DYRK2

From Wikipedia, the free encyclopedia

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2

Identifiers

External IDs

OMIM: 603496 MGI: 1330301 HomoloGene: 48437

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • protein-tyrosine kinase activity • ATP binding • transferase activity • manganese ion binding
Cellular Component:	• cytoplasm
Biological Process:	• protein amino acid phosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_003583 (mRNA)
NP_003574 (protein)

XM_972916 (mRNA)
XP_978010 (protein)

Location

Chr 12: 66.33 - 66.34 Mb

Chr 10: 118.26 - 118.27 Mb

Pubmed search

[1]

[2]

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2, also known as DYRK2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: DYRK2 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2.

[edit] Further reading

Becker W, Weber Y, Wetzel K, et al. (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. PMID 9748265.
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. 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. 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. 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. 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. 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.