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Protein

Beta-2 adrenergic receptor

Gene

ADRB2

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. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei113Agonist or antagonist1
Binding sitei118Agonist or antagonist1

GO - Molecular functioni

  • beta2-adrenergic receptor activity Source: HGNC
  • epinephrine binding Source: GO_Central
  • norepinephrine binding Source: HGNC
  • potassium channel regulator activity Source: BHF-UCL
  • protein homodimerization activity Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169252-MONOMER.
ReactomeiR-HSA-390696. Adrenoceptors.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP07550.
SIGNORiP07550.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:286. ADRB2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 34ExtracellularAdd BLAST34
Transmembranei35 – 58Helical; Name=1Add BLAST24
Topological domaini59 – 71CytoplasmicAdd BLAST13
Transmembranei72 – 95Helical; Name=2Add BLAST24
Topological domaini96 – 106ExtracellularAdd BLAST11
Transmembranei107 – 129Helical; Name=3Add BLAST23
Topological domaini130 – 150CytoplasmicAdd BLAST21
Transmembranei151 – 174Helical; Name=4Add BLAST24
Topological domaini175 – 196ExtracellularAdd BLAST22
Transmembranei197 – 220Helical; Name=5Add BLAST24
Topological domaini221 – 274CytoplasmicAdd BLAST54
Transmembranei275 – 298Helical; Name=6Add BLAST24
Topological domaini299 – 305Extracellular7
Transmembranei306 – 329Helical; Name=7Add BLAST24
Topological domaini330 – 413CytoplasmicAdd BLAST84

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • early endosome Source: UniProtKB-SubCell
  • endosome Source: ProtInc
  • integral component of plasma membrane Source: BHF-UCL
  • lysosome Source: ProtInc
  • nucleus Source: Ensembl
  • plasma membrane Source: MGI
  • receptor complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi79D → N: Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins. 1 Publication1
Mutagenesisi141Y → F: Abolishes insulin-induced tyrosine phosphorylation and insulin-induced receptor supersensitization. 1 Publication1
Mutagenesisi341C → G: Uncoupled receptor. 1 Publication1
Mutagenesisi345 – 346SS → AA: Delayed agonist-promoted desensitization. 1 Publication2
Mutagenesisi350Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 1 Publication1
Mutagenesisi354Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 1 Publication1
Mutagenesisi366Y → F: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 1 Publication1

Organism-specific databases

DisGeNETi154.
MalaCardsiADRB2.
MIMi109690. gene+phenotype.
OpenTargetsiENSG00000169252.
PharmGKBiPA39.

Chemistry databases

ChEMBLiCHEMBL210.
DrugBankiDB01193. Acebutolol.
DB00866. Alprenolol.
DB00321. Amitriptyline.
DB00182. Amphetamine.
DB01102. Arbutamine.
DB01274. Arformoterol.
DB06216. Asenapine.
DB00335. Atenolol.
DB01408. Bambuterol.
DB00195. Betaxolol.
DB00217. Bethanidine.
DB01295. Bevantolol.
DB00612. Bisoprolol.
DB08807. Bopindolol.
DB08808. Bupranolol.
DB00248. Cabergoline.
DB00521. Carteolol.
DB01136. Carvedilol.
DB04846. Celiprolol.
DB01407. Clenbuterol.
DB01151. Desipramine.
DB00449. Dipivefrin.
DB00841. Dobutamine.
DB06262. Droxidopa.
DB01363. Ephedra.
DB00668. Epinephrine.
DB01288. Fenoterol.
DB00983. Formoterol.
DB05039. Indacaterol.
DB00221. Isoetarine.
DB01064. Isoprenaline.
DB00598. Labetalol.
DB01210. Levobunolol.
DB01365. Mephentermine.
DB01214. Metipranolol.
DB00264. Metoprolol.
DB00370. Mirtazapine.
DB01203. Nadolol.
DB04861. Nebivolol.
DB00368. Norepinephrine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB09080. Olodaterol.
DB00816. Orciprenaline.
DB01580. Oxprenolol.
DB01359. Penbutolol.
DB00925. Phenoxybenzamine.
DB00397. Phenylpropanolamine.
DB00960. Pindolol.
DB01291. Pirbuterol.
DB01366. Procaterol.
DB00571. Propranolol.
DB00852. Pseudoephedrine.
DB00867. Ritodrine.
DB01001. Salbutamol.
DB00938. Salmeterol.
DB00489. Sotalol.
DB00871. Terbutaline.
DB00373. Timolol.
DB00726. Trimipramine.
DB09082. Vilanterol.
GuidetoPHARMACOLOGYi29.

