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Literature summary for 2.7.12.1 extracted from

  • 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 (2012), J. Biol. Chem., 287, 30497-30506.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
K188R a dominant negative, inactive Dyrk1A mutant Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Rattus norvegicus 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + a protein Rattus norvegicus
-
ADP + a phosphoprotein
-
?
ATP + serine/arginine-rich protein 55 Rattus norvegicus i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55 ADP + phospho-serine/arginine-rich protein 55
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus Q63470
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a protein
-
Rattus norvegicus ADP + a phosphoprotein
-
?
ATP + serine/arginine-rich protein 55 i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55 Rattus norvegicus ADP + phospho-serine/arginine-rich protein 55
-
?
ATP + 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 Rattus norvegicus ADP + phospho-serine/arginine-rich protein 55
-
?

Synonyms

Synonyms Comment Organism
dual specificity tyrosine-phosphorylated and regulated kinase 1A
-
Rattus norvegicus
DYRK1A
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Rattus norvegicus

General Information

General Information Comment Organism
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 Rattus norvegicus
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 Rattus norvegicus