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Gene Review

DYRK1A  -  dual-specificity tyrosine-(Y)...

Homo sapiens

Synonyms: DYRK, DYRK1, Dual specificity YAK1-related kinase, Dual specificity tyrosine-phosphorylation-regulated kinase 1A, HP86, ...
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Disease relevance of DYRK1A

  • In human, DYRK1A encodes a serine-threonine kinase but despite its potential involvement in the neurobiological alterations associated with Down syndrome, its physiological function has not yet been defined [1].
  • In neuroblastoma cells, Abeta induced an increase in the DYRK1A transcript, which also led to tau phosphorylation at Thr(212) under the overexpression of tau [2].
  • Consistent with our model, substitution of Tyr-321 but not of Tyr-319 by phenylalanine markedly reduced the enzymic activity of recombinant DYRK1A expressed in either Escherichia coli or mammalian cells [3].

Psychiatry related information on DYRK1A


High impact information on DYRK1A


Chemical compound and disease context of DYRK1A


Biological context of DYRK1A


Anatomical context of DYRK1A


Associations of DYRK1A with chemical compounds


Enzymatic interactions of DYRK1A

  • These experiments suggest that DYRK1A may phosphorylate FKHR at Ser(329) in vivo [17].
  • Here we describe the identification of DYRK1A as a protein kinase that phosphorylates SF3b1 in vitro and in cultivated cells [19].
  • In addition, Dyrk1 directly phosphorylates CREB, leading to the stimulation of subsequent CRE-mediated gene transcription during the neuronal differentiation in H19-7 cells [20].

Regulatory relationships of DYRK1A


Other interactions of DYRK1A

  • By fluorescence microscopy and subcellular fractionation, a green fluorescent protein (GFP) fusion protein of DYRK1A was found to accumulate in the nucleus of transfected COS-7 and HEK293 cells, whereas GFP-DYRK2 was predominantly detected in the cytoplasm [16].
  • Dual-specificity tyrosine-phosphorylated and regulated kinase 1A (DYRK1A) interacts with the phytanoyl-CoA alpha-hydroxylase associated protein 1 (PAHX-AP1), a brain specific protein [1].
  • A peptide designed after the optimal substrate sequence (DYRKtide) was efficiently phosphorylated by DYRK1A (K(m) = 35 microM) but not by ERK2 [13].
  • RESULTS: Overexpression of DYRK1A caused a markedly increased phosphorylation of SF3b1 in COS-7 cells as assessed by Western blotting with an antibody specific for phosphorylated Thr-Pro dipeptide motifs [19].
  • The protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation site [19].

Analytical, diagnostic and therapeutic context of DYRK1A

  • The information provided here should be valuable for MNBH mutation studies and aid in the development of DS animal models [22].
  • Fluorescence in situ hybridization and regional mapping data localize DYRK between markers D21S336 and D21S337 in the 21q22.2 region [23].
  • Northern blot analysis indicated that almost all the MNB/DYRK transcripts start from the newly identified 5'-noncoding exon [24].
  • PCR amplification of cDNAs from various human tissues indicated that some mRNAs contain an additional noncoding exon of 76 bp next to the 5'-end exon and there are at least three types of MNB/DYRK mRNAs containing alternatively spliced 5' exons including two novel exons [24].
  • This report describes the mapping of MNBH to a single locus on human chromosome 21q22.2 by FISH and Southern blotting [25].




