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Gene Family: Dual specificity phosphatases (DUSP)

Also known as : "Class I dual specificity Cys-based phosphatases"

Dual-specificity phosphatase: Dual-specificity phosphatase is a form of phosphatase that can act upon tyrosine or serine / threonine residues. All [DUSPs] share a similar catalytic mechanism, by which a conserved cysteine residue forms a covalent intermediate with the phosphate group to be eliminated. The residues surrounding their calatytic core obey a rather strict consensus: His-Cys-x-x-x-x-x-Arg-Ser. The serine side chain and an additional conserved aspartate play a central role in the elimination of the Cys-linked intermediate, thus completing their enzymatic cycle. The main difference between tyrosine-specific phosphatases and dual-specificity phosphatases lies in the width of the latter enzymes' catalytic pocket: thus they can accommodate phosphorylated serine or threonine side chains as well as phosphorylated tyrosines. [Source: Wikipedia]

Family contains the following subsets

Genes contained within subsets

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