Curated Information
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Home > Curated Information Page > PubMed Id: 8861947
Won KA, Reed SI (1996) Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J 15, 4182-93 8861947
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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T395-p - CCNE1 (human)
Modsite: PLPSGLLtPPQsGKK SwissProt Entrez-Gene
Orthologous residues
CCNE1 (human): T395‑p, CCNE1 (mouse): T393‑p, CCNE1 (rat): T396‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
Relevant cell lines - cell types - tissues:  Rat1 (fibroblast)
Cellular systems studied:  cell lines, primary cells
Species studied:  rat, yeast
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK2 (human)
Downstream Regulation
Effect of modification (function):  protein degradation
Effect of modification (process):  cell cycle regulation
Comments:  T380 of cyclin E is necessary for for ubiquination and targeting to the proteosome.