Curated Information

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Curated Information Page

PubMed Id: 8861947

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.

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

T395-p - CCNE1 (human)

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Orthologous residues

CCNE1 (human): T395‑p, CCNE1 (mouse): T393‑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.

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