DUSP19

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).

Dual Specificity Phosphatase 19

Has a dual specificity toward Ser/Thr and Tyr-containing proteins.

Negative regulation of JNK cascade Source: BHF-UCL
Negative regulation of JUN kinase activity Source: BHF-UCL
Negative regulation of protein kinase activity Source: BHF-UCL
Positive regulation of JNK cascade Source: BHF-UCL
Positive regulation of JUN kinase activity Source: BHF-UCL
Positive regulation of MAPK cascade Source: BHF-UCL
Positive regulation of protein kinase activity Source: BHF-UCL
Regulation of MAP kinase activity Source: GO_Central

Cytoplasm