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DUSP14
dual specificity phosphatase 14
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. DUSP14 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 14 |
| Family/Subfamily: | Protein Phosphatase , Dual specificity MKP |
| Synonyms: | DUSP14, DUSP 14, MKP-6, MKP-L, MAP kinase phosphatase 6, MKP6 |
| Target Sequences: | NM_007026 NP_008957.1 O95147 |
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