G X-ray 3.50 A 1-230 [» ]
    A 263-365 [» ]
    3PDS X-ray 3.50 A 25-230 [» ]
    A 264-348 [» ]
    3SN6 X-ray 3.20 R 29-365 [» ]
    4GBR X-ray 3.99 A 29-365 [» ]
    4LDE X-ray 2.79 A 29-348 [» ]
    4LDL X-ray 3.10 A 29-348 [» ]
    4LDO X-ray 3.20 A 29-348 [» ]
    ProteinModelPortali P07550.
    SMRi P07550. Positions 29-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106663. 237 interactions.
    DIPi DIP-33948N.
    IntActi P07550. 12 interactions.
    MINTi MINT-148142.

    Chemistry

    BindingDBi P07550.
    ChEMBLi CHEMBL2096974.
    DrugBanki 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.
    GuidetoPHARMACOLOGYi 29.

    Protein family/group databases

    TCDBi 9.A.14.3.5. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei P07550.

    Polymorphism databases

    DMDMi 296439450.

    Proteomic databases

    MaxQBi P07550.
    PaxDbi P07550.
    PRIDEi P07550.

    Protocols and materials databases

    DNASUi 154.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305988 ; ENSP00000305372 ; ENSG00000169252 .
    GeneIDi 154.
    KEGGi hsa:154.
    UCSCi uc003lpr.2. human.

    Organism-specific databases

    CTDi 154.
    GeneCardsi GC05P148186.
    HGNCi HGNC:286. ADRB2.
    HPAi HPA003431.
    MIMi 109690. gene+phenotype.
    neXtProti NX_P07550.
    PharmGKBi PA39.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262978.
    HOVERGENi HBG106962.
    InParanoidi P07550.
    KOi K04142.
    OMAi RVFQVAK.
    OrthoDBi EOG7BS4BS.
    PhylomeDBi P07550.
    TreeFami TF316350.

    Enzyme and pathway databases

    Reactomei REACT_16927. Adrenoceptors.
    REACT_19327. G alpha (s) signalling events.
    SignaLinki P07550.

    Miscellaneous databases

    EvolutionaryTracei P07550.
    GeneWikii Beta-2_adrenergic_receptor.
    GenomeRNAii 154.
    NextBioi 613.
    PROi P07550.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07550.
    Bgeei P07550.
    Genevestigatori P07550.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR002233. ADR_fam.
    IPR000332. ADRB2_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24248:SF21. PTHR24248:SF21. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01103. ADRENERGICR.
    PR00562. ADRENRGCB2AR.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
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    Publicationsi

    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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiADRB2_HUMAN
    AccessioniPrimary (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 historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 177 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3