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Protein

Beta-1 adrenergic receptor

Gene

ADRB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: GO_Central
  • 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

Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000043591.5
HGNCiHGNC:285 ADRB1
MIMi109630 gene
neXtProtiNX_P08588

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

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
DrugBankiDB08347 4-{[(2S)-3-(tert-butylamino)-2-hydroxypropyl]oxy}-3H-indole-2-carbonitrile
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
DB06726 Bufuralol
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...) asparagineCurated1
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
PeptideAtlasiP08588
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

Show more details

GO - Molecular functioni

  • alpha-2A adrenergic receptor binding Source: BHF-UCL
  • PDZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi106662, 8 interactors
CORUMiP08588
DIPiDIP-36294N
IntActiP08588, 13 interactors
MINTiP08588
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

InterProiView protein in InterPro
IPR002233 ADR_fam
IPR000507 ADRB1_rcpt
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR01103 ADRENERGICR
PR00561 ADRENRGCB1AR
PR00237 GPCRRHODOPSN
SMARTiView protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

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 dbSNP:rs34844626Ensembl.1
Natural variantiVAR_05591029A → T. Corresponds to variant dbSNP:rs35720093Ensembl.1
Natural variantiVAR_05591131R → Q. Corresponds to variant dbSNP:rs35230616Ensembl.1
Natural variantiVAR_00987949S → G Associated with high mean resting heart rate. 4 PublicationsCorresponds to variant dbSNP:rs1801252Ensembl.1
Natural variantiVAR_009880389R → G Reduced binding to G proteins. 4 PublicationsCorresponds to variant dbSNP:rs1801253Ensembl.1
Natural variantiVAR_018742389R → L1 Publication1
Natural variantiVAR_055912399R → H. Corresponds to variant dbSNP:rs36052953Ensembl.1
Natural variantiVAR_055913405H → Y. Corresponds to variant dbSNP:rs35705839Ensembl.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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiADRB1_HUMAN
AccessioniPrimary (citable) accession number: P08588
Secondary accession number(s): B0LPE2
, Q5T5Y4, Q9UKG7, Q9UKG8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 7, 2004
Last modified: March 28, 2018
This is version 187 of the entry and version 2 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health