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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]).
Gene Name: | dual specificity phosphatase 18 |
Family/Subfamily: | Protein Phosphatase , LMW-DSP |
Synonyms: | DUSP18, BK963H5.1, DSP18, DUSP20, LMWDSP20, LMW-DSP20 |
Target Sequences: | NM_152511 NP_689724.3 Q8NEJ0 |
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