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Information on EC 2.7.12.1 - dual-specificity kinase and Organism(s) Rattus norvegicus and UniProt Accession Q63470

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IUBMB Comments
This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: Q63470
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
dyrk1a, dyrk2, dyrk1b, dual-specificity kinase, dyrk3, dual specificity kinase, dual-specificity tyrosine phosphorylation-regulated kinase 1a, dual-specificity protein kinase, dyrk1a kinase, dual specificity protein kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Clik1
-
-
-
0
dual specificity tyrosine-phosphorylated and regulated kinase 1A
266578
-
dual-specificity tyrosine phosphorylation-regulated kinase
248
-
dual-specificity tyrosine-phosphorylation regulated kinase 1A
266578
-
dual-specificity tyrosine-phosphorylation-regulated kinase
248
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DYRK
266578
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DYRK1A
protein kinase CLK3
266577
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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0
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating)
This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
CAS REGISTRY NUMBER
COMMENTARY hide
134549-83-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
?
ATP + histone
ADP + phosphorylated histone
show the reaction diagram
recombinant glutathione S-transferase-Dyrk/fusion protein catalyzes histone phosphorylation on tyrosine and Ser/Thr residues
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
show the reaction diagram
ATP + SR protein
ADP + ?
show the reaction diagram
might be a component of a signaling pathway regulating nuclear functions
-
-
?
ATP + dynamin 1
ADP + phosphorylated dynamin 1
show the reaction diagram
-
-
-
-
?
ATP + microtubule associated protein 1B
ADP + phosphorylated microtubule associated protein 1B
show the reaction diagram
-
DYRK1A phosphorylates the S1392 site on microtubule associated protein 1B
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
recombinant glutathione S-transferase-Dyrk fusion protein catalyzed autophosphorylation on tyrosine and serine/threonine residues
-
-
?
ATP + SR protein
ADP + ?
show the reaction diagram
enzyme regulates a predominately testicular function
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
?
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
show the reaction diagram
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55
-
-
?
ATP + SR protein
ADP + ?
show the reaction diagram
might be a component of a signaling pathway regulating nuclear functions
-
-
?
ATP + dynamin 1
ADP + phosphorylated dynamin 1
show the reaction diagram
-
-
-
-
?
ATP + microtubule associated protein 1B
ADP + phosphorylated microtubule associated protein 1B
show the reaction diagram
-
DYRK1A phosphorylates the S1392 site on microtubule associated protein 1B
-
-
?
ATP + SR protein
ADP + ?
show the reaction diagram
enzyme regulates a predominately testicular function
-
-
?
additional information
?
-
-
neither clathrin heavy chain nor endophilin 1 is phosphorylated by the Dyrk1A
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
predominately expressed in testis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
malfunction
-
knockdown of DYRK1A in cortical neurons disrupts neuritogenesis and alters microtubule stability
physiological function
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DYRK1A primes S1388, a glycogen synthase kinase 3beta phosphorylation sites on microtubule associated protein 1B
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DYR1A_RAT
763
0
85541
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
-
SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.4
-
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hydroxylapatite column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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