Curated Information
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Curated Information Page
PubMed Id: 17030608 
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.
Benjamin D, et al. (2006) BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites. Mol Cell Biol 26, 9497-507 17030608
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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S92-p - BRF1 (human)
Orthologous residues
BRF1 (human): S92‑p, BRF1 (mouse): S92‑p, BRF1 (rat): S92‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], HT1080 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  mouse
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation, protein stabilization
 Effect of modification (process):  RNA stability, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces co-immunoprecipitation
 Comments:  for its physiological effect phosphorylation of this site cooperates with phosphorylation of S90 and S203

S203-p - BRF1 (human)
Orthologous residues
BRF1 (human): S203‑p, BRF1 (mouse): S203‑p, BRF1 (rat): S203‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], HIRcB (fibroblast), HT1080 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  mouse, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
okadaic acid increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein stabilization
 Effect of modification (process):  RNA stability, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces co-immunoprecipitation
 Comments:  for its physiological effect phosphorylation of this site cooperates with phosphorylation of S90 and S92


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