Polymorphism and mutation databases

BioMutaiADRB2.
DMDMi296439450.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000691301 – 413Beta-2 adrenergic receptorAdd BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi6N-linked (GlcNAc...)Curated1
Glycosylationi15N-linked (GlcNAc...)Curated1
Disulfide bondi106 ↔ 191
Modified residuei141Phosphotyrosine1 Publication1
Disulfide bondi184 ↔ 190
Modified residuei246PhosphoserineCombined sources1
Modified residuei261Phosphoserine; by PKASequence analysis1
Modified residuei262Phosphoserine; by PKASequence analysis1
Lipidationi341S-palmitoyl cysteine3 Publications1
Modified residuei345Phosphoserine; by PKA1 Publication1
Modified residuei346Phosphoserine; by PKA1 Publication1
Modified residuei355Phosphoserine; by BARKCurated1
Modified residuei356Phosphoserine; by BARKCurated1
Modified residuei3824-hydroxyproline1 Publication1
Modified residuei3954-hydroxyproline1 Publication1

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 (PubMed:19424180, PubMed:20559325). 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.2 Publications
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

PaxDbiP07550.
PeptideAtlasiP07550.
PRIDEiP07550.

PTM databases

iPTMnetiP07550.
PhosphoSitePlusiP07550.
SwissPalmiP07550.

Expressioni

Gene expression databases

BgeeiENSG00000169252.
ExpressionAtlasiP07550. baseline and differential.
GenevisibleiP07550. HS.

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. Interacts with CNIH4 (PubMed:24405750). Interacts with ARRDC3 (PubMed:20559325, PubMed:25220262).15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRDC3Q96B676EBI-491169,EBI-2875665
MAGI3Q5TCQ99EBI-491169,EBI-310506
SLC9A3R1O147456EBI-491169,EBI-349787
SRCP129313EBI-491169,EBI-621482

GO - Molecular functioni

  • protein homodimerization activity Source: HGNC

Protein-protein interaction databases

BioGridi106663. 242 interactors.
DIPiDIP-33948N.
IntActiP07550. 13 interactors.
MINTiMINT-148142.
STRINGi9606.ENSP00000305372.

Chemistry databases

BindingDBiP07550.

Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 27Combined sources3
Helixi31 – 60Combined sources30
Helixi62 – 64Combined sources3
Helixi67 – 85Combined sources19
Helixi87 – 96Combined sources10
Helixi102 – 136Combined sources35
Beta strandi137 – 139Combined sources3
Helixi147 – 170Combined sources24
Turni171 – 174Combined sources4
Helixi179 – 186Combined sources8
Beta strandi187 – 189Combined sources3
Helixi197 – 207Combined sources11
Helixi209 – 229Combined sources21
Turni235 – 239Combined sources5
Turni263 – 265Combined sources3
Helixi267 – 298Combined sources32
Beta strandi299 – 303Combined sources5
Helixi305 – 317Combined sources13
Helixi318 – 320Combined sources3
Helixi322 – 325Combined sources4
Helixi326 – 328Combined sources3
Helixi330 – 339Combined sources10
Turni340 – 342Combined sources3
Turni345 – 347Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QKXX-ray3.30A29-348[»]
5D5AX-ray2.48A1-230[»]
A263-365[»]
5D5BX-ray3.80A1-230[»]
A263-365[»]
5D6LX-ray3.20A1-223[»]
A264-365[»]
5JQHX-ray3.20A/B30-348[»]
ProteinModelPortaliP07550.
SMRiP07550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07550.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni193 – 207Agonist and antagonist bindingAdd BLAST15
Regioni286 – 293Agonist and antagonist binding8
Regioni312 – 316Agonist and antagonist binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi410 – 413PDZ-binding4

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

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118774.
HOVERGENiHBG106962.
InParanoidiP07550.
KOiK04142.
OMAiGRFHAQN.
OrthoDBiEOG091G06VI.
PhylomeDBiP07550.
TreeFamiTF316350.

Family and domain databases

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.
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.

P07550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQPGNGSAF LLAPNGSHAP DHDVTQERDE VWVVGMGIVM SLIVLAIVFG
60 70 80 90 100
NVLVITAIAK FERLQTVTNY FITSLACADL VMGLAVVPFG AAHILMKMWT
110 120 130 140 150
FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYFAITSPFK YQSLLTKNKA
160 170 180 190 200
RVIILMVWIV SGLTSFLPIQ MHWYRATHQE AINCYANETC CDFFTNQAYA
210 220 230 240 250
IASSIVSFYV PLVIMVFVYS RVFQEAKRQL QKIDKSEGRF HVQNLSQVEQ
260 270 280 290 300
DGRTGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD
310 320 330 340 350
NLIRKEVYIL LNWIGYVNSG FNPLIYCRSP DFRIAFQELL CLRRSSLKAY
360 370 380 390 400
GNGYSSNGNT GEQSGYHVEQ EKENKLLCED LPGTEDFVGH QGTVPSDNID
410
SQGRNCSTND SLL
Length:413
Mass (Da):46,459
Last modified:May 18, 2010 - v3
Checksum:i408C22731C6EDFBE
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71F → L in BAG35969 (PubMed:14702039).Curated1
Sequence conflicti216V → A in AAN01267 (Ref. 8) Curated1
Sequence conflicti261S → P in BAD96745 (Ref. 10) Curated1
Sequence conflicti402Q → P in AAH12481 (PubMed:15489334).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_04937315N → S.Corresponds to variant rs33973603dbSNPEnsembl.1
Natural variantiVAR_00345216G → R Common polymorphism. 8 PublicationsCorresponds to variant rs1042713dbSNPEnsembl.1
Natural variantiVAR_00345327E → Q.13 PublicationsCorresponds to variant rs1042714dbSNPEnsembl.1
Natural variantiVAR_00345434V → M.1 Publication1
Natural variantiVAR_009125159I → F.1 Publication1
Natural variantiVAR_009124159I → L.1 Publication1
Natural variantiVAR_003455164T → I.1 PublicationCorresponds to variant rs1800888dbSNPEnsembl.1
Natural variantiVAR_025101220S → C.1 PublicationCorresponds to variant rs3729943dbSNPEnsembl.1
Natural variantiVAR_009394375K → R.1 PublicationCorresponds to variant rs771585355dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QKXX-ray3.30A29-348[»]
5D5AX-ray2.48A1-230[»]
A263-365[»]
5D5BX-ray3.80A1-230[»]
A263-365[»]
5D6LX-ray3.20A1-223[»]
A264-365[»]
5JQHX-ray3.20A/B30-348[»]
ProteinModelPortaliP07550.
SMRiP07550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106663. 242 interactors.
DIPiDIP-33948N.
IntActiP07550. 13 interactors.
MINTiMINT-148142.
STRINGi9606.ENSP00000305372.

