Dual specificity tyrosine-phosphorylation-regulated kinase 3 is an enzyme that in humans is encoded by the DYRK3gene.[1][2]
This gene product belongs to the DYRK family of dual-specificity protein kinases that catalyze autophosphorylation on serine/threonine and tyrosine residues. The members of this family share structural similarity, however, differ in their substrate specificity, suggesting their involvement in different cellular functions. The encoded protein has been shown to autophosphorylate on tyrosine residue and catalyze phosphorylation of histones H3 and H2B in vitro. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]
References
↑Becker W, Weber Y, Wetzel K, Eirmbter K, Tejedor FJ, Joost HG (Nov 1998). "Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases". J Biol Chem. 273 (40): 25893–902. doi:10.1074/jbc.273.40.25893. PMID9748265.
Zhang D, Li K, Erickson-Miller CL, et al. (2005). "DYRK gene structure and erythroid-restricted features of DYRK3 gene expression". Genomics. 85 (1): 117–30. doi:10.1016/j.ygeno.2004.08.021. PMID15607427.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID15592455.
Li K, Zhao S, Karur V, Wojchowski DM (2003). "DYRK3 activation, engagement of protein kinase A/cAMP response element-binding protein, and modulation of progenitor cell survival". J. Biol. Chem. 277 (49): 47052–60. doi:10.1074/jbc.M205374200. PMID12356771.
Lord KA, Creasy CL, King AG, et al. (2000). "REDK, a novel human regulatory erythroid kinase". Blood. 95 (9): 2838–46. PMID10779429.
Xia J, Yang X, Ruan Q, et al. (1999). "[Molecular cloning and characterization of novel protein kinase gene DYRK3]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 15 (6): 327–32. PMID9845759.
