CAMK2A
Gene Ontology Biological Process
- G1/S transition of mitotic cell cycle [ISS]
- calcium ion transport [ISS]
- cytokine-mediated signaling pathway [TAS]
- interferon-gamma-mediated signaling pathway [TAS]
- peptidyl-serine phosphorylation [ISS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of calcium ion transport [ISS]
- positive regulation of cardiac muscle cell apoptotic process [ISS]
- protein autophosphorylation [ISS]
- protein phosphorylation [IDA]
- regulation of mitochondrial membrane permeability involved in apoptotic process [ISS]
- regulation of neuronal synaptic plasticity [ISS]
- regulation of neurotransmitter secretion [ISS]
- response to ischemia [ISS]
- synaptic transmission [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GRIA1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex [IBA, ISS]
- cell surface [ISS]
- dendrite [IBA, ISS]
- dendritic spine [ISS]
- dendritic spine membrane [IDA]
- endocytic vesicle membrane [TAS]
- neuron spine [ISS]
- neuronal cell body [ISS]
- plasma membrane [TAS]
- postsynaptic density [ISS]
- postsynaptic membrane [IBA]
- recycling endosome [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
Inhibitory interactions between phosphorylation sites in the C terminus of ?-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptor GluA1 subunits.
The C terminus of AMPA-type glutamate receptor (AMPAR) GluA1 subunits contains several phosphorylation sites that regulate AMPAR activity and trafficking at excitatory synapses. Although many of these sites have been extensively studied, little is known about the signaling mechanisms regulating GluA1 phosphorylation at Thr-840. Here, we report that neuronal depolarization in hippocampal slices induces a calcium and protein phosphatase 1/2A-dependent ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CAMK2A GRIA1 | 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 | 3731532 |
Curated By
- BioGRID