Curated Information
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Curated Information Page
PubMed Id: 11007883 
Chung HJ, et al. (2000) Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins. J Neurosci 20, 7258-67 11007883
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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S880-p - GluR2 (rat)
Orthologous residues
GluR2 (human): S880‑p, GluR2 iso2 (human): S880‑p, GluR2 (mouse): S880‑p, GluR2 iso3 (mouse): , GluR2 (rat): S880‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  'neuron, cortical'-brain, 'neuron, hippocampal'-brain, 293T (epithelial)
 Cellular systems studied:  cell lines, primary cultured cells, tissue
 Species studied:  human, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCA (rat)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (rat) pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin no change compared to control
phorbol ester increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, receptor internalization, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
GRIP1 (rat) Disrupts co-immunoprecipitation


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