DYRK3

Dual specificity tyrosine-phosphorylation-regulated kinase 3 is an enzyme that in humans is encoded by the DYRK3 gene.[5][6]

DYRK3
Identifiers
Aliases	DYRK3, DYRK5, RED, REDK, hYAK3-2, dual specificity tyrosine phosphorylation regulated kinase 3
External IDs	OMIM: 603497 MGI: 1330300 HomoloGene: 55762 GeneCards: DYRK3
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q32.1 Start 206,635,536 bp[1] End 206,684,419 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 E4 Start 131,127,455 bp[2] End 131,138,340 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • protein kinase activity • protein serine/threonine/tyrosine kinase activity • protein tyrosine kinase activity • nucleotide binding • ATP binding • magnesium ion binding • metal ion binding • kinase activity • protein serine/threonine kinase activity Cellular component • cell nucleus • nucleoplasm • cytosol • intracellular membrane-bounded organelle • cytoplasm • Stress granule • pericentriolar material • microtubule organizing center • cytoskeleton • nuclear speck Biological process • erythrocyte differentiation • protein phosphorylation • peptidyl-tyrosine phosphorylation • phosphorylation • stress granule disassembly • negative regulation of apoptotic process • negative regulation of DNA damage response, signal transduction by p53 class mediator • regulation of cellular response to stress • regulation of TORC1 signaling • cell cycle • nuclear speck organization • cell division • positive regulation of cell cycle G2/M phase transition • organelle disassembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8444	226419
Ensembl	ENSG00000143479	ENSMUSG00000016526
UniProt	O43781	Q922Y0
RefSeq (mRNA)	NM_001004023 NM_003582	NM_145508
RefSeq (protein)	NP_001004023 NP_003573	NP_663483
Location (UCSC)	Chr 1: 206.64 – 206.68 Mb	Chr 1: 131.13 – 131.14 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000143479 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000016526 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: DYRK3 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3".

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.
• 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. S2CID 7200157.
• 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.
• 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. doi:10.1182/blood.V95.9.2838.009k29_2838_2846. 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.