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DYRK2

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From Wikipedia, the free encyclopedia

Protein-coding gene in humans

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;OMA:DYRK2 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q15	Start	67,648,338bp^[1]
Band	12q15	End	67,665,406bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10\|10 D2	Start	118,691,508bp^[2]
Band	10\|10 D2	End	118,706,114bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

jejunal mucosa

mucosa of sigmoid colon

Skeletal muscle tissue of rectus abdominis

vastus lateralis muscle

pylorus

biceps brachii

Skeletal muscle tissue of biceps brachii

visceral pleura

right ventricle

hair follicle

Top expressed in

otolith organ

utricle

epithelium of lens

hand

knee joint

retinal pigment epithelium

left colon

hair follicle

digastric muscle

sternocleidomastoid muscle

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding protein kinase activity manganese ion binding kinase activity 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 nucleus nucleoplasm cytosol ribonucleoprotein complex
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: 118.69 – 118.71 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Dual specificity tyrosine-phosphorylation-regulated kinase 2 is anenzyme, in particular adual-specificity kinase, that in humans is encoded by theDYRK2gene.^[5]^[6]

DYRK2 belongs to a family of proteinkinases 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 toautophosphorylate on tyrosine residues. DYRK2 has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation ofhistones H3 and H2B in vitro. Twoisoforms of DYRK2 have been isolated. The predominant isoform, isoform 1, lacks a 5' terminal insert.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000127334 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000028630 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
^^a ^b"Entrez Gene: DYRK2 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2".

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.doi:10.1042/bj3550609.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.Bibcode:2002PNAS...9916899M.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.S2CID 27764390.
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.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
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.

Intracellular signaling peptides and proteins

MAP

seeMAP kinase pathway

Calcium

G protein

Heterotrimeric

cAMP:	Heterotrimeric G protein Gs/Gi Adenylate cyclase cAMP 3',5'-cyclic-AMP phosphodiesterase Protein kinase A
cGMP:	Transducin Gustducin Guanylate cyclase cGMP 3',5'-cyclic-GMP phosphodiesterase Protein kinase G
G alpha subunit G_α GNAO1 GNAI1 GNAI2 GNAI3 GNAT1 GNAT2 GNAT3 GNAZ GNAS GNAL GNAQ GNA11 GNA12 GNA13 GNA14 GNA15/GNA16
G beta-gamma complex G_β GNB1 GNB2 GNB3 GNB4 GNB5 G_γ GNGT1 GNGT2 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNG10 GNG11 GNG12 GNG13 BSCL2
G protein-coupled receptor kinase AMP-activated protein kinase

Monomeric

Cyclin

Lipid

Otherprotein kinase

Serine/threonine:	Casein kinase 1 2 eIF-2 kinase EIF2AK3 Glycogen synthase kinase GSK1 GSK2 GSK-3 GSK3A GSK3B IκB kinase CHUK IKK2 IKBKG Interleukin-1 receptor associated kinase IRAK1 IRAK2 IRAK3 IRAK4 Lim kinase LIMK1 LIMK2 p21-activated kinases PAK1 PAK2 PAK3 PAK4 Rho-associated protein kinase ROCK1 ROCK2 Ribosomal s6 kinase RPS6KA1
Tyrosine:	ZAP70 Focal adhesion protein-tyrosine kinase PTK2 PTK2B BTK
Serine/threonine/tyrosine	Dual-specificity kinase DYRK1A DYRK1B DYRK2 DYRK3 DYRK4
Arginine	Arginine kinase McsB

Otherprotein phosphatase

Serine/threonine:	Protein phosphatase 2
Tyrosine:	protein tyrosine phosphatase:Receptor-like protein tyrosine phosphatase Sh2 domain-containing protein tyrosine phosphatase
both:	Dual-specificity phosphatase