Curated Information
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Curated Information Page
PubMed Id: 11078729 
Schlegel A, Arvan P, Lisanti MP (2001) Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum. J Biol Chem 276, 4398-408 11078729
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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S80-p - Caveolin-1 (dog)
Orthologous residues
Caveolin‑1 (human): S80‑p, Caveolin‑1 (mouse): S80‑p, Caveolin‑1 (rat): S80‑p, Caveolin‑1 (dog): S80‑p, Caveolin‑1 (sheep): S80‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), AR42J (pancreatic), COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  phosphorylation of this site regulates secretion of caveolin-1 in the pancreatic acinar cells AR42J


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