Curated Information
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
Curated Information Page
PubMed Id: 11809767 
Doronin S, Shumay E, Wang HY, Malbon CC (2002) Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. J Biol Chem 277, 15124-31 11809767
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Download Sites

S346-p - ADRB2 (human)
Orthologous residues
ADRB2 (human): S346‑p, ADRB2 (mouse): S346‑p, ADRB2 (rat): S346‑p, ADRB2 (hamster): S346‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site, phospho-antibody, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  A431 (epithelial), CHO (fibroblast) [EphB1 (human), transfection]
 Cellular systems studied:  cell lines
 Species studied:  hamster, human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) genetic transfer of dominant-negative enzyme, genetic transfer of constitutively active upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
Downstream Regulation
 Effect of modification (function):  receptor desensitization, altered, receptor internalization, altered


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.