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
MIP
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Protein-peptide
An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.
Publication
Calmodulin site at the C-terminus of the putative lens gap junction protein MIP26.
Lens fiber junctions contain cell-to-cell channels believed to be composed of a 28.2 kD protein (MIP26). Previous evidence indicates that calmodulin (CaM) is involved in the regulation of channel permeability by changing the conformation of the C terminal chain of MIP26. A study of the amino acid sequence of MIP26 has revealed an amphiphilic segment of the C-terminal chain with ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| MIP 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