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Protein

Beta-1 adrenergic receptor

Gene

ADRB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei138Agonist or antagonistBy similarity1
Binding sitei143Agonist or antagonistBy similarity1

GO - Molecular functioni

  • alpha-2A adrenergic receptor binding Source: BHF-UCL
  • beta1-adrenergic receptor activity Source: ProtInc
  • beta-adrenergic receptor activity Source: ProtInc
  • epinephrine binding Source: GO_Central
  • norepinephrine binding Source: GO_Central
  • PDZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  • signal transducer activity, downstream of receptor Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

BioCyciZFISH:ENSG00000043591-MONOMER.
ReactomeiR-HSA-390696. Adrenoceptors.
R-HSA-418555. G alpha (s) signalling events.
SignaLinkiP08588.
SIGNORiP08588.

Protein family/group databases

TCDBi9.A.14.3.11. the g-protein-coupled receptor (gpcr) family.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:285. ADRB1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 55ExtracellularBy similarityAdd BLAST55
Transmembranei56 – 84Helical; Name=1By similarityAdd BLAST29
Topological domaini85 – 93CytoplasmicBy similarity9
Transmembranei94 – 120Helical; Name=2By similarityAdd BLAST27
Topological domaini121 – 132ExtracellularBy similarityAdd BLAST12
Transmembranei133 – 154Helical; Name=3By similarityAdd BLAST22
Topological domaini155 – 172CytoplasmicBy similarityAdd BLAST18
Transmembranei173 – 196Helical; Name=4By similarityAdd BLAST24
Topological domaini197 – 222ExtracellularBy similarityAdd BLAST26
Transmembranei223 – 248Helical; Name=5By similarityAdd BLAST26
Topological domaini249 – 319CytoplasmicBy similarityAdd BLAST71
Transmembranei320 – 349Helical; Name=6By similarityAdd BLAST30
Topological domaini350 – 354ExtracellularBy similarity5
Transmembranei355 – 377Helical; Name=7By similarityAdd BLAST23
Topological domaini378 – 477CytoplasmicBy similarityAdd BLAST100

GO - Cellular componenti

  • early endosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi474E → A or D: Loss of interaction with GOPC. 1 Publication1
Mutagenesisi474E → K: Loss of interaction with GOPC; when associated with A-477. 1 Publication1
Mutagenesisi475S → A: Loss of interaction with GOPC. Loss of interaction with RAPGEF2. Abolishes agonist-induced Ras activation. 2 Publications1
Mutagenesisi475S → D: Loss of interaction with RAPGEF2. 2 Publications1
Mutagenesisi475S → T: Partial loss of interaction with GOPC. 2 Publications1
Mutagenesisi476K → A: Partial loss of interaction with GOPC. 1 Publication1
Mutagenesisi477V → A, F, L, I or M: Loss of interaction with GOPC. 2 Publications1
Mutagenesisi477V → A: Loss of interaction with RAPGEF2. Abolishes agonist-induced Ras activation. 2 Publications1

Organism-specific databases

DisGeNETi153.
MIMi607276. phenotype.
PharmGKBiPA38.

Chemistry databases

ChEMBLiCHEMBL213.
DrugBankiDB01193. 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.
DB04846. Celiprolol.
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.
DB09068. Vortioxetine.
GuidetoPHARMACOLOGYi28.

Polymorphism and mutation databases

BioMutaiADRB1.
DMDMi48429211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000691181 – 477Beta-1 adrenergic receptorAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi15N-linked (GlcNAc...)Curated1
Disulfide bondi131 ↔ 216PROSITE-ProRule annotation
Disulfide bondi209 ↔ 215PROSITE-ProRule annotation
Modified residuei312Phosphoserine; by PKASequence analysis1
Lipidationi392S-palmitoyl cysteineBy similarity1
Modified residuei412Phosphoserine; by PKASequence analysis1
Modified residuei428PhosphoserineBy similarity1

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

iPTMnetiP08588.
PhosphoSitePlusiP08588.
SwissPalmiP08588.

Expressioni

Gene expression databases

BgeeiENSG00000043591.
CleanExiHS_ADRB1.
GenevisibleiP08588. HS.

Organism-specific databases

HPAiHPA067972.

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.

GO - Molecular functioni

  • alpha-2A adrenergic receptor binding Source: BHF-UCL
  • PDZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP08588.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi205 – 208Combined sources4
Helixi209 – 211Combined sources3
Helixi213 – 215Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LSQNMR-A197-221[»]
ProteinModelPortaliP08588.
SMRiP08588.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni218 – 232Agonist and antagonist bindingBy similarityAdd BLAST15
Regioni337 – 344Agonist and antagonist bindingBy similarity8
Regioni363 – 367Agonist and antagonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi474 – 477PDZ-Binding4

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

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP08588.
KOiK04141.
OrthoDBiEOG091G06VI.
PhylomeDBiP08588.
TreeFamiTF316350.

Family and domain databases

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.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
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

        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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05590926A → V.Corresponds to variant rs34844626dbSNPEnsembl.1
Natural variantiVAR_05591029A → T.Corresponds to variant rs35720093dbSNPEnsembl.1
Natural variantiVAR_05591131R → Q.Corresponds to variant rs35230616dbSNPEnsembl.1
Natural variantiVAR_00987949S → G Associated with high mean resting heart rate. 4 PublicationsCorresponds to variant rs1801252dbSNPEnsembl.1
Natural variantiVAR_009880389R → G Reduced binding to G proteins. 4 PublicationsCorresponds to variant rs1801253dbSNPEnsembl.1
Natural variantiVAR_018742389R → L.1 Publication1
Natural variantiVAR_055912399R → H.Corresponds to variant rs36052953dbSNPEnsembl.1
Natural variantiVAR_055913405H → Y.Corresponds to variant rs35705839dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LSQNMR-A197-221[»]
ProteinModelPortaliP08588.
SMRiP08588.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP08588.
ChEMBLiCHEMBL213.
DrugBankiDB01193. 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.
DB04846. Celiprolol.
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.
DB09068. Vortioxetine.
GuidetoPHARMACOLOGYi28.

Protein family/group databases

TCDBi9.A.14.3.11. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

PTM databases

iPTMnetiP08588.
PhosphoSitePlusiP08588.
SwissPalmiP08588.

Polymorphism and mutation databases

BioMutaiADRB1.
DMDMi48429211.

Proteomic databases

PaxDbiP08588.
PRIDEiP08588.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369295; ENSP00000358301; ENSG00000043591.
GeneIDi153.
KEGGihsa:153.
UCSCiuc001lba.4. human.

Organism-specific databases

CTDi153.
DisGeNETi153.
GeneCardsiADRB1.
H-InvDBHIX0035626.
HGNCiHGNC:285. ADRB1.
HPAiHPA067972.
MIMi109630. gene.
607276. phenotype.
neXtProtiNX_P08588.
PharmGKBiPA38.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP08588.
KOiK04141.
OrthoDBiEOG091G06VI.
PhylomeDBiP08588.
TreeFamiTF316350.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000043591-MONOMER.
ReactomeiR-HSA-390696. Adrenoceptors.
R-HSA-418555. G alpha (s) signalling events.
SignaLinkiP08588.
SIGNORiP08588.

Miscellaneous databases

GeneWikiiBeta-1_adrenergic_receptor.
GenomeRNAii153.
PROiP08588.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000043591.
CleanExiHS_ADRB1.
GenevisibleiP08588. HS.

Family and domain databases

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.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 177 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.