Dual Specificity Phosphatase 18 (DUSP18)

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.

DUSP18 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. DUSP18 shares 70% and 49% amino acid identity with DUSP21 and DUSP14, respectively. Expression array and Northern blot analysis of human tissues detected DUSP18 expression in testis only. DUSP18 localized to both the nucleus and cytoplasm in transfected simian kidney cells.