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 | |
| ACTB GSN | Cross-Linking-MS (XL-MS) 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). | High | - | BioGRID | 3724133 |
Curated By
- BioGRID