Curated Information
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Curated Information Page
PubMed Id: 11805080 
Cao H, Courchesne WE, Mastick CC (2002) A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase. J Biol Chem 277, 8771-4 11805080
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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Y14-p - Caveolin-1 (human)
Orthologous residues
Caveolin‑1 (human): Y14‑p, Caveolin‑1 (mouse): Y14‑p, Caveolin‑1 (rat): Y14‑p, Caveolin‑1 (dog): Y14‑p, Caveolin‑1 (sheep): Y14‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], fibroblast
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Abl (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
H2O2 increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CSK (human) Induces yeast two-hybrid
TRAF2 (human) Induces yeast two-hybrid


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