DYRK3

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3
Identifiers
Symbols	DYRK3; DYRK5; RED; REDK; hYAK3-2
External IDs	OMIM: 603497 MGI: 1330300 HomoloGene: 55762 GeneCards: DYRK3 Gene
EC number	2.7.12.1
Gene Ontology Molecular function • nucleotide binding • magnesium ion binding • protein kinase activity • protein serine/threonine kinase activity • protein tyrosine kinase activity • protein binding • ATP binding Cellular component • nucleus Biological process • protein phosphorylation • erythrocyte differentiation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8444	226419
Ensembl	ENSG00000143479	ENSMUSG00000016526
UniProt	O43781	n/a
RefSeq (mRNA)	NM_001004023.1	NM_145508.2
RefSeq (protein)	NP_001004023.1	NP_663483.1
Location (UCSC)	Chr 1: 206.81 – 206.86 Mb	Chr 1: 133.03 – 133.03 Mb
PubMed search	[1]	[2]

Dual specificity tyrosine-phosphorylation-regulated kinase 3 is an enzyme that in humans is encoded by the DYRK3 gene.^[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

1. ^ 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. PMID 9748265. 
2. ^ ^{a b} "Entrez Gene: DYRK3 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8444. 

Further reading

• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• 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. PMID 15607427. 
• 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. PMID 15592455. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. PMID 12356771. 
• Lord KA, Creasy CL, King AG, et al. (2000). "REDK, a novel human regulatory erythroid kinase.". Blood 95 (9): 2838–46. PMID 10779429. 
• 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. PMID 9845759.