LARP7
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CSNK2A1
Gene Ontology Biological Process
- axon guidance [TAS]
- chaperone-mediated protein folding [TAS]
- mitotic cell cycle [TAS]
- mitotic spindle checkpoint [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- positive regulation of Wnt signaling pathway [IMP]
- positive regulation of cell growth [IDA]
- positive regulation of cell proliferation [IDA]
- positive regulation of protein catabolic process [IDA]
- protein phosphorylation [IDA]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
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 is identified by mass spectrometric methods.
Publication
The HIV-1 Tat protein recruits a ubiquitin ligase to reorganize the 7SK snRNP for transcriptional activation.
The HIV-1 Tat protein hijacks P-TEFb kinase to activate paused RNA polymerase II (RNAP II) at the viral promoter. Tat binds additional host factors, but it is unclear how they regulate RNAP II elongation. Here, we identify the cytoplasmic ubiquitin ligase UBE2O as critical for Tat transcriptional activity. Tat hijacks UBE2O to ubiquitinate the P-TEFb kinase inhibitor HEXIM1 of the ... [more]
Throughput
- High Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
CSNK2A1 LARP7 | 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. | High | - | BioGRID | 829366 |
Curated By
- BioGRID