HNRNPA2B1
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
Cross-Linking-MS (XL-MS)
An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).
Publication
Protein interaction landscapes revealed by advanced in vivo cross-linking-mass spectrometry.
Defining protein-protein interactions (PPIs) in their native environment is crucial to understanding protein structure and function. Cross-linking-mass spectrometry (XL-MS) has proven effective in capturing PPIs in living cells; however, the proteome coverage remains limited. Here, we have developed a robust in vivo XL-MS platform to facilitate in-depth PPI mapping by integrating a multifunctional MS-cleavable cross-linker with sample preparation strategies and ... [more]
Throughput
- High Throughput
Additional Notes
- In vivo cross-linking-mass spectrometry (XL-MS) was carried out in HEK-293 cells using the cross-linking reagent Alkyne-A-DSBSO (Azide/Alkyne-tagged, acid-cleavable disuccinimidyl bissulfoxide). High confidence protein interactions were identified based on cross-linked peptides having an FDR < 1%.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HNRNPA2B1 TTN | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 2783822 |
Curated By
- BioGRID