Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 9360956 
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
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.
Download Sites

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
 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
 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

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.