RYR1
Gene Ontology Biological Process
- calcium ion transport [ISS]
- cellular response to caffeine [ISS]
- cytosolic calcium ion homeostasis [ISS]
- ion transmembrane transport [TAS]
- muscle contraction [ISS]
- ossification involved in bone maturation [ISS]
- outflow tract morphogenesis [ISS]
- release of sequestered calcium ion into cytosol [ISS]
- release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [ISS]
- response to caffeine [ISS]
- response to hypoxia [IDA]
- skeletal muscle fiber development [ISS]
- skin development [ISS]
- transmembrane transport [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
FKBP1A
Gene Ontology Biological Process
- 'de novo' protein folding [TAS]
- SMAD protein complex assembly [IDA]
- T cell activation [NAS]
- amyloid fibril formation [IDA]
- calcium ion transmembrane transport [NAS]
- chaperone-mediated protein folding [IBA]
- extracellular fibril organization [IDA]
- heart morphogenesis [ISS]
- heart trabecula formation [ISS]
- negative regulation of protein phosphatase type 2B activity [IDA]
- negative regulation of release of sequestered calcium ion into cytosol [IDA]
- negative regulation of ryanodine-sensitive calcium-release channel activity [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- positive regulation of protein binding [IDA]
- positive regulation of protein ubiquitination [IDA]
- protein folding [NAS]
- protein maturation by protein folding [TAS]
- protein peptidyl-prolyl isomerization [IDA]
- protein refolding [TAS]
- regulation of activin receptor signaling pathway [IDA]
- regulation of amyloid precursor protein catabolic process [IGI]
- regulation of immune response [IMP]
- regulation of protein localization [IGI]
- regulation of ryanodine-sensitive calcium-release channel activity [IDA, ISS]
- transforming growth factor beta receptor signaling pathway [TAS]
- ventricular cardiac muscle tissue morphogenesis [ISS]
Gene Ontology Molecular Function- FK506 binding [IDA, NAS]
- SMAD binding [IPI]
- activin binding [IPI]
- calcium channel inhibitor activity [IDA]
- ion channel binding [ISS, TAS]
- macrolide binding [NAS]
- peptidyl-prolyl cis-trans isomerase activity [IDA, TAS]
- protein binding [IPI]
- signal transducer activity [IMP]
- transforming growth factor beta receptor binding [ISS, TAS]
- type I transforming growth factor beta receptor binding [ISS]
- FK506 binding [IDA, NAS]
- SMAD binding [IPI]
- activin binding [IPI]
- calcium channel inhibitor activity [IDA]
- ion channel binding [ISS, TAS]
- macrolide binding [NAS]
- peptidyl-prolyl cis-trans isomerase activity [IDA, TAS]
- protein binding [IPI]
- signal transducer activity [IMP]
- transforming growth factor beta receptor binding [ISS, TAS]
- type I transforming growth factor beta receptor binding [ISS]
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
FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes.
The skeletal muscle sarcoplasmic reticulum (SR) Ca2+ release channel or ryanodine receptor (RyR1) binds four molecules of FKBP12, and the interaction of FKBP12 with RyR1 regulates both unitary and coupled gating of the channel. We have characterized the physiologic effects of previously identified mutations in RyR1 that disrupt FKBP12 binding (V2461G and V2461I) on excitation-contraction (EC) coupling and intracellular Ca2+ ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RYR1 FKBP1A | Affinity Capture-Western 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. | Low | - | BioGRID | - | |
| FKBP1A RYR1 | 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 | - | |
| RYR1 FKBP1A | 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