Roche KW, et al. (1996) Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16, 1179-88 8663994

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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S849-p - GluR1 (rat) ▲

Modsite: FCLIPQQsINEAIrT SwissProt Entrez-Gene Orthologous residues GluR1 (human): S849‑p, GluR1 iso6 (human): S859‑p, GluR1 (mouse): S849‑p, GluR1 (rat): S849‑p Characterization Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping Relevant cell lines - cell types - tissues:  293 (epithelial) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKCA (human) Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes phorbol_ester increase Downstream Regulation Effect of modification (function):  activity, induced Comments:  Phosphorylation increases peak current.

S863-p - GluR1 (rat) ▲

Modsite: TSTLPRNsGAGASGG SwissProt Entrez-Gene Orthologous residues GluR1 (human): S863‑p, GluR1 iso6 (human): S873‑p, GluR1 (mouse): S863‑p, GluR1 (rat): S863‑p Characterization Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping Relevant cell lines - cell types - tissues:  293 (epithelial) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKACA (human) Upstream Regulation 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:  Phosphorylation results in a 40% potentiation of the peak current through GluR1 homomeric channels.