Akt 1/2/3 (S473), Hck (Y411), PLC gamma-1 (Y783), Akt 1/2/3 (T308), HSP27 (S78/S82), PRAS40 (T246), AMPK alpha1 (T183), HSP60, Pyk2 (Y402), AMPK alpha2 (T172), JNK 1/2/3 (T183/Y185, T221/Y223), RSK1/2/3 (S380), beta-Catenin, Lck (Y394), Src (Y419), Chk-2 (T68), Lyn (Y397), STAT2 (Y689), c-Jun (S63), MSK1/2 (S376/S360), STAT3 (S727), CREB (S133), p27 (T198), STAT3 (Y705), EGF R (Y1086), p38 alpha (T180/Y182), STAT5a (Y699), eNOS (S1177), p53 (S15), STAT5a/b (Y699), ERK1/2 (T202/Y204, T185/Y187), p53 (S392), STAT5b (Y699), FAK (Y397), p53 (S46), STAT6 (Y641), Fgr (Y412), P70 S6 Kinase (T389), TOR (S2448), Fyn (Y420), p70 S6 Kinase (T421/S424), WNK-1 (T60), GSK-3 alpha/beta (S21/S9), PDGF R beta (Y751), Yes (Y426)
A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation). Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 518 protein kinase genes and they constitute about 2% of all human genes. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Protein kinases are also found in bacteria and plants, and include the pseudokinase sub-family, which exhibit unusual features including atypical nucleotide binding and weak, or no, catalytic activity and are part of a much larger pseudoenzyme group of 'degraded' enzyme relatives that are found throughout life, where they take an active participation in mechanistic cellular signaling.