Curated Information

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PubMed Id: 16732330

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.

Information from this record has been curated, but not yet edited in PhosphoSitePlus^® and may be incomplete.

Benzeno S, et al. (2006) Identification of mutations that disrupt phosphorylation-dependent nuclear export of cyclin D1. Oncogene 25, 6291-303 16732330

T286-p - CCND1 (human)

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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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