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1 See also  





2 References  





3 Further reading  














DYRK3






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DYRK3
Identifiers
AliasesDYRK3, DYRK5, RED, REDK, hYAK3-2, dual specificity tyrosine phosphorylation regulated kinase 3
External IDsOMIM: 603497; MGI: 1330300; HomoloGene: 55762; GeneCards: DYRK3; OMA:DYRK3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001004023
NM_003582

NM_145508

RefSeq (protein)

NP_001004023
NP_003573

NP_663483

Location (UCSC)Chr 1: 206.64 – 206.68 MbChr 1: 131.06 – 131.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dual specificity tyrosine-phosphorylation-regulated kinase 3 is an enzyme that in humans is encoded by the DYRK3 gene.[5][6]

This gene product belongs to the DYRK family of dual-specificity protein kinases that catalyze autophosphorylationonserine/threonine and tyrosine residues. The members of this family share structural similarity, however, differ in their substrate specificity, suggesting their involvement in different cellular functions. The encoded protein has been shown to autophosphorylate on tyrosine residue and catalyze phosphorylation of histones H3 and H2B in vitro. Alternatively spliced transcript variants encoding different isoforms have been identified.[6]

See also[edit]

References[edit]

  • ^ "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: DYRK3 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3".
  • Further reading[edit]

  • Zhang D, Li K, Erickson-Miller CL, et al. (2005). "DYRK gene structure and erythroid-restricted features of DYRK3 gene expression". Genomics. 85 (1): 117–30. doi:10.1016/j.ygeno.2004.08.021. PMID 15607427.
  • Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • 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.
  • Li K, Zhao S, Karur V, Wojchowski DM (2003). "DYRK3 activation, engagement of protein kinase A/cAMP response element-binding protein, and modulation of progenitor cell survival". J. Biol. Chem. 277 (49): 47052–60. doi:10.1074/jbc.M205374200. PMID 12356771.
  • Lord KA, Creasy CL, King AG, et al. (2000). "REDK, a novel human regulatory erythroid kinase". Blood. 95 (9): 2838–46. doi:10.1182/blood.V95.9.2838.009k29_2838_2846. PMID 10779429.
  • Xia J, Yang X, Ruan Q, et al. (1999). "[Molecular cloning and characterization of novel protein kinase gene DYRK3]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 15 (6): 327–32. PMID 9845759.

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  • Retrieved from "https://en.wikipedia.org/w/index.php?title=DYRK3&oldid=1130181635"

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