Curated Information
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Curated Information Page
PubMed Id: 12207013 
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.
Jang YJ, Ma S, Terada Y, Erikson RL (2002) Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase. J Biol Chem 277, 44115-20 12207013
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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S137-p - PLK1 (human)
Orthologous residues
PLK1 (human): S137‑p, PLK1 (mouse): S137‑p, PLK1 (rat): S137‑p, PLK1 (frog): S128‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced
 Effect of modification (process):  cell cycle regulation

T210-p - PLK1 (human)
Orthologous residues
PLK1 (human): T210‑p, PLK1 (mouse): T210‑p, PLK1 (rat): T210‑p, PLK1 (frog): T201‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, electrophoretic mobility shift, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE LOK (human)
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced
 Effect of modification (process):  cell cycle regulation


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