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]
NPM1
Gene Ontology Biological Process
- CENP-A containing nucleosome assembly [TAS]
- DNA repair [IDA]
- cell aging [IMP, ISS]
- centrosome cycle [IMP, ISS]
- intracellular protein transport [TAS]
- negative regulation of apoptotic process [IDA, NAS]
- negative regulation of cell proliferation [IMP, ISS]
- negative regulation of centrosome duplication [IMP]
- negative regulation of protein kinase activity by regulation of protein phosphorylation [IDA]
- nucleocytoplasmic transport [IDA, TAS]
- nucleosome assembly [IDA, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of translation [IDA]
- protein localization [IDA]
- protein oligomerization [IDA]
- regulation of centriole replication [IMP]
- regulation of eIF2 alpha phosphorylation by dsRNA [IDA]
- regulation of endodeoxyribonuclease activity [IDA]
- regulation of endoribonuclease activity [IDA]
- response to stress [IMP]
- ribosome assembly [TAS]
- signal transduction [NAS]
- viral process [TAS]
Gene Ontology Molecular Function- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
Gene Ontology Cellular Component
Biochemical Activity (Sumoylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
TRIM28 Is an E3 Ligase for ARF-Mediated NPM1/B23 SUMOylation That Represses Centrosome Amplification.
The tumor suppressor ARF enhances the SUMOylation of target proteins; however, the physiological function of ARF-mediated SUMOylation has been unclear due to the lack of a known, associated E3 SUMO ligase. Here we uncover TRIM28/KAP1 as a novel ARF-binding protein and SUMO E3 ligase for NPM1/B23. ARF and TRIM28 cooperate to SUMOylate NPM1, a nucleolar protein that regulates centrosome duplication ... [more]
Throughput
- Low Throughput
Additional Notes
- E2: Ubc9
- sumoylation enhanced by the presence of ARF
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NPM1 TRIM28 | 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 | - | |
| TRIM28 NPM1 | 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 | - | |
| NPM1 TRIM28 | 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 | 3764248 |
Curated By
- BioGRID