DYRK2
{{Short description|Protein-coding gene in humans}}
{{Infobox_gene}}
Dual specificity tyrosine-phosphorylation-regulated kinase 2 is an enzyme, in particular a dual-specificity kinase, that in humans is encoded by the DYRK2 gene.{{cite journal | vauthors = Becker W, Weber Y, Wetzel K, Eirmbter K, Tejedor FJ, Joost HG | title = Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases | journal = J Biol Chem | volume = 273 | issue = 40 | pages = 25893–902 |date=Nov 1998 | pmid = 9748265 | doi =10.1074/jbc.273.40.25893 | doi-access = free }}{{cite web | title = Entrez Gene: DYRK2 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8445}}
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.
See also
References
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Further reading
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- {{cite journal | author=Woods YL |title=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 |journal=Biochem. J. |volume=355 |issue= Pt 3 |pages= 609–15 |year= 2001 |pmid= 11311121 |doi= 10.1042/bj3550609| pmc=1221774 |name-list-style=vanc| author2=Cohen P | author3=Becker W | display-authors=3 | last4=Jakes | first4=R | last5=Goedert | first5=M | last6=Wang | first6=X | last7=Proud | first7=CG }}
- {{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-style=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal | author=Wang X |title=The C Terminus of Initiation Factor 4E-Binding Protein 1 Contains Multiple Regulatory Features That Influence Its Function and Phosphorylation |journal=Mol. Cell. Biol. |volume=23 |issue= 5 |pages= 1546–57 |year= 2003 |pmid= 12588975 |doi=10.1128/MCB.23.5.1546-1557.2003 | pmc=151707 |name-list-style=vanc| author2=Li W | author3=Parra JL | display-authors=3 | last4=Beugnet | first4=A. | last5=Proud | first5=C. G. }}
- {{cite journal | vauthors=Skurat AV, Dietrich AD |title=Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases |journal=J. Biol. Chem. |volume=279 |issue= 4 |pages= 2490–8 |year= 2004 |pmid= 14593110 |doi= 10.1074/jbc.M301769200 |doi-access= free }}
- {{cite journal | author=Brandenberger R |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |name-list-style=vanc| author2=Wei H | author3=Zhang S | display-authors=3 | last4=Lei | first4=Shirley | last5=Murage | first5=Jaji | last6=Fisk | first6=Gregory J | last7=Li | first7=Yan | last8=Xu | first8=Chunhui | last9=Fang | first9=Rixun |s2cid=27764390 }}
- {{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-style=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
- {{cite journal | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |name-list-style=vanc| author2=Venkatesan K | author3=Hao T | display-authors=3 | last4=Hirozane-Kishikawa | first4=Tomoko | last5=Dricot | first5=Amélie | last6=Li | first6=Ning | last7=Berriz | first7=Gabriel F. | last8=Gibbons | first8=Francis D. | last9=Dreze | first9=Matija |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
- {{cite journal | author=Kimura K |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 |name-list-style=vanc| author2=Wakamatsu A | author3=Suzuki Y | display-authors=3 | last4=Ota | first4=T | last5=Nishikawa | first5=T | last6=Yamashita | first6=R | last7=Yamamoto | first7=J | last8=Sekine | first8=M | last9=Tsuritani | first9=K }}
- {{cite journal | author=Taira N |title=DYRK2 is targeted to the nucleus and controls p53 via Ser46 phosphorylation in the apoptotic response to DNA damage |journal=Mol. Cell |volume=25 |issue= 5 |pages= 725–38 |year= 2007 |pmid= 17349958 |doi= 10.1016/j.molcel.2007.02.007 |name-list-style=vanc| author2=Nihira K | author3=Yamaguchi T | display-authors=3 | last4=Miki | first4=Yoshio | last5=Yoshida | first5=Kiyotsugu |doi-access=free }}
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{{Intracellular signaling peptides and proteins}}
{{gene-12-stub}}