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)).
DUSP19; dual specificity phosphatase 19; dual specificity protein phosphatase 19; DUSP17; SKRP1; Dual specificity phosphatase TS DSP1; Dual specificity phosphatase TS-DSP1; DUS19_HUMAN; DUSP 17; DUSP 19; LMW DSP3; LMW-DSP3; LMWDSP 3; LMWDSP3; Low molecular weight dual specificity phosphatase 3; MGC138210; Protein phosphatase SKRP1; SAPK pathway regulating phosphatase 1; SAPK pathway-regulating phosphatase 1; SKRP 1; Stress activated protein kinase pathway regulating phosphatase 1; Stress-activated protein kinase pathway-regulating phosphatase 1; TS DSP1; TS-DSP1