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P08588

- ADRB1_HUMAN

UniProt

P08588 - ADRB1_HUMAN

Protein

Beta-1 adrenergic receptor

Gene

ADRB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      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. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei138 – 1381Agonist or antagonistBy similarity
    Binding sitei143 – 1431Agonist or antagonistBy similarity

    GO - Molecular functioni

    1. alpha-2A adrenergic receptor binding Source: BHF-UCL
    2. beta1-adrenergic receptor activity Source: ProtInc
    3. beta-adrenergic receptor activity Source: ProtInc
    4. dopamine binding Source: Ensembl
    5. drug binding Source: Ensembl
    6. epinephrine binding Source: Ensembl
    7. norepinephrine binding Source: Ensembl
    8. PDZ domain binding Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. protein heterodimerization activity Source: BHF-UCL
    11. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
    12. receptor signaling protein activity Source: UniProtKB

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: ProtInc
    2. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
    3. aging Source: Ensembl
    4. apoptotic process Source: Ensembl
    5. brown fat cell differentiation Source: Ensembl
    6. diet induced thermogenesis Source: Ensembl
    7. fear response Source: Ensembl
    8. glycogen catabolic process Source: Ensembl
    9. heat generation Source: Ensembl
    10. lipid homeostasis Source: Ensembl
    11. memory Source: Ensembl
    12. negative regulation of multicellular organism growth Source: Ensembl
    13. negative regulation of smooth muscle contraction Source: Ensembl
    14. negative regulation of urine volume Source: Ensembl
    15. positive regulation of apoptotic process Source: Ensembl
    16. positive regulation of cAMP biosynthetic process Source: UniProtKB
    17. positive regulation of cAMP-mediated signaling Source: UniProtKB
    18. positive regulation of cation channel activity Source: Ensembl
    19. positive regulation of cell growth involved in cardiac muscle cell development Source: Ensembl
    20. positive regulation of heart rate by epinephrine-norepinephrine Source: Ensembl
    21. positive regulation of Ras GTPase activity Source: UniProtKB
    22. positive regulation of renin secretion into blood stream Source: Ensembl
    23. positive regulation of saliva secretion Source: Ensembl
    24. positive regulation of systemic arterial blood pressure Source: Ensembl
    25. positive regulation of the force of heart contraction by norepinephrine Source: Ensembl
    26. protein localization to organelle Source: Ensembl
    27. regulation of calcium ion transport Source: Ensembl
    28. regulation of cardiac muscle cell contraction Source: Ensembl
    29. regulation of inhibitory postsynaptic membrane potential Source: Ensembl
    30. response to cold Source: Ensembl
    31. Rho protein signal transduction Source: Ensembl
    32. sensory perception of pain Source: Ensembl
    33. vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: Ensembl
    34. wound healing 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.
    SignaLinkiP08588.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1 adrenergic receptor
    Alternative name(s):
    Beta-1 adrenoreceptor
    Short name:
    Beta-1 adrenoceptor
    Gene namesi
    Name:ADRB1
    Synonyms:ADRB1R, B1AR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:285. ADRB1.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Early endosome
    Note: Colocalizes with RAPGEF2 at the plasma membrane By similarity. Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression.By similarity

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. nucleus Source: Ensembl
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi474 – 4741E → A or D: Loss of interaction with GOPC. 1 Publication
    Mutagenesisi474 – 4741E → K: Loss of interaction with GOPC; when associated with A-477. 1 Publication
    Mutagenesisi475 – 4751S → A: Loss of interaction with GOPC. Loss of interaction with RAPGEF2. Abolishes agonist-induced Ras activation. 2 Publications
    Mutagenesisi475 – 4751S → D: Loss of interaction with RAPGEF2. 2 Publications
    Mutagenesisi475 – 4751S → T: Partial loss of interaction with GOPC. 2 Publications
    Mutagenesisi476 – 4761K → A: Partial loss of interaction with GOPC. 1 Publication
    Mutagenesisi477 – 4771V → A, F, L, I or M: Loss of interaction with GOPC. 2 Publications
    Mutagenesisi477 – 4771V → A: Loss of interaction with RAPGEF2. Abolishes agonist-induced Ras activation. 2 Publications

