DYRK2

Dual specificity tyrosine-phosphorylation-regulated kinase 2 is an enzyme that in humans is encoded by the DYRK2 gene.[5][6]

DYRK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3K2L, 3KVW, 4AZF
Identifiers
Aliases	DYRK2, dual specificity tyrosine phosphorylation regulated kinase 2
External IDs	OMIM: 603496 MGI: 1330301 HomoloGene: 48437 GeneCards: DYRK2
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q15 Start 67,648,338 bp[1] End 67,665,406 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10|10 D2 Start 118,855,603 bp[2] End 118,870,209 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • manganese ion binding • kinase activity • GO:0001948 protein binding • protein serine/threonine/tyrosine kinase activity • protein tyrosine kinase activity • ATP binding • magnesium ion binding • protein serine/threonine kinase activity Cellular component • cytoplasm • ubiquitin ligase complex • cell nucleus • nucleoplasm • cytosol • ribonucleoprotein Biological process • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator • positive regulation of glycogen biosynthetic process • phosphorylation • cellular response to DNA damage stimulus • protein phosphorylation • smoothened signaling pathway • apoptotic process • regulation of signal transduction by p53 class mediator • peptidyl-tyrosine phosphorylation • negative regulation of calcineurin-NFAT signaling cascade Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8445	69181
Ensembl	ENSG00000127334	ENSMUSG00000028630
UniProt	Q92630	Q5U4C9
RefSeq (mRNA)	NM_006482 NM_003583	NM_001014390
RefSeq (protein)	NP_003574 NP_006473	NP_001014412
Location (UCSC)	Chr 12: 67.65 – 67.67 Mb	Chr 10: 118.86 – 118.87 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

DYRK2 belongs to a family of protein kinases whose members are presumed to be involved in cellular growth and 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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000127334 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028630 - 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: DYRK2 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2".

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.
• 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.
• 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.
• 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.
• 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.
• 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.