Curated Information
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Curated Information Page
PubMed Id: 15466865 
Labrecque L, et al. (2004) Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase. J Biol Chem 279, 52132-40 15466865
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 mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial), BAEC (endothelial), COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  cow, human, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Src (human)
KINASE Fyn (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Fyn (human) transfection of wild-type enzyme
KINASE Src (human) transfection of dominant-negative enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
VEGF increase
methyl-beta-cyclodextrin VEGF augment treatment-induced 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
MMP9 (human) Induces intracellular localization electrophoretic visualization, co-immunoprecipitation


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