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P08588

- ADRB1_HUMAN

UniProt

P08588 - ADRB1_HUMAN

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Protein

Beta-1 adrenergic receptor

Gene

ADRB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 heterodimerization activity Source: BHF-UCL
  10. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  11. 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
Complete GO annotation...

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
Complete GO annotation...

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.
GeneTreeiENSGT00760000118774.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAGVLVLGA SEPGNLSSAA PLPDGAATAA RLLVPASPPA SLLPPASESP
60 70 80 90 100
EPLSQQWTAG MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL
110 120 130 140 150
ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC
160 170 180 190 200
VIALDRYLAI TSPFRYQSLL TRARARGLVC TVWAISALVS FLPILMHWWR
210 220 230 240 250
AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE
260 270 280 290 300
AQKQVKKIDS CERRFLGGPA RPPSPSPSPV PAPAPPPGPP RPAAAAATAP
310 320 330 340 350
LANGRAGKRR PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH
360 370 380 390 400
RELVPDRLFV FFNWLGYANS AFNPIIYCRS PDFRKAFQRL LCCARRAARR
410 420 430 440 450
RHATHGDRPR ASGCLARPGP PPSPGAASDD DDDDVVGATP PARLLEPWAG
460 470
CNGGAAADSD SSLDEPCRPG FASESKV
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 CHEMBL2097169.
DrugBanki DB01193. Acebutolol.
DB00866. Alprenolol.
DB01118. Amiodarone.
DB00321. Amitriptyline.
DB00182. Amphetamine.
DB01102. Arbutamine.
DB06216. Asenapine.
DB00335. Atenolol.
DB00195. Betaxolol.
DB00217. Bethanidine.
DB01295. Bevantolol.
DB00612. Bisoprolol.
DB08807. Bopindolol.
DB08808. Bupranolol.
DB00248. Cabergoline.
DB00521. Carteolol.
DB01136. Carvedilol.
DB01407. Clenbuterol.
DB01151. Desipramine.
DB00841. Dobutamine.
DB04855. Dronedarone.
DB06262. Droxidopa.
DB01363. Ephedra.
DB00668. Epinephrine.
DB00187. Esmolol.
DB01288. Fenoterol.
DB00221. Isoetarine.
DB01064. Isoprenaline.
DB00598. Labetalol.
DB01210. Levobunolol.
DB00408. Loxapine.
DB01365. Mephentermine.
DB01214. Metipranolol.
DB00264. Metoprolol.
DB00370. Mirtazapine.
DB01203. Nadolol.
DB04861. Nebivolol.
DB00368. Norepinephrine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB01580. Oxprenolol.
DB01359. Penbutolol.
DB00397. Phenylpropanolamine.
DB00960. Pindolol.
DB01291. Pirbuterol.
DB01297. Practolol.
DB00571. Propranolol.
DB00852. Pseudoephedrine.
DB01001. Salbutamol.
DB00489. Sotalol.
DB00373. Timolol.
DB00726. Trimipramine.
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.
GeneTreei ENSGT00760000118774.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 157 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