ATXN3
Gene Ontology Biological Process
- actin cytoskeleton organization [ISO]
- cellular response to heat [IMP]
- cellular response to misfolded protein [IMP]
- exploration behavior [IMP]
- intermediate filament cytoskeleton organization [ISO]
- microtubule cytoskeleton organization [ISO]
- misfolded or incompletely synthesized protein catabolic process [IMP]
- monoubiquitinated protein deubiquitination [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IMP]
- protein K48-linked deubiquitination [ISO]
- protein K63-linked deubiquitination [ISO]
- proteolysis [ISO]
- regulation of cell-substrate adhesion [IMP, ISO]
- ubiquitin-dependent protein catabolic process [IMP]
Gene Ontology Molecular Function- ATPase binding [ISO]
- Lys48-specific deubiquitinase activity [ISO]
- Lys63-specific deubiquitinase activity [ISO]
- RNA polymerase II regulatory region DNA binding [ISO]
- histone deacetylase activity [ISO]
- identical protein binding [ISO]
- protein binding [IPI]
- ubiquitin protein ligase binding [IPI, ISO]
- ubiquitin thiolesterase activity [IDA]
- ubiquitin-specific protease activity [IDA]
- ATPase binding [ISO]
- Lys48-specific deubiquitinase activity [ISO]
- Lys63-specific deubiquitinase activity [ISO]
- RNA polymerase II regulatory region DNA binding [ISO]
- histone deacetylase activity [ISO]
- identical protein binding [ISO]
- protein binding [IPI]
- ubiquitin protein ligase binding [IPI, ISO]
- ubiquitin thiolesterase activity [IDA]
- ubiquitin-specific protease activity [IDA]
Gene Ontology Cellular Component
UBC
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR).
We describe a high-throughput in-cell nuclear magnetic resonance (NMR)-based method for mapping the structural changes that accompany protein-protein interactions (STINT-NMR). The method entails sequentially expressing two (or more) proteins within a single bacterial cell in a time-controlled manner and monitoring the protein interactions using in-cell NMR spectroscopy. The resulting spectra provide a complete titration of the interaction and define structural ... [more]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- Figure 2b
- Likely protein-protein interaction
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATXN3 UBC | 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 | 1108418 | |
| UBC ATXN3 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | High | - | BioGRID | 2297261 |
Curated By
- BioGRID