Dual Specificity Phosphatase 19 (DUSP19)

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. The deduced 217-amino acid human protein contains the conserved DUSP active site motif, including a conserved cysteine residue. DUSP19 shares 81% amino acid identity with its mouse homolog. Northern blot analysis of mouse tissues detected high expression in heart, liver, kidney, and testis, and moderate expression in brain, placenta, lung, and small intestine.