MAPK6

The protein encoded by this gene is a member of the Ser/Thr protein kinase family, and is most closely related to mitogen-activated protein kinases (MAP kinases). MAP kinases also known as extracellular signal-regulated kinases (ERKs), are activated through protein phosphorylation cascades and act as integration points for multiple biochemical signals. This kinase is localized in the nucleus, and has been reported to be activated in fibroblasts upon treatment with serum or phorbol esters. [provided by RefSeq, Jul 2008]

Mitogen-Activated Protein Kinase 6

Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6. May promote entry in the cell cycle (By similarity).

Cell cycleIEA:UniProtKB-KW
Intracellular signal transductionManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of dendritic spine developmentIEA:Ensembl
Protein phosphorylationISS:UniProtKB
Signal transductionManual Assertion Based On ExperimentTAS:ProtInc

Cytoplasm
Nucleus
Translocates to the cytoplasm following interaction with MAPKAPK5.

Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in catalytic activation. Phosphorylated by MAPKAPK5 at other sites.
Ubiquitination at Met-1 leads to degradation by the proteasome pathway.