CAMK2G
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GRIN1
Gene Ontology Biological Process
- calcium ion homeostasis [ISS]
- calcium ion transmembrane transport [IDA]
- cation transport [IDA]
- ion transmembrane transport [IBA]
- ionotropic glutamate receptor signaling pathway [IBA, ISS]
- positive regulation of excitatory postsynaptic membrane potential [ISS]
- positive regulation of transcription from RNA polymerase II promoter [ISS]
- propylene metabolic process [ISS]
- regulation of excitatory postsynaptic membrane potential [ISS]
- regulation of membrane potential [IDA]
- response to ethanol [IDA]
- synaptic transmission [TAS]
- synaptic transmission, glutamatergic [IBA]
- visual learning [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- N-methyl-D-aspartate selective glutamate receptor complex [IDA]
- cell surface [ISS]
- dendrite [IDA]
- dendritic spine [ISS]
- excitatory synapse [ISS]
- integral component of plasma membrane [IDA]
- neuron projection [ISS]
- plasma membrane [TAS]
- postsynaptic density [ISS]
- postsynaptic membrane [IBA, ISS]
- synapse [ISS]
- synaptic cleft [ISS]
- synaptic vesicle [ISS]
- terminal bouton [ISS]
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
Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin.
The N-methyl-D-aspartate receptor (NMDA-R) and brain spectrin, a protein that links membrane proteins to the actin cytoskeleton, are major components of post-synaptic densities (PSDs). Since the activity of the NMDA-R channel is dependent on the integrity of actin and leads to calpain-mediated spectrin breakdown, we have investigated whether the actin-binding spectrin may interact directly with NMDA-Rs. Spectrin is reported here ... [more]
Throughput
- Low Throughput
Additional Notes
- phosphorlation decreases binding to spectrin
Curated By
- BioGRID