DYRK2

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2
Rendering based on PDB 3K2L.
Available structures PDB 3K2L, 3KVW
Identifiers
Symbols	DYRK2; FLJ21217; FLJ21365
External IDs	OMIM: 603496 MGI: 1330301 HomoloGene: 48437 GeneCards: DYRK2 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 • ATP binding • manganese ion binding Cellular component • nucleus • nucleolus • cytoplasm • intracellular membrane-bounded organelle Biological process • protein phosphorylation • apoptosis • smoothened signaling pathway • DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis • positive regulation of glycogen biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8445	69181
Ensembl	ENSG00000127334	ENSMUSG00000028630
UniProt	Q92630	n/a
RefSeq (mRNA)	NM_003583.3	NM_001014390.2
RefSeq (protein)	NP_003574.1	NP_001014412.1
Location (UCSC)	Chr 12: 68.04 – 68.06 Mb	Chr 10: 118.3 – 118.31 Mb
PubMed search	[1]	[2]

Dual specificity tyrosine-phosphorylation-regulated kinase 2 is an enzyme that in humans is encoded by the DYRK2 gene.^[1][2]

DYRK2 belongs to a family of protein kinases whose members are presumed to be involved in cellular growth and/or development. The family is defined by structural similarity of their kinase domains and their capability to autophosphorylate on tyrosine residues. DYRK2 has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation of histones H3 and H2B in vitro. Two isoforms of DYRK2 have been isolated. The predominant isoform, isoform 1, lacks a 5' terminal insert.^[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: DYRK2 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8445. 

Further reading

• Woods YL, Cohen P, Becker W et al. (2001). "The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase". Biochem. J. 355 (Pt 3): 609–15. PMC 1221774. PMID 11311121. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1221774. 
• 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. 
• Wang X, Li W, Parra JL et al. (2003). "The C Terminus of Initiation Factor 4E-Binding Protein 1 Contains Multiple Regulatory Features That Influence Its Function and Phosphorylation". Mol. Cell. Biol. 23 (5): 1546–57. doi:10.1128/MCB.23.5.1546-1557.2003. PMC 151707. PMID 12588975. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151707. 
• Skurat AV, Dietrich AD (2004). "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases". J. Biol. Chem. 279 (4): 2490–8. doi:10.1074/jbc.M301769200. PMID 14593110. 
• Brandenberger R, Wei H, Zhang S et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
• Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• 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. 
• Taira N, Nihira K, Yamaguchi T et al. (2007). "DYRK2 is targeted to the nucleus and controls p53 via Ser46 phosphorylation in the apoptotic response to DNA damage". Mol. Cell 25 (5): 725–38. doi:10.1016/j.molcel.2007.02.007. PMID 17349958.