an oncogenic AGC kinase that plays a critical role in regulating cell survival and metabolism in many different signaling pathways. Dual phosphorylation is required for its activation. T308 is phosphorylated by PDK1 in the PI3 kinase pathway, and S473 is phosphorylated by mTOR in the mTORC2 pathway. The 'Lys-63'-linked ubiquitination of AKT1 by TRAF6 is important for its translocation to the plasma membrane, phosphorylation, and activation. When Akt is fully phosphorylated it translocates into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its proteosomal degradation. Hyperactive or overexpressed in a number of cancers including breast, prostate, lung, pancreatic, liver, ovarian and colorectal. Over 160 protein substrates are known including many that regulate transcription, metabolism, apoptosis, cell cycle, and growth. Note: This description may include information from UniProtKB.
Protein type: AGC group; AKT family; EC 188.8.131.52; Kinase, protein; Oncoprotein; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor)
Molecular Function: protein kinase activity; protein serine/threonine kinase activity
Biological Process: chitin-based embryonic cuticle biosynthetic process; cholesterol homeostasis; circadian rhythm; dendrite regeneration; epithelial cell migration, open tracheal system; insulin receptor signaling pathway; lipid metabolic process; multicellular organism growth; myoblast fusion; negative regulation of apoptosis; negative regulation of synaptic growth at neuromuscular junction; oogenesis; open tracheal system development; positive regulation of axon regeneration; positive regulation of cell growth; positive regulation of cell size; positive regulation of multicellular organism growth; positive regulation of organ growth; protein amino acid phosphorylation; regulation of cell shape; regulation of dendrite development; regulation of hemocyte proliferation; regulation of multicellular organism growth; regulation of protein import into nucleus; response to oxidative stress; sequestering of lipid; somatic muscle development