Curated Information
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Curated Information Page
PubMed Id: 14690436 
This page summarizes selected information from the article 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.
Obsil T, et al. (2003) Two 14-3-3 binding motifs are required for stable association of Forkhead transcription factor FOXO4 with 14-3-3 proteins and inhibition of DNA binding. Biochemistry 42, 15264-72 14690436
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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T32-p - FOXO4 (mouse)
Orthologous residues
FOXO4 (human): T32‑p, FOXO4 (mouse): T32‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 zeta (human) Induces in vitro

S197-p - FOXO4 (mouse)
Orthologous residues
FOXO4 (human): S197‑p, FOXO4 (mouse): S197‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 zeta (human) Induces in vitro


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