{"symbol":"DUSP7","synonyms":["PYST2","MKPX"],"name":"dual specificity phosphatase 7","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. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]","ncbiEntrezGeneId":1849,"ncbiEntrezGeneUrl":"http://www.ncbi.nlm.nih.gov/gene/1849","proteins":[{"symbol":"DUS7_HUMAN","href":"/api/1.0/protein/DUS7_HUMAN"}],"hgncRootFamilies":[{"name":"Phosphatases","href":"/api/1.0/gene_family/Phosphatases"}]}