SSU72
Gene Ontology Biological Process
- dephosphorylation of RNA polymerase II C-terminal domain [IDA, IMP]
- mRNA 3'-end processing [IMP]
- mRNA cleavage [IMP]
- snoRNA transcription [IMP]
- termination of RNA polymerase II transcription [IMP]
- termination of RNA polymerase II transcription, exosome-dependent [IMP, IPI]
- termination of RNA polymerase II transcription, poly(A)-coupled [IMP, IPI]
- transcription antitermination [IMP]
- transcription elongation from RNA polymerase II promoter [IGI, IMP]
- transcription initiation from RNA polymerase II promoter [IGI, IPI]
- transcriptional start site selection at RNA polymerase II promoter [IGI, IMP]
Gene Ontology Molecular Function
SYC1
Gene Ontology Biological Process
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
Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination.
The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an important role in coordinating stage-specific recruitment and release of cellular machines during transcription. Dynamic placement and removal of phosphorylation marks on different residues of a repeating heptapeptide (YSPTSPS) of the CTD underlies the engagement of relevant cellular machinery. Whereas sequential placement of phosphorylation marks ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| SSU72 SYC1 | Affinity Capture-MS 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. | Low | - | BioGRID | - | |
| SYC1 SSU72 | Affinity Capture-MS 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. | High | - | BioGRID | - | |
| SYC1 SSU72 | Affinity Capture-MS 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. | Low | - | BioGRID | - | |
| SYC1 SSU72 | Affinity Capture-MS 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. | High | 3 | BioGRID | 3606072 | |
| SSU72 SYC1 | Affinity Capture-MS 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. | Low | - | BioGRID | - | |
| SYC1 SSU72 | Affinity Capture-MS 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. | Low | - | BioGRID | - | |
| SSU72 SYC1 | Negative Genetic Negative Genetic Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores. | High | -0.1201 | BioGRID | 2011494 |
Curated By
- BioGRID