SRB2
Gene Ontology Biological Process
- RNA polymerase II transcriptional preinitiation complex assembly [IDA]
- negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to chemical stimulus [IMP]
- negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
Gene Ontology Molecular Function- RNA polymerase II transcription coactivator activity involved in preinitiation complex assembly [IDA]
- RNA polymerase II transcription factor recruiting transcription factor activity [IMP]
- TBP-class protein binding RNA polymerase II transcription factor activity involved in preinitiation complex assembly [IDA]
- core RNA polymerase II binding transcription factor activity [IDA, IGI]
- protein domain specific binding [IGI]
- RNA polymerase II transcription coactivator activity involved in preinitiation complex assembly [IDA]
- RNA polymerase II transcription factor recruiting transcription factor activity [IMP]
- TBP-class protein binding RNA polymerase II transcription factor activity involved in preinitiation complex assembly [IDA]
- core RNA polymerase II binding transcription factor activity [IDA, IGI]
- protein domain specific binding [IGI]
Gene Ontology Cellular Component
MED8
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
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Identification of protein-protein interactions often provides insight into protein function, and many cellular processes are performed by stable protein complexes. We used tandem affinity purification to process 4,562 different tagged proteins of the yeast Saccharomyces cerevisiae. Each preparation was analysed by both matrix-assisted laser desorption/ionization-time of flight mass spectrometry and liquid chromatography tandem mass spectrometry to increase coverage and accuracy. ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| MED8 SRB2 | 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 | - | |
| MED8 SRB2 | 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 | 8 | BioGRID | 3618873 | |
| MED8 SRB2 | 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 | 1518332 | |
| MED8 SRB2 | 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 | - | |
| MED8 SRB2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| MED8 SRB2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
| MED8 SRB2 | 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 | -0.1368 | BioGRID | 1962001 |
Curated By
- BioGRID