GSN
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ACTB
Gene Ontology Biological Process
- 'de novo' posttranslational protein folding [TAS]
- ATP-dependent chromatin remodeling [IDA]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- adherens junction organization [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell junction assembly [TAS]
- cell-cell junction organization [TAS]
- cellular component movement [TAS]
- cellular protein metabolic process [TAS]
- chromatin organization [TAS]
- innate immune response [TAS]
- membrane organization [TAS]
- platelet aggregation [IMP]
- protein folding [TAS]
- retina homeostasis [IEP]
- substantia nigra development [IEP]
Gene Ontology Molecular Function- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- Tat protein binding [IPI]
- kinesin binding [IPI]
- nitric-oxide synthase binding [IPI]
- nucleosomal DNA binding [IDA]
- protein binding [IPI]
- structural constituent of cytoskeleton [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- Tat protein binding [IPI]
- kinesin binding [IPI]
- nitric-oxide synthase binding [IPI]
- nucleosomal DNA binding [IDA]
- protein binding [IPI]
- structural constituent of cytoskeleton [TAS]
Gene Ontology Cellular Component
- MLL5-L complex [IDA]
- NuA4 histone acetyltransferase complex [IDA]
- blood microparticle [IDA]
- cytoplasm [TAS]
- cytoplasmic ribonucleoprotein granule [IDA]
- cytoskeleton [TAS]
- cytosol [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- membrane [IDA]
- nuclear chromatin [IDA]
- nucleoplasm [TAS]
- protein complex [IDA]
- ribonucleoprotein complex [IDA]
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 N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF.
The actin filament-severing functionality of gelsolin resides in its N-terminal three domains (G1-G3). We have determined the structure of this fragment in complex with an actin monomer. The structure reveals the dramatic domain rearrangements that activate G1-G3, which include the replacement of interdomain interactions observed in the inactive, calcium-free protein by new contacts to actin, and by a novel G2-G3 ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ACTB GSN | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | - | BioGRID | 3347396 | |
| ACTB GSN | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | 0.9997 | BioGRID | 3029765 | |
| ACTB GSN | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | 0.4793 | BioGRID | 3241927 |
Curated By
- BioGRID