Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 8631952 
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
This page summarizes selected information from the record 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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download Sites

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
 Enzymes shown to modify site in vitro
Type Enzyme

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

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.