Curated Information
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Home > Curated Information Page > PubMed Id: 8094892
Raymond LA, Blackstone CD, Huganir RL (1993) Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase. Nature 361, 637-41 8094892
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S715-p - GluR6 (rat)
Modsite: FMSSRRQsVLVKSNE SwissProt Entrez-Gene
Orthologous residues
GluR6 (human): S715‑p, GluR6 (mouse): S715‑p, GluR6 (rat): S715‑p
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
Relevant cell lines - cell types - tissues:  293 (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) genetic transfer of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
colforsin increase
Downstream Regulation
Effect of modification (function):  activity, induced
Comments:  PKA-mediated phosphorylation increases the potentiation of the glutamate response.