Curated Information
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Curated Information Page
PubMed Id: 10660530 
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
MacNicol MC, Muslin AJ, MacNicol AM (2000) Disruption of the 14-3-3 binding site within the B-Raf kinase domain uncouples catalytic activity from PC12 cell differentiation. J Biol Chem 275, 3803-9 10660530
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S729-p - BRAF (human)
Orthologous residues
BRAF (human): S729‑p, BRAF (mouse): S766‑p, BRAF iso3 (mouse): , BRAF (rat): S766‑p, BRAF (chicken): S769‑p, BRAF (quail): S769‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  adrenal cancer, pheochromocytoma
 Relevant cell lines - cell types - tissues:  oocyte, PC-12 (chromaffin)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, rat
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
 Effect of modification (process):  cell differentiation, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces yeast two-hybrid, pull-down assay


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