Aliases for DUSP13 Gene
External Ids for DUSP13 Gene
Previous GeneCards Identifiers for DUSP13 Gene
Members of the protein-tyrosine phosphatase superfamily cooperate with protein kinases to regulate cell proliferation and differentiation. This superfamily is separated into two families based on the substrate that is dephosphorylated. One family, the dual specificity phosphatases (DSPs) acts on both phosphotyrosine and phosphoserine/threonine residues. This gene encodes different but related DSP proteins through the use of non-overlapping open reading frames, alternate splicing, and presumed different transcription promoters. Expression of the distinct proteins from this gene has been found to be tissue specific and the proteins may be involved in postnatal development of specific tissues. A protein encoded by the upstream ORF was found in skeletal muscle, whereas the encoded protein from the downstream ORF was found only in testis. In mouse, a similar pattern of expression was found. Multiple alternatively spliced transcript variants were described, but the full-length sequence of only some were determined. [provided by RefSeq, Jul 2008]
GeneCards Summary for DUSP13 Gene
DUSP13 (Dual Specificity Phosphatase 13) is a Protein Coding gene. Diseases associated with DUSP13 include Ruvalcaba Syndrome and Cowden Syndrome. Gene Ontology (GO) annotations related to this gene include phosphatase activity and protein tyrosine/serine/threonine phosphatase activity. An important paralog of this gene is DUPD1.
UniProtKB/Swiss-Prot for DUSP13 Gene
Probable protein tyrosine phosphatase. Has phosphatase activity with synthetic substrates (PubMed:15252030, PubMed:29106959). Has a phosphatase activity-independent regulatory role in MAP3K5/ASK1-mediated apoptosis, preventing MAP3K5/ASK1 inhibition by AKT1. Shows no phosphatase activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and MAP3K5/ASK1.
Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro. Exhibits intrinsic phosphatase activity towards both phospho-seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro.