plays a role in phosphatidylinositol 3-kinase (PI3K)/AKT survival signaling. PRAS40 is a physiological target of in vivo insulin action. Hyperinsulinemia increased its phosphorylation in human skeletal muscle biopsies. Phosphorylated PRAS40 is predominantly localized to the nucleus. In rats fed a high-fat diet (HFD), phosphorylation of PRAS40 was markedly reduced when compared with low-fat diet-fed animals in all tissues examined. A novel mTOR binding partner that mediates Akt signals to mTOR. Binding of PRAS40 inhibits mTOR activity and suppresses constitutive activation of mTOR in cells lacking TSC2. Phosphorylation by Akt and perhaps related kinases leads to its binding to 14-3-3. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Biological Process: negative regulation of cell size; negative regulation of protein kinase activity; negative regulation of TOR signaling pathway; regulation of apoptosis; regulation of neuron apoptosis