UBE2I
Gene Ontology Biological Process
- cellular protein metabolic process [TAS]
- cellular protein modification process [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of transcription, DNA-templated [IDA]
- post-translational protein modification [TAS]
- protein sumoylation [IDA, TAS]
- protein ubiquitination [IBA]
- ubiquitin-dependent protein catabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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
PIAS1-mediated sumoylation promotes STUbL-dependent proteasomal degradation of the human telomeric protein TRF2.
The human telomeric protein TRF2 protects chromosome ends by facilitating their organization into the protective capping structure. Here we show that the stability of TRF2 is regulated via modification by the small ubiquitin-like modifiers (SUMO). TRF2 specifically interacts with and is sumoylated by PIAS1 in mammalian cells. The proteasome inhibitor stabilizes SUMO-conjugated TRF2 without affecting the level of unmodified TRF2, ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID