DUSP4

The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus. Two alternatively spliced transcript variants, encoding distinct isoforms, have been observed for this gene. In addition, multiple polyadenylation sites have been reported. [provided by RefSeq, Jul 2008]

Dual Specificity Phosphatase 4

Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.

Dephosphorylation Source: UniProtKB
Endoderm formation Source: GO_Central
Inactivation of MAPK activity Source: UniProtKB
Negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
Peptidyl-threonine dephosphorylation Source: UniProtKB
Peptidyl-tyrosine dephosphorylation Source: UniProtKB
Protein dephosphorylation Source: GO_Central

Nucleus

Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein.