TMSB4X
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ACTG1
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- adherens junction organization [TAS]
- axon guidance [TAS]
- cell junction assembly [TAS]
- cell-cell junction organization [TAS]
- cellular component movement [TAS]
- innate immune response [TAS]
- membrane organization [TAS]
- platelet aggregation [IMP]
- retina homeostasis [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
The actin binding site of thymosin beta 4 mapped by mutational analysis.
We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants. The N-terminal part (residues 1-16) and a hexapeptide motif (residues 17-22) form separate structural entities. In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex ... [more]
Throughput
- Low Throughput
Additional Notes
- ACG1 from rabbit
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ACTG1 TMSB4X | Co-crystal Structure 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. | Low | - | BioGRID | - | |
| TMSB4X ACTG1 | 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 | 3745523 |
Curated By
- BioGRID