  1. Dual-specificity tyrosine-phosphorylated and regulated kinase 1A (DYRK1A) interacts with the phytanoyl-CoA alpha-hydroxylase associated protein 1 (PAHX-AP1), a brain specific protein. Bescond, M., Rahmani, Z. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  2. The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between {beta}-amyloid production and tau phosphorylation in Alzheimer disease. Kimura, R., Kamino, K., Yamamoto, M., Nuripa, A., Kida, T., Kazui, H., Hashimoto, R., Tanaka, T., Kudo, T., Yamagata, H., Tabara, Y., Miki, T., Akatsu, H., Kosaka, K., Funakoshi, E., Nishitomi, K., Sakaguchi, G., Kato, A., Hattori, H., Uema, T., Takeda, M. Hum. Mol. Genet. (2007) [Pubmed]
  3. Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A. Himpel, S., Panzer, P., Eirmbter, K., Czajkowska, H., Sayed, M., Packman, L.C., Blundell, T., Kentrup, H., Grötzinger, J., Joost, H.G., Becker, W. Biochem. J. (2001) [Pubmed]
  4. Cloning and characterization of DYRK1B, a novel member of the DYRK family of protein kinases. Leder, S., Weber, Y., Altafaj, X., Estivill, X., Joost, H.G., Becker, W. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  5. DYRK1A BAC transgenic mice show altered synaptic plasticity with learning and memory defects. Ahn, K.J., Jeong, H.K., Choi, H.S., Ryoo, S.R., Kim, Y.J., Goo, J.S., Choi, S.Y., Han, J.S., Ha, I., Song, W.J. Neurobiol. Dis. (2006) [Pubmed]
  6. 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. Woods, Y.L., Cohen, P., Becker, W., Jakes, R., Goedert, M., Wang, X., Proud, C.G. Biochem. J. (2001) [Pubmed]
  7. A repressor complex, AP4 transcription factor and geminin, negatively regulates expression of target genes in nonneuronal cells. Kim, M.Y., Jeong, B.C., Lee, J.H., Kee, H.J., Kook, H., Kim, N.S., Kim, Y.H., Kim, J.K., Ahn, K.Y., Kim, K.K. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  8. DYRK1A enhances the mitogen-activated protein kinase cascade in PC12 cells by forming a complex with Ras, B-Raf, and MEK1. Kelly, P.A., Rahmani, Z. Mol. Biol. Cell (2005) [Pubmed]
  9. Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. Ferrer, I., Barrachina, M., Puig, B., Martínez de Lagrán, M., Martí, E., Avila, J., Dierssen, M. Neurobiol. Dis. (2005) [Pubmed]
  10. Dyrk1A potentiates steroid hormone-induced transcription via the chromatin remodeling factor Arip4. Sitz, J.H., Tigges, M., Baumgärtel, K., Khaspekov, L.G., Lutz, B. Mol. Cell. Biol. (2004) [Pubmed]
  11. MNB/DYRK1A phosphorylation regulates the interactions of synaptojanin 1 with endocytic accessory proteins. Adayev, T., Chen-Hwang, M.C., Murakami, N., Wang, R., Hwang, Y.W. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  12. Kinetic Properties of a MNB/DYRK1A Mutant Suitable for the Elucidation of Biochemical Pathways. Adayev, T., Chen-Hwang, M.C., Murakami, N., Wegiel, J., Hwang, Y.W. Biochemistry (2006) [Pubmed]
  13. Specificity determinants of substrate recognition by the protein kinase DYRK1A. Himpel, S., Tegge, W., Frank, R., Leder, S., Joost, H.G., Becker, W. J. Biol. Chem. (2000) [Pubmed]
  14. DYRK1A accumulates in splicing speckles through a novel targeting signal and induces speckle disassembly. Alvarez, M., Estivill, X., de la Luna, S. J. Cell. Sci. (2003) [Pubmed]
  15. Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases. Skurat, A.V., Dietrich, A.D. J. Biol. Chem. (2004) [Pubmed]
  16. Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases. Becker, W., Weber, Y., Wetzel, K., Eirmbter, K., Tejedor, F.J., Joost, H.G. J. Biol. Chem. (1998) [Pubmed]
  17. The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site. Woods, Y.L., Rena, G., Morrice, N., Barthel, A., Becker, W., Guo, S., Unterman, T.G., Cohen, P. Biochem. J. (2001) [Pubmed]
  18. Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors. de Graaf, K., Hekerman, P., Spelten, O., Herrmann, A., Packman, L.C., Büssow, K., Müller-Newen, G., Becker, W. J. Biol. Chem. (2004) [Pubmed]
  19. The protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation site. de Graaf, K., Czajkowska, H., Rottmann, S., Packman, L.C., Lilischkis, R., Lüscher, B., Becker, W. BMC Biochem. (2006) [Pubmed]
  20. Protein kinase Dyrk1 activates cAMP response element-binding protein during neuronal differentiation in hippocampal progenitor cells. Yang, E.J., Ahn, Y.S., Chung, K.C. J. Biol. Chem. (2001) [Pubmed]
  21. HAN11 binds mDia1 and controls GLI1 transcriptional activity. Morita, K., Celso, C.L., Spencer-Dene, B., Zouboulis, C.C., Watt, F.M. J. Dermatol. Sci. (2006) [Pubmed]
  22. Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome. Guimera, J., Casas, C., Estivill, X., Pritchard, M. Genomics (1999) [Pubmed]
  23. Isolation of human and murine homologues of the Drosophila minibrain gene: human homologue maps to 21q22.2 in the Down syndrome "critical region". Song, W.J., Sternberg, L.R., Kasten-Sportès, C., Keuren, M.L., Chung, S.H., Slack, A.C., Miller, D.E., Glover, T.W., Chiang, P.W., Lou, L., Kurnit, D.M. Genomics (1996) [Pubmed]
  24. Identification of two novel 5' noncoding exons in human MNB/DYRK gene and alternatively spliced transcripts. Wang, J., Kudoh, J., Shintani, A., Minoshima, S., Shimizu, N. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  25. Minibrain (MNBH) is a single copy gene mapping to human chromosome 21q22.2. Guimera, J., Pritchard, M., Nadal, M., Estivill, X. Cytogenet. Cell Genet. (1997) [Pubmed]
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