BAIT
KIN28
TFIIH complex serine/threonine-protein kinase subunit KIN28, L000000905, YDL108W
Serine/threonine protein kinase, subunit of transcription factor TFIIH; involved in transcription initiation at RNA polymerase II promoters; phosphorylates Ser5 residue of the PolII C-terminal domain (CTD) at gene promoters; relocalizes to the cytosol in response to hypoxia
GO Process (8)
GO Function (4)
GO Component (4)
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
Saccharomyces cerevisiae (S288c)
PREY
RPP2B
RPL45, YPA1, ribosomal protein P2B, YP2beta, P2B, L45, L000001736, YDR382W
Ribosomal protein P2 beta; a component of the ribosomal stalk, which is involved in the interaction between translational elongation factors and the ribosome; free (non-ribosomal) P2 stimulates the phosphorylation of the eIF2 alpha subunit (Sui2p) by Gcn2p; regulates the accumulation of P1 (Rpp1Ap and Rpp1Bp) in the cytoplasm
GO Process (2)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
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]
Genes Dev. Apr. 01, 2011; 25(7);767-78 [Pubmed: 21460040]
Throughput
- High Throughput
Additional Notes
- High Throughput: Proteome microarrays were used to identify proteins that interact with protein kinases.
Curated By
- BioGRID