    Organism-specific databases

    MIMi607276. phenotype.
    PharmGKBiPA38.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 477477Beta-1 adrenergic receptorPRO_0000069118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi15 – 151N-linked (GlcNAc...)Curated
    Disulfide bondi131 ↔ 216PROSITE-ProRule annotation
    Disulfide bondi209 ↔ 215PROSITE-ProRule annotation
    Modified residuei312 – 3121Phosphoserine; by PKASequence Analysis
    Lipidationi392 – 3921S-palmitoyl cysteineBy similarity
    Modified residuei412 – 4121Phosphoserine; by PKASequence Analysis

    Post-translational modificationi

    Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP08588.
    PRIDEiP08588.

    PTM databases

    PhosphoSiteiP08588.

    Expressioni

    Gene expression databases

    BgeeiP08588.
    CleanExiHS_ADRB1.
    GenevestigatoriP08588.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus PDZ motif) with RAPGEF2; the interaction is direct. Interacts with GOPC, MAGI3 and DLG4.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAGI2Q86UL82EBI-991009,EBI-311035
    MAGI3Q5TCQ95EBI-991009,EBI-310506
    Pde4dP142702EBI-991009,EBI-8333209From a different organism.

    Protein-protein interaction databases

    BioGridi106662. 8 interactions.
    DIPiDIP-36294N.
    IntActiP08588. 10 interactions.
    MINTiMINT-208845.
    STRINGi9606.ENSP00000358301.

    Structurei

    Secondary structure

    1
    477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi205 – 2084
    Helixi209 – 2113
    Helixi213 – 2153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LSQNMR-A197-221[»]
    ProteinModelPortaliP08588.
    SMRiP08588. Positions 51-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5555ExtracellularBy similarityAdd
    BLAST
    Topological domaini85 – 939CytoplasmicBy similarity
    Topological domaini121 – 13212ExtracellularBy similarityAdd
    BLAST
    Topological domaini155 – 17218CytoplasmicBy similarityAdd
    BLAST
    Topological domaini197 – 22226ExtracellularBy similarityAdd
    BLAST
    Topological domaini249 – 31971CytoplasmicBy similarityAdd
    BLAST
    Topological domaini350 – 3545ExtracellularBy similarity
    Topological domaini378 – 477100CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei56 – 8429Helical; Name=1By similarityAdd
    BLAST
    Transmembranei94 – 12027Helical; Name=2By similarityAdd
    BLAST
    Transmembranei133 – 15422Helical; Name=3By similarityAdd
    BLAST
    Transmembranei173 – 19624Helical; Name=4By similarityAdd
    BLAST
    Transmembranei223 – 24826Helical; Name=5By similarityAdd
    BLAST
    Transmembranei320 – 34930Helical; Name=6By similarityAdd
    BLAST
    Transmembranei355 – 37723Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni218 – 23215Agonist and antagonist bindingBy similarityAdd
    BLAST
    Regioni337 – 3448Agonist and antagonist bindingBy similarity
    Regioni363 – 3675Agonist and antagonist bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi474 – 4774PDZ-Binding

    Domaini

    The PDZ domain-binding motif mediates competitive interactions with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of the receptor.

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262978.
    HOGENOMiHOG000239242.
    HOVERGENiHBG106962.
    InParanoidiP08588.
    KOiK04141.
    OrthoDBiEOG7BS4BS.
    PhylomeDBiP08588.
    TreeFamiTF316350.

