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
AMPH
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.
Membrane remodeling by BAR (Bin, Amphiphysin, RVS) domain-containing proteins, such as endophilins and amphiphysins, is integral to the process of endocytosis. However, little is known about the regulation of endocytic BAR domain activity. We have identified an interaction between the yeast Rvs167 N-BAR domain and calmodulin. Calmodulin-binding mutants of Rvs167 exhibited defects in endocytic vesicle release. In vitro, calmodulin enhanced ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID