BAIT
CALM1
CALML2, CAMI, CPVT4, DD132, PHKD, caM
calmodulin 1 (phosphorylase kinase, delta)
GO Process (43)
GO Function (11)
GO Component (13)
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
Homo sapiens
PREY
CACNA1C
CACH2, CACN2, CACNL1A1, CCHL1A1, CaV1.2, LQT8, TS
calcium channel, voltage-dependent, L type, alpha 1C subunit
GO Process (11)
GO Function (5)
GO Component (6)
Gene Ontology Biological Process
- axon guidance [TAS]
- calcium ion import [IBA]
- calcium ion transport into cytosol [TAS]
- calcium-mediated signaling using extracellular calcium source [TAS]
- cell communication by electrical coupling involved in cardiac conduction [TAS]
- energy reserve metabolic process [TAS]
- membrane depolarization during action potential [IBA]
- positive regulation of cytosolic calcium ion concentration [IDA]
- regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [TAS]
- regulation of insulin secretion [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
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 of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.
Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2 Ca2+ channel require calmodulin binding to a putative IQ motif in the carboxy-terminal tail of the pore-forming subunit. We present the 1.45 A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v)1.2. This structure shows that parallel binding of calmodulin to the IQ ... [more]
Structure Dec. 01, 2005; 13(12);1881-6 [Pubmed: 16338416]
Throughput
- Low Throughput
Additional Notes
- protein-peptide complex.
Curated By
- BioGRID