Curated Information
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Curated Information Page
PubMed Id: 10871288 
Lampe PD, et al. (2000) Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication. J Cell Biol 149, 1503-12 10871288
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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S368-p - GJA1 (rat)
Orthologous residues
GJA1 (human): S368‑p, GJA1 (mouse): S368‑p, GJA1 (rat): S368‑p, GJA1 (rabbit): S368‑p, GJA1 (hamster): S368‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  fibroblast-skin, T51B (epithelial)
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  mouse, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCA (cow)
KINASE PKCG (human)
KINASE PKCB (cow)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (mouse) pharmacological activator of upstream enzyme
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
phorbol ester increase
Downstream Regulation
 Effect of modification (function):  activity, inhibited


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