Tyr350
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Home > Phosphorylation Site Page: > Tyr350  -  ADRB2 (hamster)

Site Information
RRSSSKAyGNGySSN   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 449808

In vivo Characterization
Methods used to characterize site in vivo:
2D analysis ( 4 ) , [32P] bio-synthetic labeling ( 4 ) , immunoprecipitation ( 1 , 4 ) , mutation of modification site ( 1 , 2 , 4 ) , phospho-antibody ( 1 ) , phosphopeptide mapping ( 4 ) , western blotting ( 1 )
Relevant cell line - cell type - tissue:
A431 (epithelial) ( 1 ) , CHO (fibroblast) ( 2 ) , CHO (fibroblast) [EphB1 (human), transfection] ( 1 , 4 )

Upstream Regulation
Kinases, in vitro:
INSR (human) ( 3 , 4 )
Treatments:
insulin ( 2 , 4 ) , isoproterenol ( 1 , 4 )

Downstream Regulation
Effects of modification on ADRB2:
molecular association, regulation ( 1 ) , receptor desensitization, altered ( 1 )
Induce interaction with:
Src (mouse) ( 1 )

References 

1

Fan G, Shumay E, Malbon CC, Wang H (2001) c-Src tyrosine kinase binds the beta 2-adrenergic receptor via phospho-Tyr-350, phosphorylates G-protein-linked receptor kinase 2, and mediates agonist-induced receptor desensitization. J Biol Chem 276, 13240-7
11278940   Curated Info

2

Wang H, Doronin S, Malbon CC (2000) Insulin activation of mitogen-activated protein kinases Erk1,2 is amplified via beta-adrenergic receptor expression and requires the integrity of the Tyr350 of the receptor. J Biol Chem 275, 36086-93
10940302   Curated Info

3

Baltensperger K, et al. (1996) The beta-adrenergic receptor is a substrate for the insulin receptor tyrosine kinase. J Biol Chem 271, 1061-4
8557631   Curated Info

4

Karoor V, et al. (1995) Phosphorylation of tyrosyl residues 350/354 of the beta-adrenergic receptor is obligatory for counterregulatory effects of insulin. J Biol Chem 270, 25305-8
7592686   Curated Info