Curated Information
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Curated Information Page
PubMed Id: 17018293 
Sasaki T, et al. (2006) Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role. Mol Cell 24, 63-75 17018293
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.
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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S32-p - Fos (human)
Orthologous residues
Fos (human): S32‑p, Fos (mouse): S32‑p, Fos (rat): S32‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK5 (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein stabilization
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
UBR1 (human) Disrupts co-immunoprecipitation

T232-p - Fos (human)
Orthologous residues
Fos (human): T232‑p, Fos (mouse): T232‑p, Fos (rat): T232‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK5 (human)
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Site located within nuclear export signal; phosphorylation inhibits nuclear export and causes nuclear retention of Fos.


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