| Post Translational Modifications | Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin. |
| Function | May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression. |
| Protein Name | Caveolin-2 |
| Database Links | Reactome: R-HSA-9009391 |
| Cellular Localisation | NucleusCytoplasmGolgi Apparatus MembranePeripheral Membrane ProteinCell MembraneMembraneCaveolaPotential Hairpin-Like Structure In The MembraneMembrane Protein Of CaveolaeTyr-19-Phosphorylated Form Is Enriched At Sites Of Cell-Cell Contact And Is Translocated To The Nucleus In Complex With Mapk1 In Response To InsulinTyr-27-Phosphorylated Form Is Located Both In The Cytoplasm And Plasma MembraneCav1-Mediated Ser-23-Phosphorylated Form Locates To The Plasma MembraneSer-36-Phosphorylated Form Resides In Intracellular Compartments |
| Alternative Protein Names | Caveolin-2 proteinCAV2 protein |
Information sourced from Uniprot.org
