Background：

Stress-activated serine/threonine-protein kinase involved in cytokine production， endocytosis， reorganization of the cytoskeleton， cell migration， cell cycle control， chromatin remodeling， DNA damage response and transcriptional regulation. Following stress， it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14， leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence， Hyd-X-R-X2-S， where Hyd is a large hydrophobic residue. Phosphorylates ALOX5， CDC25B， CDC25C， CEP131， ELAVL1， HNRNPA0， HSP27/HSPB1， KRT18， KRT20， LIMK1， LSP1， PABPC1， PARN， PDE4A， RCSD1， RPS6KA3， TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization， DNA-binding and transactivation activities. Mediates phosphorylation of HSP27/HSPB1 in response to stress， leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their ch