    Family and domain databases

    Gene3Di1.20.1070.10. 2 hits.
    InterProiIPR002233. ADR_fam.
    IPR000507. ADRB1_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR01103. ADRENERGICR.
    PR00561. ADRENRGCB1AR.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08588-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAGVLVLGA SEPGNLSSAA PLPDGAATAA RLLVPASPPA SLLPPASESP    50
    EPLSQQWTAG MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL 100
    ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC 150
    VIALDRYLAI TSPFRYQSLL TRARARGLVC TVWAISALVS FLPILMHWWR 200
    AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE 250
    AQKQVKKIDS CERRFLGGPA RPPSPSPSPV PAPAPPPGPP RPAAAAATAP 300
    LANGRAGKRR PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH 350
    RELVPDRLFV FFNWLGYANS AFNPIIYCRS PDFRKAFQRL LCCARRAARR 400
    RHATHGDRPR ASGCLARPGP PPSPGAASDD DDDDVVGATP PARLLEPWAG 450
    CNGGAAADSD SSLDEPCRPG FASESKV 477
    Length:477
    Mass (Da):51,323
    Last modified:June 7, 2004 - v2
    Checksum:i0950F2684E4721B8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261A → V.
    Corresponds to variant rs34844626 [ dbSNP | Ensembl ].
    VAR_055909
    Natural varianti29 – 291A → T.
    Corresponds to variant rs35720093 [ dbSNP | Ensembl ].
    VAR_055910
    Natural varianti31 – 311R → Q.
    Corresponds to variant rs35230616 [ dbSNP | Ensembl ].
    VAR_055911
    Natural varianti49 – 491S → G Associated with high mean resting heart rate. 4 Publications
    Corresponds to variant rs1801252 [ dbSNP | Ensembl ].
    VAR_009879
    Natural varianti389 – 3891R → G Reduced binding to G proteins. 4 Publications
    Corresponds to variant rs1801253 [ dbSNP | Ensembl ].
    VAR_009880
    Natural varianti389 – 3891R → L.1 Publication
    VAR_018742
    Natural varianti399 – 3991R → H.
    Corresponds to variant rs36052953 [ dbSNP | Ensembl ].
    VAR_055912
    Natural varianti405 – 4051H → Y.
    Corresponds to variant rs35705839 [ dbSNP | Ensembl ].
    VAR_055913

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03019 mRNA. Translation: AAA51667.1.
    AF169006 Genomic DNA. Translation: AAD53696.1.
    AF169007 Genomic DNA. Translation: AAD53697.1.
    AY567837 Genomic DNA. Translation: AAS66983.1.
    EU332832 Genomic DNA. Translation: ABY87521.1.
    AL355543 Genomic DNA. Translation: CAI16920.1.
    CCDSiCCDS7586.1.
    PIRiA39911. QRHUB1.
    RefSeqiNP_000675.1. NM_000684.2.
    UniGeneiHs.99913.

    Genome annotation databases

    EnsembliENST00000369295; ENSP00000358301; ENSG00000043591.
    GeneIDi153.
    KEGGihsa:153.
    UCSCiuc001lba.3. human.

    Polymorphism databases

    DMDMi48429211.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03019 mRNA. Translation: AAA51667.1 .
    AF169006 Genomic DNA. Translation: AAD53696.1 .
    AF169007 Genomic DNA. Translation: AAD53697.1 .
    AY567837 Genomic DNA. Translation: AAS66983.1 .
    EU332832 Genomic DNA. Translation: ABY87521.1 .
    AL355543 Genomic DNA. Translation: CAI16920.1 .
    CCDSi CCDS7586.1.
    PIRi A39911. QRHUB1.
    RefSeqi NP_000675.1. NM_000684.2.
    UniGenei Hs.99913.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LSQ NMR - A 197-221 [» ]
    ProteinModelPortali P08588.
    SMRi P08588. Positions 51-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106662. 8 interactions.
    DIPi DIP-36294N.
    IntActi P08588. 10 interactions.
    MINTi MINT-208845.
    STRINGi 9606.ENSP00000358301.

    Chemistry

    BindingDBi P08588.
    ChEMBLi CHEMBL213.
    DrugBanki DB01193. Acebutolol.
    DB00866. Alprenolol.
    DB01118. Amiodarone.
    DB01102. Arbutamine.
    DB00335. Atenolol.
    DB00195. Betaxolol.
    DB01295. Bevantolol.
    DB00612. Bisoprolol.
    DB01158. Bretylium.
    DB00521. Carteolol.
    DB01136. Carvedilol.
    DB01151. Desipramine.
    DB00841. Dobutamine.
    DB00988. Dopamine.
    DB00668. Epinephrine.
    DB00187. Esmolol.
    DB00221. Isoetharine.
    DB01064. Isoproterenol.
    DB00598. Labetalol.
    DB01210. Levobunolol.
    DB01214. Metipranolol.
    DB00264. Metoprolol.
    DB01203. Nadolol.
    DB00368. Norepinephrine.
    DB01580. Oxprenolol.
    DB01359. Penbutolol.
    DB00960. Pindolol.
    DB01297. Practolol.
    DB00571. Propranolol.
    DB00734. Risperidone.
    DB00373. Timolol.
    DB00246. Ziprasidone.
    GuidetoPHARMACOLOGYi 28.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P08588.

