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Literature summary for 2.7.12.1 extracted from

  • Morrugares, R.; Correa-Saez, A.; Moreno, R.; Garrido-Rodriguez, M.; Munoz, E.; de la Vega, L.; Calzado, M.A.
    Phosphorylation-dependent regulation of the NOTCH1 intracellular domain by dual-specificity tyrosine-regulated kinase 2 (2020), Cell. Mol. Life Sci., 77, 2621-2639 .
    View publication on PubMed
Search for more literature for 2.7.12.1

Application

Application Comment Organism
medicine DYRK2 phosphorylates Notch1-IC in response to chemotherapeutic agents and facilitates its proteasomal degradation by FBXW7 ubiquitin ligase through a Thr-2512 phosphorylation-dependent mechanism. DYRK2 regulation by chemotherapeutic agents has a relevant effect on the viability, motility and invasion capacity of cancer cells expressing NOTCH1 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92630
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293T cell
-
 Homo sapiens
-
HeLa cell
-
 Homo sapiens
-
MCF-7 cell
-
 Homo sapiens
-
MDA-MB-468 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Notch-IC
-
 Homo sapiens ADP + phosphorylated Notch-IC
-
 ?

Synonyms

Synonyms Comment Organism
DYRK2
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function DYRK2 phosphorylates Notch1-IC in response to chemotherapeutic agents and facilitates its proteasomal degradation by FBXW7 ubiquitin ligase through a Thr-2512 phosphorylation-dependent mechanism. DYRK2 regulation by chemotherapeutic agents has a relevant effect on the viability, motility and invasion capacity of cancer cells expressing NOTCH1 Homo sapiens