Curated Information
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Curated Information Page
PubMed Id: 10588651 
Adams JC, et al. (1999) Cell-matrix adhesions differentially regulate fascin phosphorylation. Mol Biol Cell 10, 4177-90 10588651
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.
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S39-p - Fascin (mouse)
Orthologous residues
Fascin (human): S39‑p, Fascin (mouse): S39‑p, Fascin (rat): S39‑p
 Methods used to characterize site in vivo 2D analysis, mutation of modification site
 Relevant cell lines - cell types - tissues:  LLC-PK1 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  pig
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (mouse) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
fibronectin increase S39 phosphorylation was induced by cell adhesion to fibronectin
calphostin C decrease
chelerythrine decrease
phorbol ester increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
ACTB (mouse) Disrupts not reported microscopy-colocalization

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