Dual Specificity Phosphatase 14 (DUSP14)

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.Binding and deletion analyses established that the interaction between the cytoplasmic tail of CD28 and DUSP14 occurs at tyr200 of CD28 and is specific for both partners; however, tyr200 could be mutated to phe200 without a loss of binding ability.