KPNA1
Gene Ontology Biological Process
Gene Ontology Molecular Function
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]
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
Identification and characterization of a nuclear localization signal of TRIM28 that overlaps with the HP1 box.
Tripartite motif-containing 28 (TRIM28) is a transcription regulator, which forms a repressor complex containing heterochromatin protein 1 (HP1). Here, we report identification of a nuclear localization signal (NLS) within the 462-494 amino acid region of TRIM28 that overlaps with its HP1 binding site, HP1 box. GST-pulldown experiments revealed the interaction of the arginine-rich TRIM28 NLS with various importin α subtypes ... [more]
Throughput
- Low Throughput
Additional Notes
- Figure 2
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM28 KPNA1 | Reconstituted Complex 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. | Low | - | BioGRID | 1512960 |
Curated By
- BioGRID