{"symbol":"DUSP18","synonyms":["DUSP20","DSP18","LMWDSP20"],"name":"dual specificity phosphatase 18","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. 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 (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]","ncbiEntrezGeneId":150290,"ncbiEntrezGeneUrl":"http://www.ncbi.nlm.nih.gov/gene/150290","proteins":[{"symbol":"DUS18_HUMAN","href":"/api/1.0/protein/DUS18_HUMAN"}],"hgncRootFamilies":[{"name":"Phosphatases","href":"/api/1.0/gene_family/Phosphatases"}]}