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
PTEN
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- T cell receptor signaling pathway [TAS]
- activation of mitotic anaphase-promoting complex activity [IDA]
- apoptotic process [ISS]
- brain morphogenesis [ISS]
- canonical Wnt signaling pathway [IDA]
- cell migration [ISS]
- cell proliferation [TAS]
- central nervous system development [ISS]
- central nervous system myelin maintenance [ISS]
- central nervous system neuron axonogenesis [ISS]
- dendritic spine morphogenesis [ISS]
- dentate gyrus development [ISS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- forebrain morphogenesis [ISS]
- heart development [ISS]
- innate immune response [TAS]
- inositol phosphate dephosphorylation [IDA]
- inositol phosphate metabolic process [TAS]
- learning or memory [ISS]
- locomotor rhythm [ISS]
- locomotory behavior [ISS]
- multicellular organismal response to stress [ISS]
- negative regulation of G1/S transition of mitotic cell cycle [IDA]
- negative regulation of axonogenesis [ISS]
- negative regulation of cell migration [IMP]
- negative regulation of cell proliferation [IDA, IMP]
- negative regulation of cell size [ISS]
- negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [IDA]
- negative regulation of dendritic spine morphogenesis [ISS]
- negative regulation of excitatory postsynaptic membrane potential [ISS]
- negative regulation of focal adhesion assembly [IMP]
- negative regulation of organ growth [ISS]
- negative regulation of phosphatidylinositol 3-kinase signaling [TAS]
- negative regulation of protein kinase B signaling [IMP]
- negative regulation of protein phosphorylation [IDA]
- negative regulation of synaptic vesicle clustering [ISS]
- neuron-neuron synaptic transmission [ISS]
- neurotrophin TRK receptor signaling pathway [TAS]
- peptidyl-tyrosine dephosphorylation [IDA]
- phosphatidylinositol biosynthetic process [TAS]
- phosphatidylinositol dephosphorylation [IDA, IMP]
- phosphatidylinositol-mediated signaling [TAS]
- phospholipid metabolic process [TAS]
- positive regulation of cell proliferation [ISS]
- positive regulation of excitatory postsynaptic membrane potential [ISS]
- positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IMP]
- postsynaptic density assembly [ISS]
- prepulse inhibition [ISS]
- presynaptic membrane assembly [ISS]
- protein dephosphorylation [IDA, TAS]
- protein kinase B signaling [ISS]
- protein stabilization [IDA]
- regulation of cellular component size [ISS]
- regulation of cyclin-dependent protein serine/threonine kinase activity [TAS]
- regulation of neuron projection development [ISS]
- regulation of protein stability [IMP]
- rhythmic synaptic transmission [ISS]
- small molecule metabolic process [TAS]
- social behavior [ISS]
- synapse assembly [ISS]
- synapse maturation [ISS]
Gene Ontology Molecular Function- PDZ domain binding [IPI]
- anaphase-promoting complex binding [IPI]
- enzyme binding [IPI]
- inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity [IDA, TAS]
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity [IDA, TAS]
- phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity [IDA, TAS]
- phosphatidylinositol-3-phosphatase activity [IDA]
- phosphoprotein phosphatase activity [IDA]
- protein binding [IPI]
- protein serine/threonine phosphatase activity [IDA]
- protein tyrosine phosphatase activity [IDA]
- PDZ domain binding [IPI]
- anaphase-promoting complex binding [IPI]
- enzyme binding [IPI]
- inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity [IDA, TAS]
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity [IDA, TAS]
- phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity [IDA, TAS]
- phosphatidylinositol-3-phosphatase activity [IDA]
- phosphoprotein phosphatase activity [IDA]
- protein binding [IPI]
- protein serine/threonine phosphatase activity [IDA]
- protein tyrosine phosphatase activity [IDA]
Gene Ontology Cellular Component
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
Plk1 phosphorylation of PTEN causes a tumor-promoting metabolic state.
One outcome of activation of the phosphatidylinositol 3-kinase (PI3K) pathway is increased aerobic glycolysis, but the upstream signaling events that regulate the PI3K pathway, and thus the Warburg effect, are elusive. Increasing evidence suggests that Plk1, a cell cycle regulator, is also involved in cellular events in addition to mitosis. To test whether Plk1 contributes to activation of the PI3K ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PTEN CSNK2A1 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | Low | - | BioGRID | - | |
| CSNK2A1 PTEN | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 262809 | |
| PTEN CSNK2A1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| PTEN CSNK2A1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | High | - | BioGRID | - |
Curated By
- BioGRID