ING4
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [IDA]
- DNA replication [IDA]
- apoptotic process [IDA]
- cell cycle arrest [IDA]
- chromatin organization [TAS]
- histone H3 acetylation [IDA]
- histone H4-K12 acetylation [IDA]
- histone H4-K16 acetylation [IDA]
- histone H4-K5 acetylation [IDA]
- histone H4-K8 acetylation [IDA]
- negative regulation of cell proliferation [IDA]
- negative regulation of growth [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- positive regulation of apoptotic process [IDA]
- protein acetylation [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HIST1H3A
Gene Ontology Biological Process
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
Inhibitor of Growth 4 (ING4) is a positive regulator of rRNA synthesis.
Ribosome biogenesis is essential for maintaining basic cellular activities although its mechanism is not fully understood. Inhibitor of growth 4 (ING4) is a member of ING family while its cellular functions remain controversial. Here, we identified several nucleolar proteins as novel ING4 interacting proteins. ING4 localized in the nucleus with strong accumulation in the nucleolus through its plant homeodomain, which ... [more]
Throughput
- Low Throughput
Additional Notes
- assayed using GST (glutathione S-transferase) pull-down experiments
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ING4 HIST1H3A | 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 | - | |
| ING4 HIST1H3A | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| ING4 HIST1H3A | 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 | 1051370 |
Curated By
- BioGRID