Curated Information
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Curated Information Page
PubMed Id: 18163231 
Park DJ, et al. (2007) Akt phosphorylates Connexin43 on Ser373, a "mode-1" binding site for 14-3-3. Cell Commun Adhes 14, 211-26 18163231
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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S369-p - GJA1 (rat)
Orthologous residues
GJA1 (human): S369‑p, GJA1 (mouse): S369‑p, GJA1 (rat): S369‑p, GJA1 (rabbit): S369‑p, GJA1 (pig): S369‑p, GJA1 (hamster): S369‑p
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)

S373-p - GJA1 (rat)
Orthologous residues
GJA1 (human): S373‑p, GJA1 (mouse): S373‑p, GJA1 (rat): S373‑p, GJA1 (rabbit): S373‑p, GJA1 (pig): S373‑p, GJA1 (hamster): S373‑p
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  Rat1 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt3 (rat) phospho-motif antibody, microscopy-colocalization, pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 theta (mouse) Induces pull-down assay

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