Curated Information

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Curated Information Page

PubMed Id: 11078729

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.

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

S80-p - caveolin-1 (dog)

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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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