Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ADRB2 (human)

Overview
ADRB2 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. Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily. Note: This description may include information from UniProtKB.
Protein type: Receptor, GPCR; GPCR, family 1; Membrane protein, integral
Cellular Component: axon; integral to plasma membrane; lysosome; apical plasma membrane; plasma membrane; dendritic spine; caveola; nucleus; endosome; receptor complex; sarcolemma
Molecular Function: ionotropic glutamate receptor binding; protein binding; potassium channel regulator activity; protein homodimerization activity; dopamine binding; beta2-adrenergic receptor activity; norepinephrine binding; drug binding; epinephrine binding; adenylate cyclase binding
Biological Process: diet induced thermogenesis; transmembrane receptor protein tyrosine kinase activation (dimerization); wound healing; positive regulation of apoptosis; positive regulation of potassium ion transport; positive regulation of vasodilation; G-protein signaling, adenylate cyclase activating pathway; cell surface receptor linked signal transduction; positive regulation of MAPKKK cascade; negative regulation of smooth muscle contraction; diaphragm contraction; positive regulation of cell proliferation; negative regulation of ossification; endosome to lysosome transport; bone resorption; arrestin mediated desensitization of G-protein coupled receptor protein signaling pathway; receptor-mediated endocytosis; synaptic transmission, glutamatergic; negative regulation of multicellular organism growth; adenylate cyclase activation; positive regulation of bone mineralization; G-protein signaling, coupled to cAMP nucleotide second messenger; positive regulation of the force of heart contraction by epinephrine; positive regulation of protein ubiquitination; negative regulation of inflammatory response; heat generation; brown fat cell differentiation; positive regulation of transcription from RNA polymerase II promoter; regulation of sensory perception of pain; response to cold; positive regulation of skeletal muscle growth; regulation of excitatory postsynaptic membrane potential; norepinephrine-epinephrine vasodilation involved in regulation of systemic arterial blood pressure
Reference #:  P07550 (UniProtKB)
Alt. Names/Synonyms: ADRB2; ADRB2R; ADRBR; adrenergic, beta-2-, receptor, surface; B2AR; BAR; Beta-2 adrenergic receptor; Beta-2 adrenoceptor; Beta-2 adrenoreceptor; BETA2AR; catecholamine receptor
Gene Symbols: ADRB2
Molecular weight: 46,459 Da
Basal Isoelectric point: 6.59  Predict pI for various phosphorylation states
Select Structure to View Below

ADRB2

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
activation: T68‑p, Y132‑p, Y141‑p, Y219‑p
molecular association, regulation: S355‑p, S356‑p, T360‑p, S364‑p
protein degradation: S355‑p, S356‑p
receptor desensitization, altered: S345‑p, S346‑p, S355‑p, S356‑p, S364‑p
receptor internalization, altered: S346‑p, S355‑p, S356‑p, T360‑p, S364‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 T68-p FERLQTVtNYFITSL
3 0 Y132-p CVIAVDRyFAITSPF
4 0 Y141-p AITSPFKyQSLLTKN
1 0 Y219-p LVIMVFVySRVFQEA
1 4 S246-p RFHVQNLsQVEQDGR
5 0 S261-p TGHGLRRssKFCLKE
9 1 S262-p GHGLRRssKFCLKEH
3 0 Y326-p SGFNPLIyCRSPDFR
6 0 S345-p ELLCLRRssLKAyGN
7 1 S346-p LLCLRRssLKAyGNG
7 0 Y350-p RRssLKAyGNGyssN
5 0 Y354-p LKAyGNGyssNGNtG
15 0 S355-p KAyGNGyssNGNtGE
15 0 S356-p AyGNGyssNGNtGEQ
5 0 - gap
2 0 T360-p GyssNGNtGEQsGYH
4 0 S364-p NGNtGEQsGYHVEQE
4 0 T384-p LCEDLPGtEDFVGHQ
3 0 T393-p DFVGHQGtVPsDNID
4 0 S396-p GHQGtVPsDNIDsQG
3 0 S401-p VPsDNIDsQGRNCst
4 0 S407-p DsQGRNCstNDsLL_
1 0 T408-p sQGRNCstNDsLL__
5 0 S411-p RNCstNDsLL_____
  mouse

 
T68 FERLQTVTNYFIISL
Y132 CVIAVDRYVAITSPF
Y141 AITSPFKYQSLLTKN
Y219 LVVMVFVYSRVFQVA
S246-p RFHAQNLsQVEQDGR
S261 SGHGLRRSSKFCLKE
S262 GHGLRRSSKFCLKEH
Y326-p SAFNPLIyCRSPDFR
S345 ELLCLRRSSSKTYGN
S346 LLCLRRSSSKTYGNG
Y350 RRSSSKTYGNGYssN
Y354 SKTYGNGYssNSNGR
S355-p KTYGNGYssNSNGRT
S356-p TYGNGYssNSNGRTD
Y364 NSNGRTDYTGEPNTC
T365 SNGRTDYTGEPNTCQ
N369 TDYTGEPNTCQLGQE
M389 LCEDPPGMEGFVNCQ
T398 GFVNCQGTVPSLSVD
S401 NCQGTVPSLSVDSQG
S406 VPSLSVDSQGRNCST
S412 DSQGRNCSTNDSPL_
T413 SQGRNCSTNDSPL__
S416 RNCSTNDSPL_____
  rat

 
T68 FERLQTVTNYFITSL
Y132 CVIAVDRYVAITSPF
Y141 AITSPFKYQSLLTKN
Y219 LVVMVFVYSRVFQVA
S246 RFHAQNLSQVEQDGR
S261 SGHGLRSSSKFCLKE
S262 GHGLRSSSKFCLKEH
Y326 SAFNPLIYCRSPDFR
S345 ELLCLRRSSSKTYGN
S346 LLCLRRSSSKTYGNG
Y350 RRSSSKTYGNGYSSN
Y354 SKTYGNGYSSNSNGR
S355 KTYGNGYSSNSNGRT
S356 TYGNGYSSNSNGRTD
Y364 NSNGRTDYTGEQSAY
T365 SNGRTDYTGEQSAYQ
S369 TDYTGEQSAYQLGQE
M389 LCEEAPGMEGFVNCQ
T398 GFVNCQGTVPSLSID
S401 NCQGTVPSLSIDSQG
S406 VPSLSIDSQGRNCNT
N412 DSQGRNCNTNDSPL_
T413 SQGRNCNTNDSPL__
S416 RNCNTNDSPL_____
  hamster

 
T68 FERLQTVTNYFITSL
Y132-p CVIAVDRyIAITSPF
Y141-p AITSPFKyQSLLTKN
Y219 LVVMVFVYSRVFQVA
G246 RFHSPNLGQVEQDGR
S261-p SGHGLRRssKFCLKE
S262-p GHGLRRssKFCLKEH
Y326 SAFNPLIYCRSPDFR
S345 ELLCLRRSSSKAyGN
S346 LLCLRRSSSKAyGNG
Y350-p RRSSSKAyGNGySSN
Y354-p SKAyGNGySSNSNGK
S355 KAyGNGySSNSNGKT
S356 AyGNGySSNSNGKTD
Y364-p NSNGKTDyMGEASGC
M365 SNGKTDyMGEASGCQ
S369 TDyMGEASGCQLGQE
T389 LCEDPPGTESFVNCQ
T398 SFVNCQGTVPSLSLD
S401 NCQGTVPSLSLDSQG
S406 VPSLSLDSQGRNCST
S412 DSQGRNCSTNDSPL_
T413 SQGRNCSTNDSPL__
S416 RNCSTNDSPL_____
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.