Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00837
Entry Name
UniProt Accession
Theoretical PI
6.59
Molecular Weight
46458.67
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Beta-2 adrenergic receptor
Protein Synonyms/Alias
Beta-2 adrenoreceptor; Beta-2 adrenoceptor;
Gene Name
ADRB2
Gene Synonyms/Alias
ADRB2R; B2AR;
Created Date
01-APR-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
341
Canonical
IAFQELLCLRRSSLK
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] O'Dowd BF, Hnatowich M, Caron MG, Lefkowitz RJ, Bouvier M. Palmitoylation ofthe human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tailleads to an uncoupled nonpalmitoylated form of the receptor. J Biol Chem. 1989May 5;264(13):7564-9.[PMID:2540197]
[2] Trester-Zedlitz M, Burlingame A, Kobilka B, von Zastrow M. Mass spectrometric analysis of agonist effects on posttranslational modifications of the beta-2adrenoceptor in mammalian cells. Biochemistry. 2005 Apr 26;44(16):6133-43. PubMedPMID: 15835901.[PMID:15835901]
Functional Description
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.
Sequence Annotation
Topological domain: 1 34 Extracellular.
Transmembrane: 35 58 Helical; Name=1.
Topological domain: 59 71 Cytoplasmic.
Transmembrane: 72 95 Helical; Name=2.
Topological domain: 96 106 Extracellular.
Transmembrane: 107 129 Helical; Name=3.
Topological domain: 130 150 Cytoplasmic.
Transmembrane: 151 174 Helical; Name=4.
Topological domain: 175 196 Extracellular.
Transmembrane: 197 220 Helical; Name=5.
Topological domain: 221 274 Cytoplasmic.
Transmembrane: 275 298 Helical; Name=6.
Topological domain: 299 305 Extracellular.
Transmembrane: 306 329 Helical; Name=7.
Topological domain: 330 413 Cytoplasmic.
Region: 193 207 Agonist and antagonist binding.
Region: 286 293 Agonist and antagonist binding.
Region: 312 316 Agonist and antagonist binding.
Motif: 410 413 PDZ-binding.
Binding site: 113 113 Agonist or antagonist.
Binding site: 118 118 Agonist or antagonist.
Modified residue: 141 141 Phosphotyrosine.
Modified residue: 246 246 Phosphoserine.
Modified residue: 261 261 Phosphoserine; by PKA.
Modified residue: 262 262 Phosphoserine; by PKA.
Modified residue: 345 345 Phosphoserine; by PKA.
Modified residue: 346 346 Phosphoserine; by PKA.
Modified residue: 355 355 Phosphoserine; by BARK.
Modified residue: 356 356 Phosphoserine; by BARK.
Modified residue: 382 382 4-hydroxyproline.
Modified residue: 395 395 4-hydroxyproline.
Protein Length
413 AA.
Protein Sequence
(Canonical)
MGQPGNGSAF LLAPNGSHAP DHDVTQERDE VWVVGMGIVM SLIVLAIVFG NVLVITAIAK  60
FERLQTVTNY FITSLACADL VMGLAVVPFG AAHILMKMWT FGNFWCEFWT SIDVLCVTAS  120
IETLCVIAVD RYFAITSPFK YQSLLTKNKA RVIILMVWIV SGLTSFLPIQ MHWYRATHQE  180
AINCYANETC CDFFTNQAYA IASSIVSFYV PLVIMVFVYS RVFQEAKRQL QKIDKSEGRF  240
HVQNLSQVEQ DGRTGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD  300
NLIRKEVYIL LNWIGYVNSG FNPLIYCRSP DFRIAFQELL CLRRSSLKAY GNGYSSNGNT  360
GEQSGYHVEQ EKENKLLCED LPGTEDFVGH QGTVPSDNID SQGRNCSTND SLL         413
FASTA
(Canonical)
>LipidDB-9606-00837|P07550
MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAK
FERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTAS
IETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQE
AINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRF
HVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQD
NLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNT
GEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL
Gene Ontology
GO:0016324; C:apical plasma membrane; IEA:Ensembl
GO:0005768; C:endosome; TAS:ProtInc
GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL
GO:0005764; C:lysosome; TAS:ProtInc
GO:0005634; C:nucleus; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:MGI
GO:0043235; C:receptor complex; IDA:HGNC
GO:0004941; F:beta2-adrenergic receptor activity; IDA:HGNC
GO:0051380; F:norepinephrine binding; IDA:HGNC
GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL
GO:0042803; F:protein homodimerization activity; IDA:HGNC
GO:0007190; P:activation of adenylate cyclase activity; IDA:HGNC
GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IEA:Ensembl
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; TAS:ProtInc
GO:0071875; P:adrenergic receptor signaling pathway; IDA:GOC
GO:0045453; P:bone resorption; IEA:Ensembl
GO:0050873; P:brown fat cell differentiation; IEA:Ensembl
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc
GO:0002032; P:desensitization of G-protein coupled receptor protein signaling pathway by arrestin; IDA:HGNC
GO:0002024; P:diet induced thermogenesis; IEA:Ensembl
GO:0008333; P:endosome to lysosome transport; TAS:ProtInc
GO:0031649; P:heat generation; IEA:Ensembl
GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl
GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl
GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl
GO:0043410; P:positive regulation of MAPK cascade; IDA:HGNC
GO:0031398; P:positive regulation of protein ubiquitination; IMP:BHF-UCL
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl
GO:0006898; P:receptor-mediated endocytosis; IDA:HGNC
GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl
GO:0042312; P:regulation of vasodilation; IEA:InterPro
GO:0009409; P:response to cold; IEA:Ensembl
GO:0002025; P:vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure; IEA:Ensembl
Interpro
InterPro; IPR002233; ADR_fam
InterPro; IPR000332; ADRB2_rcpt
InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
Pfam
Pfam; PF00001; 7tm_1;
SMART
PROSITE
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PRINTS
PRINTS; PR01103; ADRENERGICR;
PRINTS; PR00562; ADRENRGCB2AR;
PRINTS; PR00237; GPCRRHODOPSN;