CALM1
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- G-protein coupled receptor signaling pathway [TAS]
- activation of phospholipase C activity [TAS]
- blood coagulation [TAS]
- carbohydrate metabolic process [TAS]
- detection of calcium ion [IMP]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- glucose metabolic process [TAS]
- glycogen catabolic process [TAS]
- innate immune response [TAS]
- inositol phosphate metabolic process [TAS]
- membrane organization [TAS]
- muscle contraction [TAS]
- negative regulation of peptidyl-threonine phosphorylation [TAS]
- negative regulation of ryanodine-sensitive calcium-release channel activity [ISS]
- neurotrophin TRK receptor signaling pathway [TAS]
- nitric oxide metabolic process [TAS]
- phototransduction, visible light [TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cyclic nucleotide metabolic process [IDA]
- positive regulation of cyclic-nucleotide phosphodiesterase activity [IDA]
- positive regulation of peptidyl-threonine phosphorylation [TAS]
- positive regulation of phosphoprotein phosphatase activity [IDA]
- positive regulation of protein autophosphorylation [TAS]
- positive regulation of protein dephosphorylation [IDA]
- positive regulation of protein serine/threonine kinase activity [TAS]
- positive regulation of ryanodine-sensitive calcium-release channel activity [IDA]
- regulation of cardiac muscle contraction [IMP]
- regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [IC]
- regulation of cell communication by electrical coupling involved in cardiac conduction [IC]
- regulation of cytokinesis [IMP]
- regulation of heart rate [IMP]
- regulation of nitric-oxide synthase activity [TAS]
- regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [IDA]
- regulation of rhodopsin mediated signaling pathway [TAS]
- response to calcium ion [IDA]
- rhodopsin mediated signaling pathway [TAS]
- signal transduction [TAS]
- small molecule metabolic process [TAS]
- substantia nigra development [IEP]
- synaptic transmission [TAS]
Gene Ontology Molecular Function- N-terminal myristoylation domain binding [IPI]
- calcium ion binding [IDA, ISS]
- ion channel binding [IPI]
- phospholipase binding [IPI]
- protein binding [IPI]
- protein domain specific binding [IPI]
- protein kinase binding [IPI]
- protein phosphatase activator activity [IDA]
- protein serine/threonine kinase activator activity [TAS]
- thioesterase binding [IPI]
- titin binding [IPI]
- N-terminal myristoylation domain binding [IPI]
- calcium ion binding [IDA, ISS]
- ion channel binding [IPI]
- phospholipase binding [IPI]
- protein binding [IPI]
- protein domain specific binding [IPI]
- protein kinase binding [IPI]
- protein phosphatase activator activity [IDA]
- protein serine/threonine kinase activator activity [TAS]
- thioesterase binding [IPI]
- titin binding [IPI]
Gene Ontology Cellular Component
NOS2
Gene Ontology Biological Process
- arginine catabolic process [IDA]
- blood coagulation [TAS]
- defense response to Gram-negative bacterium [NAS]
- defense response to bacterium [IMP, ISS]
- inflammatory response [IBA]
- innate immune response in mucosa [NAS]
- interaction with host [TAS]
- negative regulation of blood pressure [IBA]
- negative regulation of gene expression [IGI]
- nitric oxide biosynthetic process [IDA]
- nitric oxide mediated signal transduction [IBA]
- peptidyl-cysteine S-nitrosylation [ISS]
- phagosome maturation [TAS]
- positive regulation of guanylate cyclase activity [IBA]
- positive regulation of killing of cells of other organism [IMP]
- positive regulation of leukocyte mediated cytotoxicity [TAS]
- positive regulation of vasodilation [IBA]
- regulation of cellular respiration [TAS]
- regulation of insulin secretion [IMP]
- response to bacterium [NAS]
- superoxide metabolic process [ISS]
Gene Ontology Molecular Function- FMN binding [ISS]
- NADP binding [TAS]
- NADPH-hemoprotein reductase activity [IBA]
- arginine binding [ISS]
- flavin adenine dinucleotide binding [ISS]
- heme binding [ISS]
- nitric-oxide synthase activity [IDA]
- protein binding [IPI]
- protein homodimerization activity [ISS]
- receptor binding [IPI]
- tetrahydrobiopterin binding [ISS]
- FMN binding [ISS]
- NADP binding [TAS]
- NADPH-hemoprotein reductase activity [IBA]
- arginine binding [ISS]
- flavin adenine dinucleotide binding [ISS]
- heme binding [ISS]
- nitric-oxide synthase activity [IDA]
- protein binding [IPI]
- protein homodimerization activity [ISS]
- receptor binding [IPI]
- tetrahydrobiopterin binding [ISS]
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: effects of a phosphomimetic CaM mutation.
Nitric oxide synthase (NOS) plays a major role in a number of key physiological and pathological processes. Knowledge of how this is regulated is important. The small acidic calcium binding protein, calmodulin (CaM), is required to fully activate the enzyme. The exact mechanism of how CaM activates NOS is not fully understood. Studies have shown CaM to act like a ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NOS2 CALM1 | 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. | High | - | BioGRID | 833359 | |
| NOS2 CALM1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| CALM1 NOS2 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 798316 | |
| NOS2 CALM1 | 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