Alternative titles; symbols
HGNC Approved Gene Symbol: DUSP21
Cytogenetic location: Xp11.3 Genomic coordinates (GRCh38) : X:44,844,021-44,844,888 (from NCBI)
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. DUSP21 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 600714) (summary by Patterson et al., 2009).
By EST database analysis, Hood et al. (2002) identified DUSP21, which they called LMWDSP21. The deduced 190-amino acid DUSP21 protein has a calculated molecular mass of 21.5 kD and contains the DUSP consensus motif and the conserved PTP signature motif and catalytic domain without the N-terminal CH2 domain. DUSP21 shares 70% and 44% amino acid identity with DUSP18 (611446) and DUSP14 (606618), respectively. Expression array and Northern blot analysis of human tissues detected DUSP21 expression in testis only. DUSP21 localized to both the nucleus and cytoplasm in transfected simian kidney cells.
Hood et al. (2002) demonstrated that DUSP21 displayed in vitro phosphotyrosine activity using phosphotyrosine analog pNPP as a substrate. Using synthetic MAPK phosphopeptides, they showed that DUSP21 displayed a preference for phosphotyrosine and dually phosphorylated peptides over a phosphothreonine peptide, with higher activity against JNK (MAPK8; 601158) and ERK (MAPK3; 601795) compared to p38 (MAPK14; 600289). However, in vivo assay of DUSP21 transfected into COS cells failed to detect DUSP21 phosphatase activity against any of the MAPK substrates tested.
Hood et al. (2002) determined that the DUSP21 gene contains 1 exon.
By genomic sequence analysis, Hood et al. (2002) mapped the DUSP21 gene to chromosome Xp11.4-p11.23.
Hood, K. L., Tobin, J. F., Yoon, C. Identification and characterization of two novel low-molecular-weight dual specificity phosphatases. Biochem. Biophys. Res. Commun. 298: 545-551, 2002. [PubMed: 12408986] [Full Text: https://doi.org/10.1016/s0006-291x(02)02488-9]
Patterson, K. I., Brummer, T., O'Brien, P. M., Daly, R. J. Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem. J. 418: 475-489, 2009. [PubMed: 19228121] [Full Text: https://doi.org/10.1042/bj20082234]