KIN28
Gene Ontology Biological Process
- 7-methylguanosine mRNA capping [IMP]
- phosphorylation of RNA polymerase II C-terminal domain [IDA, IMP]
- phosphorylation of RNA polymerase II C-terminal domain involved in recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex [IMP, IPI]
- phosphorylation of RNA polymerase II C-terminal domain serine 5 residues involved in recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein phosphorylation [IDA]
- transcription from RNA polymerase I promoter [IMP]
- transcription from RNA polymerase II promoter [IDA, IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RTT106
Gene Ontology Biological Process
- DNA replication-dependent nucleosome assembly [IGI]
- DNA replication-independent nucleosome assembly [IMP]
- heterochromatin assembly involved in chromatin silencing [IGI, IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- transcription elongation from RNA polymerase II promoter [IGI, IMP]
Gene Ontology Molecular Function
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes.
Protein kinases are key regulators of cellular processes. In spite of considerable effort, a full understanding of the pathways they participate in remains elusive. We globally investigated the proteins that interact with the majority of yeast protein kinases using protein microarrays. Eighty-five kinases were purified and used to probe yeast proteome microarrays. One-thousand-twenty-three interactions were identified, and the vast majority ... [more]
Throughput
- High Throughput
Additional Notes
- High Throughput: Proteome microarrays were used to identify proteins that interact with protein kinases.
Curated By
- BioGRID