    Polymorphism databases

    DMDMi 48429211.

    Proteomic databases

    PaxDbi P08588.
    PRIDEi P08588.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369295 ; ENSP00000358301 ; ENSG00000043591 .
    GeneIDi 153.
    KEGGi hsa:153.
    UCSCi uc001lba.3. human.

    Organism-specific databases

    CTDi 153.
    GeneCardsi GC10P115793.
    H-InvDB HIX0035626.
    HGNCi HGNC:285. ADRB1.
    MIMi 109630. gene.
    607276. phenotype.
    neXtProti NX_P08588.
    PharmGKBi PA38.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262978.
    HOGENOMi HOG000239242.
    HOVERGENi HBG106962.
    InParanoidi P08588.
    KOi K04141.
    OrthoDBi EOG7BS4BS.
    PhylomeDBi P08588.
    TreeFami TF316350.

    Enzyme and pathway databases

    Reactomei REACT_16927. Adrenoceptors.
    REACT_19327. G alpha (s) signalling events.
    SignaLinki P08588.

    Miscellaneous databases

    GeneWikii Beta-1_adrenergic_receptor.
    GenomeRNAii 153.
    NextBioi 609.
    PROi P08588.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08588.
    CleanExi HS_ADRB1.
    Genevestigatori P08588.

    Family and domain databases

    Gene3Di 1.20.1070.10. 2 hits.
    InterProi IPR002233. ADR_fam.
    IPR000507. ADRB1_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01103. ADRENERGICR.
    PR00561. ADRENRGCB1AR.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Racial differences in the frequencies of cardiac beta(1)-adrenergic receptor polymorphisms: analysis of c145A>G and c1165G>C."
      Moore J.D., Mason D.A., Green S.A., Hsu J., Liggett S.B.
      Hum. Mutat. 14:271-271(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-49 AND GLY-389.
    3. SeattleSNPs variation discovery resource
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-49; GLY-389 AND LEU-389.
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-389.
    6. "Direct binding of the beta1 adrenergic receptor to the cyclic AMP-dependent guanine nucleotide exchange factor CNrasGEF leads to Ras activation."
      Pak Y., Pham N., Rotin D.
      Mol. Cell. Biol. 22:7942-7952(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAPGEF2, MUTAGENESIS OF SER-475 AND VAL-477.
    7. "Interaction with cystic fibrosis transmembrane conductance regulator-associated ligand (CAL) inhibits beta1-adrenergic receptor surface expression."
      He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.
      J. Biol. Chem. 279:50190-50196(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GOPC AND DLG4, MUTAGENESIS OF GLU-474; SER-475; LYS-476 AND VAL-477, SUBCELLULAR LOCATION.
    8. "Down-modulation of the G-protein-coupled estrogen receptor, GPER, from the cell surface occurs via a trans-Golgi-proteasome pathway."
      Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.
      J. Biol. Chem. 286:22441-22455(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "A gain-of-function polymorphism in a G-protein coupling domain of the human beta1-adrenergic receptor."
      Mason D.A., Moore J.D., Green S.A., Liggett S.B.
      J. Biol. Chem. 274:12670-12674(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLY-389.
    10. "A novel polymorphism in the gene coding for the beta(1)-adrenergic receptor associated with survival in patients with heart failure."
      Borjesson M., Magnusson Y., Hjalmarson A., Andersson B.
      Eur. Heart J. 21:1853-1858(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLY-49.
    11. Cited for: VARIANT GLY-49.

    Entry informationi

    Entry nameiADRB1_HUMAN
    AccessioniPrimary (citable) accession number: P08588
    Secondary accession number(s): B0LPE2
    , Q5T5Y4, Q9UKG7, Q9UKG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 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 10
      Human chromosome 10: 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