Curated Information
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Curated Information Page
PubMed Id: 8631952 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Kentrup H, et al. (1996) 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, 3488-95 8631952
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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Y219-p - DYRK1A (rat)
Orthologous residues
DYRK1A (human): Y219‑p, DYRK1A iso2 (human): Y210‑p, DYRK1A iso4 (human): Y219‑p, DYRK1A (mouse): Y219‑p, DYRK1A (rat): Y219‑p, DYRK1A (rabbit): Y76‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE DYRK1A (rat)

Y319-p - DYRK1A (rat)
Orthologous residues
DYRK1A (human): Y319‑p, DYRK1A iso2 (human): Y310‑p, DYRK1A iso4 (human): Y319‑p, DYRK1A (mouse): Y319‑p, DYRK1A (rat): Y319‑p, DYRK1A (rabbit):
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced

Y321-p - DYRK1A (rat)
Orthologous residues
DYRK1A (human): Y321‑p, DYRK1A iso2 (human): Y312‑p, DYRK1A iso4 (human): Y321‑p, DYRK1A (mouse): Y321‑p, DYRK1A (rat): Y321‑p, DYRK1A (rabbit):
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced


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