DUSP23

Dual specificity phosphatase 23
PDB rendering based on 2img.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2IMG​, 4ERC​
Identifiers
Symbols	DUSP23 ; DUSP25; LDP-3; MOSP; VHZ
External IDs	MGI: 1915690 HomoloGene: 32368 GeneCards: DUSP23 Gene
EC number	3.1.3.16, 3.1.3.48
Gene ontology Molecular function • protein tyrosine phosphatase activity • protein binding • protein tyrosine/serine/threonine phosphatase activity Cellular component • nucleus • cytosol • extracellular exosome Biological process • peptidyl-tyrosine dephosphorylation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	54935	68440
Ensembl	ENSG00000158716	ENSMUSG00000026544
UniProt	Q9BVJ7	Q6NT99
RefSeq (mRNA)	NM_017823	NM_026725
RefSeq (protein)	NP_060293	NP_081001
Location (UCSC)	Chr 1: 159.78 – 159.78 Mb	Chr 1: 172.63 – 172.63 Mb
PubMed search

Dual specificity protein phosphatase 23, also known as low molecular mass dual specificity phosphatase 3 (LDP-3), is an enzyme (EC 3.1.3.16 and EC 3.1.3.48) that in humans is encoded by the DUSP23 gene.^[1][2]

References

1. "Entrez Gene: dual specificity phosphatase 23".
2. Wu Q, Li Y, Gu S, Li N, Zheng D, Li D, Zheng Z, Ji C, Xie Y, Mao Y (August 2004). "Molecular cloning and characterization of a novel dual-specificity phosphatase 23 gene from human fetal brain". Int. J. Biochem. Cell Biol. 36 (8): 1542–53. doi:10.1016/j.biocel.2003.12.014. PMID 15147733.

Further reading

• Talmud PJ, Drenos F, Shah S; et al. (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.". Am. J. Hum. Genet. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121.
• Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
• Liu CY, Wu MC, Chen F; et al. (2010). "A Large-scale genetic association study of esophageal adenocarcinoma risk.". Carcinogenesis 31 (7): 1259–63. doi:10.1093/carcin/bgq092. PMC 2893800. PMID 20453000.
• Alonso A, Burkhalter S, Sasin J; et al. (2004). "The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ.". J. Biol. Chem. 279 (34): 35768–74. doi:10.1074/jbc.M403412200. PMID 15201283.
• Takagaki K, Satoh T, Tanuma N; et al. (2004). "Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38.". Biochem. J. 383 (Pt. 3): 447–55. doi:10.1042/BJ20040498. PMC 1133737. PMID 15281913.
• Bailey SD, Xie C, Do R; et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.". Diabetes Care 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.
• Tang JP, Tan CP, Li J; et al. (2010). "VHZ is a novel centrosomal phosphatase associated with cell growth and human primary cancers.". Mol. Cancer 9: 128. doi:10.1186/1476-4598-9-128. PMC 2893100. PMID 20509867.