BAIT
KCNN2
KCa2.2, SK2, SKCA2, SKCa 2, hSK2
potassium intermediate/small conductance calcium-activated channel, subfamily N, member 2
GO Process (4)
GO Function (5)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
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
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 the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin.
Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening ... [more]
Nature Apr. 26, 2001; 410(6832);1120-4 [Pubmed: 11323678]
Throughput
- Low Throughput
Curated By
- BioGRID