ANK1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TTN
Gene Ontology Biological Process
- blood coagulation [TAS]
- cardiac muscle contraction [IMP]
- cardiac muscle fiber development [IMP]
- cardiac muscle hypertrophy [IMP]
- cardiac muscle tissue morphogenesis [IMP]
- cardiac myofibril assembly [IMP]
- detection of muscle stretch [TAS]
- mitotic chromosome condensation [IEP]
- muscle contraction [NAS, TAS]
- muscle filament sliding [TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- regulation of catalytic activity [IMP]
- regulation of protein kinase activity [IMP]
- response to calcium ion [IDA]
- sarcomere organization [IMP]
- sarcomerogenesis [IMP]
- skeletal muscle myosin thick filament assembly [IMP]
- skeletal muscle thin filament assembly [IMP]
- striated muscle contraction [TAS]
Gene Ontology Molecular Function- actin filament binding [IDA]
- actinin binding [IDA, IPI]
- calcium ion binding [IDA]
- calmodulin binding [IPI, TAS]
- enzyme binding [IPI]
- identical protein binding [IPI]
- muscle alpha-actinin binding [IPI]
- protease binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- protein self-association [IDA]
- protein serine/threonine kinase activity [IDA]
- structural constituent of muscle [IMP, TAS]
- structural molecule activity conferring elasticity [TAS]
- telethonin binding [IPI, ISS]
- actin filament binding [IDA]
- actinin binding [IDA, IPI]
- calcium ion binding [IDA]
- calmodulin binding [IPI, TAS]
- enzyme binding [IPI]
- identical protein binding [IPI]
- muscle alpha-actinin binding [IPI]
- protease binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- protein self-association [IDA]
- protein serine/threonine kinase activity [IDA]
- structural constituent of muscle [IMP, TAS]
- structural molecule activity conferring elasticity [TAS]
- telethonin binding [IPI, ISS]
Gene Ontology Cellular Component
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin.
Little is known about the mechanisms that organize the internal membrane systems in eukaryotic cells. We are addressing this question in striated muscle, which contains two novel systems of internal membranes, the transverse tubules and the sarcoplasmic reticulum (SR). Small ankyrin-1 (sAnk1) is an approximately 17-kDa transmembrane protein of the SR that concentrates around the Z-disks and M-lines of each ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TTN ANK1 | 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 | - | |
| ANK1 TTN | 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