AKT2

RAC-beta serine/threonine-protein kinase

RAC-beta serine/threonine-protein kinase ;
Protein kinase Akt-2 ;
Protein kinase B beta ;
PKB beta ;
RAC-PK-beta ;

catalytic activity:ATP + a protein = ADP + a phosphoprotein.,disease:Alterations of AKT2 may contribute to the pathogenesis of ovarian carcinomas.,enzyme regulation:Two specific sites, one in the kinase domain (Thr-309) and the other in the C-terminal regulatory region (Ser-474), need to be phosphorylated for its full activation.,function:General protein kinase capable of phosphorylating several known proteins.,similarity:Belongs to the protein kinase superfamily.,similarity:Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.,similarity:Contains 1 AGC-kinase C-terminal domain.,similarity:Contains 1 PH domain.,similarity:Contains 1 protein kinase domain.,subunit:Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B.,tissue specificity:In all human cell types so far analyzed.,

regulation of sodium ion transport, regulation of glycogen biosynthetic process, regulation of carbohydrate metabolic process, protein amino acid phosphorylation, phosphorus metabolic process, phosphate metabolic process, cell surface receptor linked signal transduction, enzyme linked receptor protein signaling pathway, transmembrane receptor protein tyrosine kinase signaling pathway, insulin receptor signaling pathway, response to endogenous stimulus, response to hormone stimulus, positive regulation of biosynthetic process, regulation of catabolic process,positive regulation of catabolic process, response to organic substance, positive regulation of macromolecule biosynthetic process, regulation of cellular ketone metabolic process, positive regulation of macromolecule metabolic process, regulation of protein kinase cascade, regulation of cellular carbohydrate metabolic process, positive regulation of cellular carbohydrate metabolic process, regulation of plasma membrane long-chain fatty acid transport,negative regulation of plasma membrane long-chain fatty acid transport, positive regulation of sodium ion transport,regulation of glucose transport, positive regulation of glucose transport, regulation of glucose metabolic process,positive regulation of glucose metabolic process, regulation of metal ion transport, regulation of glucan biosynthetic process, phosphorylation, regulation of lipid metabolic process, regulation of fatty acid metabolic process, positive regulation of cellular biosynthetic process, regulation of cellular catabolic process, positive regulation of cellular catabolic process, regulation of fatty acid beta-oxidation, positive regulation of fatty acid beta-oxidation, regulation of lipid transport, negative regulation of lipid transport, response to insulin stimulus, cellular response to insulin stimulus,cellular response to hormone stimulus, regulation of polysaccharide metabolic process, regulation of polysaccharide biosynthetic process, regulation of organic acid transport, negative regulation of organic acid transport, regulation of carbohydrate biosynthetic process, regulation of ion transport, positive regulation of ion transport, regulation of MAPKKK cascade, response to peptide hormone stimulus, regulation of generation of precursor metabolites and energy, positive regulation of glycogen biosynthetic process, positive regulation of lipid metabolic process, positive regulation of carbohydrate metabolic process, positive regulation of fatty acid metabolic process, regulation of fatty acid oxidation, positive regulation of fatty acid oxidation, regulation of glucose import, positive regulation of glucose import, regulation of JNK cascade, regulation of lipid catabolic process, positive regulation of lipid catabolic process,positive regulation of transport, negative regulation of transport, regulation of stress-activated protein kinase signaling pathway, regulation of cellular response to stress,

Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Early endosome . Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 in early endosomes (By similarity). .

Expressed in all cell types so far analyzed.