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.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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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 (hamster): S369‑p
Characterization
 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 (hamster): S373‑p
Characterization
 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, pharmacological activator of upstream enzyme, microscopy-colocalization
 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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