dual specificity phosphatase 14(DUSP14) Homo sapiens 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]).[supplied by OMIM, Dec 2009],
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Function:
Catalytic activity:A phosphoprotein + H(2)O = a protein + phosphate.,Catalytic activity:Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.,Function:Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.,similarity:Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.,similarity:Contains 1 tyrosine-protein phosphatase domain.,subunit:Interacts with CD28.,