DUSP19 Gene

dual specificity phosphatase 19

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]

DUSP19 Gene Set

From DEPOD Substrates of Phosphatases

substrates of the phosphatase DUSP19 from the curated DEPOD Substrates of Phosphatases dataset.

DUSP19 Gene Set

From Pathway Commons Protein-Protein Interactions

interacting proteins for DUSP19 from the Pathway Commons Protein-Protein Interactions dataset.