Curated Information
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Curated Information Page
PubMed Id: 16732330 
Benzeno S, et al. (2006) Identification of mutations that disrupt phosphorylation-dependent nuclear export of cyclin D1. Oncogene 25, 6291-303 16732330
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
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T286-p - CCND1 (human)
Orthologous residues
CCND1 (human): T286‑p, CCND1 (mouse): T286‑p
Characterization
 Methods used to characterize site in vivo microscopy-colocalization with upstream kinase, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cycloheximide decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell cycle regulation, cell growth, altered
 Comments:  Mutant T286D mutant is constitutively nuclear and stable.


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