MDM2
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [IMP, TAS]
- Fc-epsilon receptor signaling pathway [TAS]
- cellular response to hypoxia [IEP]
- epidermal growth factor receptor signaling pathway [TAS]
- establishment of protein localization [IDA]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- negative regulation of DNA damage response, signal transduction by p53 class mediator [IDA]
- negative regulation of cell cycle arrest [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- neurotrophin TRK receptor signaling pathway [TAS]
- peptidyl-lysine modification [IMP]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of cell proliferation [TAS]
- positive regulation of mitotic cell cycle [IMP]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- protein complex assembly [IDA]
- protein destabilization [IDA]
- protein localization to nucleus [IDA]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IDA]
- regulation of protein catabolic process [IDA]
- response to antibiotic [IEP]
- synaptic transmission [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HIST2H2BE
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
The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression.
Histone modifications play a pivotal role in regulating transcription and other chromatin-associated processes. In yeast, histone H2B monoubiquitylation affects gene silencing. However, mammalian histone ubiquitylation remains poorly understood. We report that the Mdm2 oncoprotein, a RING domain E3 ubiquitin ligase known to ubiquitylate the p53 tumor suppressor protein, can interact directly with histones and promote in vitro monoubiquitylation of histones ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HIST2H2BE MDM2 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| MDM2 HIST2H2BE | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 470961 |
Curated By
- BioGRID