Curated Information
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Curated Information Page
PubMed Id: 9360956 
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.
Dubois T, et al. (1997) 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J Biol Chem 272, 28882-8 9360956
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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S232-p - 14-3-3 theta (human)
Orthologous residues
14‑3‑3 theta (human): S232‑p, 14‑3‑3 theta (mouse): S232‑p, 14‑3‑3 theta (rat): S232‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK1A (human)

T232-p - 14-3-3 zeta (human)
Orthologous residues
14‑3‑3 zeta (human): T232‑p, 14‑3‑3 zeta (mouse): T232‑p, 14‑3‑3 zeta (rat): T232‑p, 14‑3‑3 zeta (sheep): T232‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mass spectrometry, mutation of modification site, peptide sequencing
 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 CK1A (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
RAF1 (human) Disrupts


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