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
ADAR
Gene Ontology Biological Process
- adenosine to inosine editing [IDA, IMP, TAS]
- base conversion or substitution editing [IDA]
- cytokine-mediated signaling pathway [TAS]
- gene expression [TAS]
- innate immune response [TAS]
- mRNA modification [TAS]
- miRNA loading onto RISC involved in gene silencing by miRNA [IDA]
- negative regulation of protein kinase activity by regulation of protein phosphorylation [IDA, IMP]
- positive regulation of viral genome replication [IDA, IMP]
- pre-miRNA processing [IDA]
- protein export from nucleus [IDA]
- protein import into nucleus [IDA]
- response to interferon-alpha [IDA]
- response to virus [IMP]
- type I interferon signaling pathway [TAS]
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
SUMO-1 modification alters ADAR1 editing activity.
We identify ADAR1, an RNA-editing enzyme with transient nucleolar localization, as a novel substrate for sumoylation. We show that ADAR1 colocalizes with SUMO-1 in a subnucleolar region that is distinct from the fibrillar center, the dense fibrillar component, and the granular component. Our results further show that human ADAR1 is modified by SUMO-1 on lysine residue 418. An arginine substitution ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID