AKT1
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- G-protein coupled receptor signaling pathway [TAS]
- RNA metabolic process [TAS]
- T cell costimulation [TAS]
- activation-induced cell death of T cells [IMP]
- apoptotic process [TAS]
- blood coagulation [TAS]
- cell differentiation [TAS]
- cell proliferation [TAS]
- cellular protein modification process [TAS]
- cellular response to insulin stimulus [IMP, ISS]
- endocrine pancreas development [TAS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- gene expression [TAS]
- innate immune response [TAS]
- insulin receptor signaling pathway [IMP]
- insulin-like growth factor receptor signaling pathway [IMP]
- intracellular signal transduction [IDA]
- intrinsic apoptotic signaling pathway [TAS]
- mRNA metabolic process [TAS]
- mammary gland epithelial cell differentiation [TAS]
- membrane organization [TAS]
- negative regulation of apoptotic process [IDA]
- negative regulation of autophagy [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [ISS]
- negative regulation of endopeptidase activity [IMP]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [TAS]
- negative regulation of fatty acid beta-oxidation [IMP]
- negative regulation of neuron death [NAS]
- negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [NAS]
- negative regulation of plasma membrane long-chain fatty acid transport [IMP]
- negative regulation of protein kinase activity [IMP, ISS]
- negative regulation of proteolysis [IMP]
- negative regulation of release of cytochrome c from mitochondria [ISS]
- neurotrophin TRK receptor signaling pathway [TAS]
- nitric oxide biosynthetic process [TAS]
- nitric oxide metabolic process [TAS]
- peptidyl-serine phosphorylation [IDA]
- phosphatidylinositol-mediated signaling [TAS]
- phosphorylation [IDA]
- platelet activation [TAS]
- positive regulation of blood vessel endothelial cell migration [IDA]
- positive regulation of cell growth [IDA]
- positive regulation of cellular protein metabolic process [ISS]
- positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [IDA]
- positive regulation of endothelial cell proliferation [IMP]
- positive regulation of establishment of protein localization to plasma membrane [IMP]
- positive regulation of fat cell differentiation [IMP]
- positive regulation of glucose import [IMP]
- positive regulation of glucose metabolic process [IMP]
- positive regulation of glycogen biosynthetic process [IMP, NAS]
- positive regulation of lipid biosynthetic process [IMP]
- positive regulation of nitric oxide biosynthetic process [IMP]
- positive regulation of nitric-oxide synthase activity [IMP]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- protein autophosphorylation [TAS]
- protein import into nucleus, translocation [IMP]
- protein phosphorylation [IDA]
- regulation of cell cycle checkpoint [TAS]
- regulation of cell migration [IMP, TAS]
- regulation of glycogen biosynthetic process [IMP]
- regulation of neuron projection development [ISS]
- regulation of nitric-oxide synthase activity [TAS]
- response to UV-A [IDA]
- response to fluid shear stress [IMP]
- response to heat [TAS]
- response to oxidative stress [ISS]
- signal transduction [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function- 14-3-3 protein binding [IPI]
- ATP binding [IC, IDA]
- enzyme binding [ISS]
- identical protein binding [IPI]
- kinase activity [IDA]
- nitric-oxide synthase regulator activity [IMP]
- phosphatidylinositol-3,4,5-trisphosphate binding [IDA]
- phosphatidylinositol-3,4-bisphosphate binding [IDA]
- protein binding [IPI]
- protein kinase activity [TAS]
- protein serine/threonine kinase activity [IDA, TAS]
- protein serine/threonine/tyrosine kinase activity [IDA]
- 14-3-3 protein binding [IPI]
- ATP binding [IC, IDA]
- enzyme binding [ISS]
- identical protein binding [IPI]
- kinase activity [IDA]
- nitric-oxide synthase regulator activity [IMP]
- phosphatidylinositol-3,4,5-trisphosphate binding [IDA]
- phosphatidylinositol-3,4-bisphosphate binding [IDA]
- protein binding [IPI]
- protein kinase activity [TAS]
- protein serine/threonine kinase activity [IDA, TAS]
- protein serine/threonine/tyrosine kinase activity [IDA]
SRPK2
Gene Ontology Biological Process
- RNA splicing [IDA]
- angiogenesis [ISS]
- innate immune response [IC]
- intracellular signal transduction [IDA]
- negative regulation of viral genome replication [IDA]
- nuclear speck organization [ISS]
- positive regulation of cell cycle [ISS]
- positive regulation of cell proliferation [IDA]
- positive regulation of gene expression [ISS]
- positive regulation of neuron apoptotic process [ISS]
- positive regulation of viral genome replication [IDA]
- protein phosphorylation [IDA]
- regulation of mRNA splicing, via spliceosome [TAS]
- spliceosomal complex assembly [IDA]
Gene Ontology Molecular Function
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
Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons.
Terminally differentiated neurons are unable to reenter the cell cycle. Aberrant cell cycle activation provokes neuronal cell death, whereas cell cycle inhibition elevates neuronal survival. However, the molecular mechanism regulating the cell cycle and cell death in mature neurons remains elusive. Here we show that SRPK2, a protein kinase specific for the serine/arginine (SR) family of splicing factors, triggers cell ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| SRPK2 AKT1 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| AKT1 SRPK2 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | - | |
| AKT1 SRPK2 | 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 | - |
Curated By
- BioGRID