CSNK2A1
Gene Ontology Biological Process
- axon guidance [TAS]
- chaperone-mediated protein folding [TAS]
- mitotic cell cycle [TAS]
- mitotic spindle checkpoint [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- positive regulation of Wnt signaling pathway [IMP]
- positive regulation of cell growth [IDA]
- positive regulation of cell proliferation [IDA]
- positive regulation of protein catabolic process [IDA]
- protein phosphorylation [IDA]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CAV2
Gene Ontology Biological Process
- caveola assembly [IMP]
- endoplasmic reticulum organization [ISS]
- mitochondrion organization [ISS]
- negative regulation of endothelial cell proliferation [ISS]
- positive regulation of dopamine receptor signaling pathway [IMP]
- regulation of mitosis [IEP]
- skeletal muscle fiber development [ISS]
- vesicle docking [IDA]
- vesicle fusion [IDA]
- vesicle organization [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Golgi apparatus [ISS]
- caveola [IDA]
- cytoplasmic vesicle [IDA]
- extrinsic component of cytoplasmic side of plasma membrane [IDA]
- integral component of plasma membrane [IDA]
- intracellular [IDA]
- membrane [IDA]
- membrane raft [IDA]
- perinuclear region of cytoplasm [IDA]
- plasma membrane [IDA]
- protein complex [IDA]
- transport vesicle [IDA]
Biochemical Activity (Phosphorylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation.
Caveolin-1 and -2 are the two major coat proteins found in plasma membrane caveolae of most of cell types. Here, by using adenoviral transduction of either caveolin-1 or caveolin-2 or both isoforms into cells lacking both caveolins, we demonstrate that caveolin-2 positively regulates caveolin-1-dependent caveolae formation. More importantly, we show that caveolin-2 is phosphorylated in vivo at two serine residues ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID