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]).[supplied by OMIM, Dec 2009]
Forensic Context
A study in humans identified the DUSP18 as a top differentially expressed gene when comparing the 7-day and 3-month post-acute myocardial infarction stages, and it showed a strong correlation (coefficient ≥0.8) with the metabolite HMDB0259626 [Wang et al. DOI:10.1038/s41598-024-60945-3].