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EC Tree
IUBMB Comments This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
The taxonomic range for the selected organisms is: Rattus norvegicus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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a [protein]-(L-serine/L-threonine)
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a [protein]-(L-serine/L-threonine) phosphate
Synonyms
dyrk1a, dyrk2, dyrk1b, dyrk3, dual-specificity kinase, dyrk1, dual specificity kinase, dual-specificity tyrosine phosphorylation-regulated kinase 1a, dual-specificity protein kinase, dyrk1a kinase,
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dual specificity tyrosine-phosphorylated and regulated kinase 1A
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dual-specificity tyrosine phosphorylation-regulated kinase
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dual-specificity tyrosine-phosphorylation regulated kinase 1A
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dual-specificity tyrosine-phosphorylation-regulated kinase
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DYRK1A
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phospho group transfer
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ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating)
This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
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ATP + protein
ADP + phosphoprotein
recombinant glutathione S-transferase-Dyrk fusion protein catalyzed autophosphorylation on tyrosine and serine/threonine residues
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ATP + SR protein
ADP + ?
enzyme regulates a predominately testicular function
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ATP + a protein
ADP + a phosphoprotein
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ATP + dynamin 1
ADP + phosphorylated dynamin 1
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ATP + histone
ADP + phosphorylated histone
recombinant glutathione S-transferase-Dyrk/fusion protein catalyzes histone phosphorylation on tyrosine and Ser/Thr residues
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ATP + microtubule associated protein 1B
ADP + phosphorylated microtubule associated protein 1B
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DYRK1A phosphorylates the S1392 site on microtubule associated protein 1B
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ATP + protein
ADP + phosphoprotein
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
ATP + SR protein
ADP + ?
might be a component of a signaling pathway regulating nuclear functions
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?
additional information
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ATP + protein
ADP + phosphoprotein
autophosphorylation
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ATP + protein
ADP + phosphoprotein
when expressed in E. coli the enzyme catalyzes autophosphorylation on Tyr residues
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ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55
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ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55. Dyrk1A phosphorylation sites are Ser280, Ser303, and Ser316
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additional information
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a glutathione S-transferase fusion protein of Clk3 catalyzes autophosphorylation of the kinase but not phosphorylation of the exogenous substrates histone or casein
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additional information
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activity is dependent on tyrosine residues between subdomains VII and VIII
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additional information
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neither clathrin heavy chain nor endophilin 1 is phosphorylated by the Dyrk1A
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ATP + SR protein
ADP + ?
enzyme regulates a predominately testicular function
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ATP + a protein
ADP + a phosphoprotein
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ATP + dynamin 1
ADP + phosphorylated dynamin 1
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ATP + microtubule associated protein 1B
ADP + phosphorylated microtubule associated protein 1B
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DYRK1A phosphorylates the S1392 site on microtubule associated protein 1B
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ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55
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?
ATP + SR protein
ADP + ?
might be a component of a signaling pathway regulating nuclear functions
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?
additional information
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neither clathrin heavy chain nor endophilin 1 is phosphorylated by the Dyrk1A
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?
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ATP
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SwissProt
brenda
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predominately expressed in testis
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malfunction
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knockdown of DYRK1A in cortical neurons disrupts neuritogenesis and alters microtubule stability
malfunction
overexpression of Dyrk1A does not affect Tau exon 10 inclusion, whereas the expression of dominant negative Dyrk1A, Dyrk1AK188R, which results in the loss of its kinase activity, significantly promotes Tau exon10 inclusion
physiological function
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DYRK1A primes S1388, a glycogen synthase kinase 3beta phosphorylation sites on microtubule associated protein 1B
physiological function
enzyme Dyrk1A regulates the pre-mRNA alternative splicing of Tau through splicing factors. Dyrk1A interacts with SRp55 through its RRM domain, phosphorylates its proline-rich domain and inhibits its ability to promote Tau exon 10 inclusion. Upregulation of Dyrk1A disrupts the alternative splicing of Tau exon 10, which encodes the second microtubule-binding repeat. Tau 10 alternative splicing generates Tau isoforms with three- or four-microtubule-binding repeats, named 3R-tau and 4R-tau Dysregulation of the alternative splicing of Tau exon 10 causes several types of neurodegenerative diseases, e.g. neurofibrillary degeneration
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CLK3_RAT
490
0
58485
Swiss-Prot
other Location (Reliability: 4 )
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phosphoprotein
autophosphorylation
phosphoprotein
dual specificity protein kinase that is regulated by tyrosine phosphorylation in the activation loop
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K188R
a dominant negative, inactive Dyrk1A mutant
additional information
exchange of two Tyr residues in the activation loop between subdomains VII and VIII for Phe almost completely suppresses the activity and Tyr autophosphorylation of Dyrk. Tyr autophosphorylation is also reduced by exchange of Tyr219 in a tyrosine phosphorylation consensus motif
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6.5 - 7.4
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the kinase is resistant to high salt and Triton X-100 extraction at pH 6.5. At pH 7.4, the kinase becomes soluble to some extent after treatment with Triton X-100 and 1.0 M NaCl
702352
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Triton X-100
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the kinase is resistant to high salt and Triton X-100 extraction at pH 6.5. At pH 7.4, the kinase becomes soluble to some extent after treatment with Triton X-100 and 1.0 M NaCl
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hydroxylapatite column chromatography
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fusion protein of DYRK1A accumulates in the nucleus of transfected COS-7 and HEK293 cells, expression in Escherichia coli
gene dyrk1A, Dyrk1A and HA-tagged SRp55 are cotransfected into HEK-293FT cells for 48 h, and SRp55 is immunoprecipitated with anti-HA antibodies. Dyrk1A is coimmunoprecipitated by SRp55. SRp55 interacts with Dyrk1A through its RRM domain. DYRK1A and SRp55 coexpression and colocalization in HeLA cell nuclei
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Becker, W.; Weber, Y.; Wetzel, K.; Eirmbter, K.; Tejedor, F.J.; Joost, H.G.
Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases
J. Biol. Chem.
273
25893-25902
1998
Homo sapiens (O43781), Homo sapiens (Q92630), Rattus norvegicus (Q63470)
brenda
Becker, W.; Kentrup, H.; Heukelbach, J.; Joost, H.G.
cDNA cloning and characterization of rat Clk3, a LAMMER kinase predominately expressed in testis
Biochim. Biophys. Acta
1312
63-67
1996
Rattus norvegicus (Q63117)
brenda
Kentrup, H.; Becker, W.; Heukelbach, J.; Wilmes, A.; Schurmann, A.; Huppertz, C.; Kainulainen, H.; Joost, H.G.
Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII
J. Biol. Chem.
271
3488-3495
1996
Rattus norvegicus (Q63470)
brenda
Murakami, N.; Bolton, D.; Hwang, Y.W.
Dyrk1A binds to multiple endocytic proteins required for formation of clathrin-coated vesicles
Biochemistry
48
9297-305
2009
Rattus norvegicus
brenda
Scales, T.M.; Lin, S.; Kraus, M.; Goold, R.G.; Gordon-Weeks, P.R.
Nonprimed and DYRK1A-primed GSK3 beta-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons
J. Cell Sci.
122
2424-2435
2009
Rattus norvegicus
brenda
Yin, X.; Jin, N.; Gu, J.; Shi, J.; Zhou, J.; Gong, C.-X.; Iqbal, K.; Grundke-Iqbal, I.; Liu, F.
Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10 inclusion
J. Biol. Chem.
287
30497-30506
2012
Rattus norvegicus (Q63470)
brenda