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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 NCBI)
Top mentioned proteins: cdc25, AP-1, SAPK, GST, ACID
Papers on SAPK pathway-regulating phosphatase 1
Crystal structure of a novel mitogen-activated protein kinase phosphatase, SKRP1.
Ryu et al., Seoul, South Korea. In Proteins, 2011
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
Molecular cloning and characterization of a novel human protein phosphatase, LMW-DSP3.
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]
A novel dual specificity phosphatase SKRP1 interacts with the MAPK kinase MKK7 and inactivates the JNK MAPK pathway. Implication for the precise regulation of the particular MAPK pathway.
Hagiwara et al., Tokyo, Japan. In J Biol Chem, 2002
We report the identification and characterization of a novel MKP termed SKRP1 (SAPK pathway-regulating phosphatase 1).
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