DYRK3

From Wikipedia, the free encyclopedia

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3

Identifiers

DYRK3; RED; DYRK5; REDK

External IDs

OMIM: 603497 MGI: 1330300 HomoloGene: 55762

Gene ontology
Molecular Function:	• nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • protein-tyrosine kinase activity • ATP binding • transferase activity
Biological Process:	• protein amino acid phosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_001004023 (mRNA)
NP_001004023 (protein)

NM_145508 (mRNA)
NP_663483 (protein)

Location

Chr 1: 204.88 - 204.92 Mb

Chr 1: 132.96 - 132.97 Mb

Pubmed search

[1]

[2]

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3, also known as DYRK3, is a human gene.^[1]

This gene product belongs to the DYRK family of dual-specificity protein kinases that catalyze autophosphorylation on serine/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.^[1]

[edit] References

^ ^a ^b Entrez Gene: DYRK3 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3.

[edit] Further reading

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.
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.
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.
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. 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.
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.