SCN2A
Gene Ontology Biological Process
- intrinsic apoptotic signaling pathway in response to osmotic stress [ISO]
- membrane depolarization during action potential [IBA]
- myelination [IEP]
- nervous system development [ISO]
- neuron apoptotic process [ISO]
- neuronal action potential [IBA, IDA, TAS]
- sodium ion transmembrane transport [IBA, IDA, ISO]
- sodium ion transport [IDA, ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- T-tubule [ISO]
- axon [ISO]
- axon initial segment [IDA]
- intercalated disc [ISO]
- intracellular [ISO]
- intrinsic component of plasma membrane [IDA]
- membrane [ISO]
- neuron projection [IDA]
- node of Ranvier [IDA]
- paranode region of axon [ISO]
- plasma membrane [IBA]
- sodium channel complex [IDA]
- voltage-gated sodium channel complex [IDA]
CALM1
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [ISO]
- activation of adenylate cyclase activity [IDA]
- calcium-mediated signaling [IMP]
- detection of calcium ion [ISO]
- positive regulation of DNA binding [ISO]
- positive regulation of cyclic nucleotide metabolic process [ISO]
- positive regulation of cyclic-nucleotide phosphodiesterase activity [ISO]
- positive regulation of nitric-oxide synthase activity [IDA]
- positive regulation of phosphoprotein phosphatase activity [ISO]
- positive regulation of protein dephosphorylation [ISO]
- positive regulation of ryanodine-sensitive calcium-release channel activity [ISO]
- regulation of cardiac muscle contraction [ISO]
- regulation of cytokinesis [ISO]
- regulation of heart rate [ISO]
- regulation of high voltage-gated calcium channel activity [IMP]
- regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [ISO]
- regulation of ryanodine-sensitive calcium-release channel activity [IDA]
- regulation of store-operated calcium channel activity [IC]
- response to amphetamine [IEP]
- response to calcium ion [ISO]
- substantia nigra development [ISO]
Gene Ontology Molecular Function- N-terminal myristoylation domain binding [ISO]
- adenylate cyclase binding [IDA]
- calcium channel regulator activity [NAS]
- calcium ion binding [IDA, ISO]
- calcium-dependent protein binding [IPI]
- enzyme regulator activity [IMP]
- ion channel binding [IDA, ISO]
- nitric-oxide synthase binding [IDA]
- nitric-oxide synthase regulator activity [IDA]
- phosphatidylinositol 3-kinase binding [IPI]
- phospholipase binding [ISO]
- protein N-terminus binding [IMP]
- protein binding [IPI]
- protein domain specific binding [IPI, ISO]
- protein kinase binding [ISO]
- protein phosphatase activator activity [ISO]
- thioesterase binding [ISO]
- titin binding [ISO]
- type 3 metabotropic glutamate receptor binding [IPI]
- N-terminal myristoylation domain binding [ISO]
- adenylate cyclase binding [IDA]
- calcium channel regulator activity [NAS]
- calcium ion binding [IDA, ISO]
- calcium-dependent protein binding [IPI]
- enzyme regulator activity [IMP]
- ion channel binding [IDA, ISO]
- nitric-oxide synthase binding [IDA]
- nitric-oxide synthase regulator activity [IDA]
- phosphatidylinositol 3-kinase binding [IPI]
- phospholipase binding [ISO]
- protein N-terminus binding [IMP]
- protein binding [IPI]
- protein domain specific binding [IPI, ISO]
- protein kinase binding [ISO]
- protein phosphatase activator activity [ISO]
- thioesterase binding [ISO]
- titin binding [ISO]
- type 3 metabotropic glutamate receptor binding [IPI]
Gene Ontology Cellular Component
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.
Publication
Calmodulin binds to the C terminus of sodium channels Nav1.4 and Nav1.6 and differentially modulates their functional properties.
Modulation of voltage-gated sodium channels (VGSC) can have a major impact on cell excitability. Analysis of calmodulin (CaM) binding to GST-fusion proteins containing the C-terminal domains of Nav1.1-Nav1.9 indicates that some of the tetrodotoxin-sensitive VGSC isoforms, including NaV1.4 and NaV1.6, are able to bind CaM in a calcium-independent manner. Here we demonstrate that association with CaM is important for functional ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID