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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: Membrane protein, integral; Membrane protein, multi-pass; Receptor, GPCR; GPCR, family 1
Chromosomal Location of Human Ortholog: 5q31-q32
Cellular Component: endosome; integral to plasma membrane; lysosome; plasma membrane; receptor complex
Molecular Function: beta2-adrenergic receptor activity; epinephrine binding; norepinephrine binding; potassium channel regulator activity; protein binding; protein homodimerization activity
Biological Process: adenylate cyclase activation; arrestin mediated desensitization of G-protein coupled receptor protein signaling pathway; cell surface receptor linked signal transduction; cell-cell signaling; endosome to lysosome transport; G-protein signaling, coupled to cAMP nucleotide second messenger; negative regulation of smooth muscle contraction; norepinephrine-epinephrine vasodilation involved in regulation of systemic arterial blood pressure; positive regulation of MAPKKK cascade; positive regulation of protein ubiquitination; receptor-mediated endocytosis; transmembrane receptor protein tyrosine kinase activation (dimerization)
Disease: Asthma, Susceptibility To; Obesity
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.
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Sites Implicated In
cytoskeletal reorganization: S345‑p, S346‑p
activity, induced: 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
receptor recycling, inhibited: S345‑p, S346‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment



 LTP 

LTP: 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.


 HTP 

HTP: 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 9 S246‑p RFHVQNLsQVEQDGR
7 1 S261‑p TGHGLRRssKFCLKE
13 2 S262‑p GHGLRRssKFCLKEH
1 0 Y308‑p NLIRKEVyILLNWIG
4 0 Y326‑p SGFNPLIyCRSPDFR
9 1 S345‑p ELLCLRRssLKAyGN
10 2 S346‑p LLCLRRssLKAyGNG
8 0 Y350‑p RRssLKAyGNGyssN
5 0 Y354‑p LKAyGNGyssNGNtG
22 1 S355‑p KAyGNGyssNGNtGE
22 1 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‑p SGHGLRRssKFCLKE
S262‑p GHGLRRssKFCLKEH
Y308 NLIPKEVYILLNWLG
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‑p RFHAQNLsQVEQDGR
S261 SGHGLRSSSKFCLKE
S262 GHGLRSSSKFCLKEH
Y308 NLIPKEVYILLNWLG
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
Y308 NLIPKEVYILLNWLG
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_____
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