{"symbol":"DUSP19","synonyms":["LMWDSP3","TS-DSP1","DUSP17","SKRP1"],"name":"dual specificity phosphatase 19","description":"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]","ncbiEntrezGeneId":142679,"ncbiEntrezGeneUrl":"http://www.ncbi.nlm.nih.gov/gene/142679","proteins":[{"symbol":"DUS19_HUMAN","href":"/api/1.0/protein/DUS19_HUMAN"}],"hgncRootFamilies":[{"name":"Phosphatases","href":"/api/1.0/gene_family/Phosphatases"}]}