TERF2
Gene Ontology Biological Process
- age-dependent telomere shortening [NAS]
- cellular senescence [NAS]
- negative regulation of telomere maintenance [IDA, IMP]
- negative regulation of telomere maintenance via semi-conservative replication [NAS]
- protection from non-homologous end joining at telomere [IMP]
- protein localization to chromosome, telomeric region [IMP]
- telomere capping [IMP, NAS]
- telomere maintenance [IMP, TAS]
- telomere maintenance via telomerase [IC]
- telomeric loop formation [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
EP300
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- N-terminal peptidyl-lysine acetylation [IDA]
- Notch signaling pathway [TAS]
- apoptotic process [IMP]
- cellular response to hypoxia [TAS]
- chromatin organization [TAS]
- circadian rhythm [ISS]
- histone H2B acetylation [IDA]
- histone H4 acetylation [IMP]
- innate immune response [TAS]
- internal peptidyl-lysine acetylation [IDA]
- internal protein amino acid acetylation [IDA]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [IDA]
- mitotic cell cycle [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- nervous system development [TAS]
- positive regulation by host of viral transcription [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response [ISS]
- positive regulation of type I interferon production [TAS]
- protein stabilization [ISS]
- regulation of androgen receptor signaling pathway [IDA]
- regulation of cell cycle [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of transcription, DNA-templated [IDA]
- regulation of tubulin deacetylation [IDA]
- response to estrogen [IDA]
- response to hypoxia [IDA]
Gene Ontology Molecular Function- DNA binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- acetyltransferase activity [IDA, IMP]
- activating transcription factor binding [IPI]
- androgen receptor binding [IPI]
- beta-catenin binding [IPI]
- chromatin binding [IMP]
- core promoter binding [IDA]
- histone acetyltransferase activity [IDA]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA]
- nuclear hormone receptor binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- transferase activity, transferring acyl groups [IDA]
- DNA binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- acetyltransferase activity [IDA, IMP]
- activating transcription factor binding [IPI]
- androgen receptor binding [IPI]
- beta-catenin binding [IPI]
- chromatin binding [IMP]
- core promoter binding [IDA]
- histone acetyltransferase activity [IDA]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA]
- nuclear hormone receptor binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- transferase activity, transferring acyl groups [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
p300-mediated acetylation of TRF2 is required for maintaining functional telomeres.
The human telomeric protein TRF2 is required to protect chromosome ends by facilitating their organization into the protective capping structure. Post-translational modifications of TRF2 such as phosphorylation, ubiquitination, SUMOylation, methylation and poly(ADP-ribosyl)ation have been shown to play important roles in telomere function. Here we show that TRF2 specifically interacts with the histone acetyltransferase p300, and that p300 acetylates the lysine ... [more]
Throughput
- Low Throughput
Additional Notes
- Figure 2D
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EP300 TERF2 | 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 | 1036469 | |
| TERF2 EP300 | 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 | 1036471 | |
| EP300 TERF2 | 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 | 1036475 |
Curated By
- BioGRID