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dual specificity phosphatase 19(DUSP19) 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. 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]).[supplied by OMIM, Dec 2009],catalytic activity:A phosphoprotein + H(2)O = a protein + phosphate.,catalytic activity:Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.,function:Has a dual specificity toward Ser/Thr and Tyr-containing proteins.,similarity:Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.,similarity:Contains 1 tyrosine-protein phosphatase domain.,tissue specificity:Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest.,

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