Curated Information
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Curated Information Page
PubMed Id: 17486076 
Kida A, et al. (2007) Glycogen synthase kinase-3beta and p38 phosphorylate cyclin D2 on Thr280 to trigger its ubiquitin/proteasome-dependent degradation in hematopoietic cells. Oncogene 26, 6630-40 17486076
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.
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T280-p - CCND2 (human)
Orthologous residues
CCND2 (human): T280‑p, CCND2 (mouse): T280‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  32Dcl3 (myeloid), B lymphocyte, lymphoblast, myeloid
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE P38A (human)
KINASE GSK3B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE P38A (human) pharmacological inhibitor of upstream enzyme
KINASE GSK3B (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
osmotic stress increase
IL-3 decrease activates PI3K/Akt pathway, thereby inhibiting GSK3beta-mediated phosphorylation, preventing cyclin D2 degradation
lithium decrease inhibits GSK3beta, thereby reducing phosphorylation leading to decreased degradation
SB216763 decrease inhibits GSK3beta, thereby reducing phosphorylation leading to decreased degradation
Downstream Regulation
 Effect of modification (function):  protein degradation


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