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: 10567225 
This page summarizes selected information from the article 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.
Navé BT, et al. (1999) Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem J 344 Pt 2, 427-31 10567225
Download Sites

S2448-p - mTOR (human)
Orthologous residues
mTOR (human): S2448‑p, mTOR (mouse): S2448‑p, mTOR (rat): S2448‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, phospho-antibody, phosphopeptide mapping, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], CHO (fibroblast) [EphB1 (human), transfection]
 Cellular systems studied:  cell lines
 Species studied:  hamster, human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
amino acid starvation decrease
insulin increase
rapamycin insulin no effect upon treatment-induced increase
wortmannin insulin inhibit treatment-induced increase
amino acid starvation insulin inhibit treatment-induced increase


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.