Curated Information
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Curated Information Page
PubMed Id: 15504744 
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.
Makagiansar IT, et al. (2004) Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility. J Biol Chem 279, 55262-70 15504744
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T2256-p - NG2 (rat)
Orthologous residues
NG2 (human): T2252‑p, NG2 (mouse): T2257‑p, NG2 (rat): T2256‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phospho-antibody, phosphoamino acid analysis, phosphopeptide mapping, western blotting
 Disease tissue studied:  brain cancer, glioblastoma, glioma
 Relevant cell lines - cell types - tissues:  U251 (glial) [NG2 (rat)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) co-immunoprecipitation, pharmacological activator of upstream enzyme, phospho-motif antibody, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
GF109203X phorbol ester inhibit treatment-induced increase
Go 6976 phorbol ester inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell adhesion, altered, cell motility, altered


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