The p38 MAPK cascade regulates a variety of cellular responses to stress, inflammation, and other signals. p38 MAPK is relatively inactive in the nonphosphorylated form and becomes rapidly activated by dual phosphorylation of a Thr-Gly-Tyr motifs. There are four isoforms of p38 MAPK, which differ in their tissue expression and affinity for upstream activators and downstream effectors. When cells are exposed to tumor necrosis factor, interleukin-1, heat shock, or other activating stimuli, activation of MAPK kinase-3 occurs by phosphorylation. Activated MAPK kinase-3/6 phosphorylate each residue of Thr180 and Tyr182 in p38 MAPK. Phospho-p38 MAPK activates ATF-2, CHOP-1, MEF-2 and other transcription factors through phosphorylation.
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Protein Aliases: CSAID-binding protein; Csaids binding protein; cytokine suppressive anti-inflammatory drug binding protein; Cytokine suppressive anti-inflammatory drug-binding protein; MAP kinase 14; MAP kinase MXI2; MAP kinase p38 alpha; MAX-interacting protein 2; Mitogen-activated protein kinase 14; Mitogen-activated protein kinase p38 alpha; p38 MAP kinase; p38 mitogen activated protein kinase; p38alpha Exip; SAPK2a; Stress-activated protein kinase 2a
Gene Aliases: CSBP; CSBP1; CSBP2; CSPB1; EXIP; MAPK14; MXI2; p38; p38ALPHA; PRKM14; PRKM15; RK; SAPK2A
UniProt ID: (Human) Q16539
Molecular Function: non-receptor serine/threonine protein kinase