Literature summary for 2.7.12.1 extracted from

Qian, W.; Jin, N.; Shi, J.; Yin, X.; Jin, X.; Wang, S.; Cao, M.; Iqbal, K.; Gong, C.X.; Liu, F.
Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) enhances tau expression (2013), J. Alzheimers Dis., 37, 529-538.

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Protein Variants

Protein Variants	Comment	Organism
K188R	site-directed mutagenesis, catalytically inactive mutant	Homo sapiens
additional information	construction of three deletion mutations of Dyrk1A from C-terminus, including Dyrk1A1-616 without S/T region, Dyrk1A1-588 without His repeats and S/T region, and Dyrk1A1-474 without PEST, His repeats, and S/T region for investigation whether C-terminus of Dyrk1A is responsible for the regulation of tau expression. All three C-terminal deletion mutations of Dyrk1A enhance the expression of tau to a much less extent as compared with the full length Dyrk1A	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
nucleus	Dyrk1A contains a nuclear targeting signal sequence	Homo sapiens	5634	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q13627	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HEK-293FT cell	-	Homo sapiens	-
neuronal cell	-	Homo sapiens	-

Subunits

Subunits	Comment	Organism
More	Dyrk1A contains a nuclear targeting signal sequence, a protein kinase domain, a PEST domain (protein domain that is enriched in proline (P), glutamic acid (E), serine (S), and threonine (T) residues), 13 consecutive histidine residues (His repeats) and a serine/threonine rich segment (S/T). The PEST region is located in the C terminus of the catalytic domain. A stretch of 13 histidines located between 607 and 619 amino acid residues follows subsequently a segment of 14 serine/threonine residues	Homo sapiens

Synonyms

Synonyms	Comment	Organism
dual-specificity tyrosine phosphorylation-regulated kinase 1A Dyrk1A	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	enzyme Dyrk1A interacts with and phosphorylates diverse cellular proteins including transcription and splicing factors. Dyrk1A enhances tau expression and regulates expression of endogenous tau in neuronal cells, mechanism, overview. Dyrk1A does not enhance tau gene transcription, but increases tau mRNA stability. The enhancement does not require the kinase activity of Dyrk1A, the inactive enzyme mutant K188R also increases tau expression. Dyrk1A increases the expression of tau isoforms containing exon 10 to a larger extent than isoforms lacking exon 10. Dyrk1A is overexpressed in Down syndrome and may play a critical role in the early onset of tau pathology in this disease	Homo sapiens

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Release 2023.1 (January 2023)