BARD1
Gene Ontology Biological Process
- cell cycle arrest [NAS]
- cellular response to DNA damage stimulus [NAS]
- negative regulation of apoptotic process [IMP]
- negative regulation of mRNA 3'-end processing [NAS]
- negative regulation of protein export from nucleus [IDA]
- positive regulation of apoptotic process [IMP]
- positive regulation of protein catabolic process [NAS]
- protein K6-linked ubiquitination [IDA]
- protein ubiquitination [NAS]
- regulation of phosphorylation [IMP]
- tissue homeostasis [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
POLR2H
Gene Ontology Biological Process
- 7-methylguanosine mRNA capping [TAS]
- DNA repair [TAS]
- RNA splicing [TAS]
- gene expression [TAS]
- innate immune response [TAS]
- mRNA splicing, via spliceosome [TAS]
- nucleotide-excision repair [TAS]
- positive regulation of type I interferon production [TAS]
- positive regulation of viral transcription [TAS]
- termination of RNA polymerase I transcription [TAS]
- termination of RNA polymerase III transcription [TAS]
- transcription elongation from RNA polymerase I promoter [TAS]
- transcription elongation from RNA polymerase II promoter [TAS]
- transcription elongation from RNA polymerase III promoter [TAS]
- transcription from RNA polymerase I promoter [TAS]
- transcription from RNA polymerase II promoter [IDA, TAS]
- transcription from RNA polymerase III promoter [TAS]
- transcription initiation from RNA polymerase I promoter [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription-coupled nucleotide-excision repair [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Ubiquitination)
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
Intrinsic disorder drives N-terminal ubiquitination by Ube2w.
Ubiquitination of the αN-terminus of protein substrates has been reported sporadically since the early 1980s. However, the identity of an enzyme responsible for this unique ubiquitin (Ub) modification has only recently been elucidated. We show the Ub-conjugating enzyme (E2) Ube2w uses a unique mechanism to facilitate the specific ubiquitination of the α-amino group of its substrates that involves recognition of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| POLR2H BARD1 | 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 | - | |
| BARD1 POLR2H | 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 | 573153 |
Curated By
- BioGRID