Dual specificity phosphatase 19 (DUSP19)

Dual specificity phosphatase 19 (DUSP19) is an atypical member of the dual-specificity phosphatase subfamily, itself part of the type I cysteine-based protein tyrosine phosphatase (PTP) superfamily. It is distinguished by its ability to dephosphorylate both tyrosine and serine/threonine residues on protein substrates. DUSP19 lacks the N-terminal CH2 domain found in the mitogen-activated protein kinase phosphatase (MKP) class but contains a variant catalytic domain, with a unique active site structure compared to other DUSPs. It has been implicated as a modulator of critical cell signaling pathways, particularly MAP kinase cascades, and may have specialized scaffold functions regulating MAPK pathway assembly and activation. Clinical associations include rare genetic diseases such as congenital ichthyosis and myoclonic epilepsy of Lafora 1. There are currently no approved or experimental drugs that selectively target DUSP19, and its precise physiological substrates and cellular functions continue to be defined.

Other names

DUSP17SKRP1Stress-Activated Protein Kinase Pathway-Regulating Phosphatase 1Low Molecular Weight Dual Specificity Phosphatase 3SAPK Pathway-Regulating Phosphatase 1Dual specificity protein phosphatase 19

No known mechanism of drug action as DUSP19 is not currently a direct pharmacological target