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. DUSP14 contains the consensus DUSP C-terminal catalytic domain but 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]).
Function
MAP kinase tyrosine/serine/threonine phosphatase activity; hydrolase activity; protein tyrosine phosphatase activity; protein tyrosine/serine/threonine phosphatase activity;
Synonyms
DUSP14; dual specificity phosphatase 14; dual specificity protein phosphatase 14; MKP 1 like protein tyrosine phosphatase; MKP L; MKP6; MKP-6; MAP kinase phosphatase 6; MKP-1 like protein tyrosine phosphatase; MKP-1-like protein tyrosine phosphatase; mitogen-activated protein kinase phosphatase 6; MKP-L;
Citations
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