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Dual specificity phosphatase 19
SAPK pathway-regulating phosphatase 1, LMW-DSP3
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] (from
crystal structure of SKRP1 (C150S) has been determined and refined at 1.26 A resolution (Table I). The structure reveals 142 residues (residues 65-206) of SKRP1 and three ions (two sulfates and one phosphate) at the catalytic site
Mao et al., Shanghai, China. In Int J Biochem Cell Biol, 2003
LMW-DSP3 was expressed in the heart, lung, liver, and pancreas, and the expression level in the pancreas was highest. The LMW-DSP3 gene was located in human chromosome 2q32, and consisted of five exons spanning 21kb of human genomic DNA[LMW-DSP3]