TRIM28
Gene Ontology Biological Process
- DNA repair [IDA]
- epithelial to mesenchymal transition [ISS]
- gene expression [TAS]
- innate immune response [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of viral release from host cell [IDA]
- positive regulation of DNA repair [IDA]
- positive regulation of transcription factor import into nucleus [IDA]
- positive regulation of transcription, DNA-templated [ISS]
- protein oligomerization [IDA]
- protein sumoylation [IDA]
- protein ubiquitination [IDA]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- DNA binding [IDA]
- Krueppel-associated box domain binding [IDA]
- chromo shadow domain binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- sequence-specific DNA binding transcription factor activity [ISS]
- transcription corepressor activity [IDA]
- ubiquitin protein ligase binding [IDA]
- ubiquitin-protein transferase activity [IDA]
- zinc ion binding [IDA]
- DNA binding [IDA]
- Krueppel-associated box domain binding [IDA]
- chromo shadow domain binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- sequence-specific DNA binding transcription factor activity [ISS]
- transcription corepressor activity [IDA]
- ubiquitin protein ligase binding [IDA]
- ubiquitin-protein transferase activity [IDA]
- zinc ion binding [IDA]
ZNF74
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Acetylation-Mimic Mutation of TRIM28-Lys304 to Gln Attenuates the Interaction with KRAB-Zinc-Finger Proteins and Affects Gene Expression in Leukemic K562 Cells.
TRIM28/KAP1/TIF1? is a crucial epigenetic modifier. Genetic ablation of trim28 is embryonic lethal, although RNAi-mediated knockdown in somatic cells yields viable cells. Reduction in TRIM28 abundance at the cellular or organismal level results in polyphenism. Posttranslational modifications such as phosphorylation and sumoylation have been shown to regulate TRIM28 activity. Moreover, several lysine residues of TRIM28 are subject to acetylation, but ... [more]
Throughput
- High Throughput
Additional Notes
- Affinity capture MS was carried out to identify protein interactors of TRIM28 and a TRIM28 acetylation mimic
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM28 ZNF74 | 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 | 3374021 | |
| ZNF74 TRIM28 | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | - | |
| TRIM28 ZNF74 | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | 3201171 |
Curated By
- BioGRID