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
TRIM24
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Cross-talk between chromatin acetylation and SUMOylation of tripartite motif-containing protein 24 (TRIM24) impacts cell adhesion.
Proteins with domains that recognize and bind post-translational modifications (PTMs) of histones are collectively termed epigenetic readers. Numerous interactions between specific reader protein domains and histone PTMs and their regulatory outcomes have been reported, but little is known about how reader proteins may in turn be modulated by these interactions. Tripartite motif-containing protein 24 (TRIM24) is a histone reader aberrantly ... [more]
Throughput
- Low Throughput
Additional Notes
- in vitro sumoylation using UBA2/SAE1 as E1, Ubc9 as E2, SUMO1 as modifier and TRIM24 as substrate
Curated By
- BioGRID