Chemistry databases

BindingDBiP07550.
ChEMBLiCHEMBL210.
DrugBankiDB01193. Acebutolol.
DB00866. Alprenolol.
DB00321. Amitriptyline.
DB00182. Amphetamine.
DB01102. Arbutamine.
DB01274. Arformoterol.
DB06216. Asenapine.
DB00335. Atenolol.
DB01408. Bambuterol.
DB00195. Betaxolol.
DB00217. Bethanidine.
DB01295. Bevantolol.
DB00612. Bisoprolol.
DB08807. Bopindolol.
DB08808. Bupranolol.
DB00248. Cabergoline.
DB00521. Carteolol.
DB01136. Carvedilol.
DB04846. Celiprolol.
DB01407. Clenbuterol.
DB01151. Desipramine.
DB00449. Dipivefrin.
DB00841. Dobutamine.
DB06262. Droxidopa.
DB01363. Ephedra.
DB00668. Epinephrine.
DB01288. Fenoterol.
DB00983. Formoterol.
DB05039. Indacaterol.
DB00221. Isoetarine.
DB01064. Isoprenaline.
DB00598. Labetalol.
DB01210. Levobunolol.
DB01365. Mephentermine.
DB01214. Metipranolol.
DB00264. Metoprolol.
DB00370. Mirtazapine.
DB01203. Nadolol.
DB04861. Nebivolol.
DB00368. Norepinephrine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB09080. Olodaterol.
DB00816. Orciprenaline.
DB01580. Oxprenolol.
DB01359. Penbutolol.
DB00925. Phenoxybenzamine.
DB00397. Phenylpropanolamine.
DB00960. Pindolol.
DB01291. Pirbuterol.
DB01366. Procaterol.
DB00571. Propranolol.
DB00852. Pseudoephedrine.
DB00867. Ritodrine.
DB01001. Salbutamol.
DB00938. Salmeterol.
DB00489. Sotalol.
DB00871. Terbutaline.
DB00373. Timolol.
DB00726. Trimipramine.
DB09082. Vilanterol.
GuidetoPHARMACOLOGYi29.

Protein family/group databases

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

PTM databases

iPTMnetiP07550.
PhosphoSitePlusiP07550.
SwissPalmiP07550.

Polymorphism and mutation databases

BioMutaiADRB2.
DMDMi296439450.

Proteomic databases

PaxDbiP07550.
PeptideAtlasiP07550.
PRIDEiP07550.

Protocols and materials databases

DNASUi154.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305988; ENSP00000305372; ENSG00000169252.
GeneIDi154.
KEGGihsa:154.

Organism-specific databases

CTDi154.
DisGeNETi154.
GeneCardsiADRB2.
HGNCiHGNC:286. ADRB2.
HPAiHPA003431.
MalaCardsiADRB2.
MIMi109690. gene+phenotype.
neXtProtiNX_P07550.
OpenTargetsiENSG00000169252.
PharmGKBiPA39.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118774.
HOVERGENiHBG106962.
InParanoidiP07550.
KOiK04142.
OMAiGRFHAQN.
OrthoDBiEOG091G06VI.
PhylomeDBiP07550.
TreeFamiTF316350.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169252-MONOMER.
ReactomeiR-HSA-390696. Adrenoceptors.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP07550.
SIGNORiP07550.

Miscellaneous databases

EvolutionaryTraceiP07550.
GeneWikiiBeta-2_adrenergic_receptor.
GenomeRNAii154.
PROiP07550.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169252.
ExpressionAtlasiP07550. baseline and differential.
GenevisibleiP07550. HS.

Family and domain databases

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.
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 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: November 2, 2016
This is version 199 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

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.