BAIT
RPL37A
ribosomal 60S subunit protein L37A, L37e, YL35, L43, L37A, L000002884, YLR185W
Ribosomal 60S subunit protein L37A; homologous to mammalian ribosomal protein L37, no bacterial homolog; RPL37A has a paralog, RPL37B, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
CHD1
chromatin-remodeling ATPase CHD1, L000003467, YER164W
Chromatin remodeler that regulates various aspects of transcription; acts in in conjunction with Isw1b to regulate chromatin structure and maintain chromatin integrity during transcription elongation by RNAP II by preventing trans-histone exchange over coding regions; contains a chromo domain, a helicase domain and a DNA-binding domain; component of both the SAGA and SLIK complexes
GO Process (14)
GO Function (6)
GO Component (5)
Gene Ontology Biological Process
- ATP-dependent chromatin remodeling [IDA]
- chromatin organization involved in regulation of transcription [IGI, IMP]
- histone H2B conserved C-terminal lysine ubiquitination [IMP]
- negative regulation of DNA-dependent DNA replication [IGI]
- negative regulation of histone H3-K14 acetylation [IMP]
- negative regulation of histone H3-K9 acetylation [IMP]
- negative regulation of histone exchange [IMP]
- nucleosome mobilization [IDA]
- nucleosome positioning [IDA, IGI]
- regulation of chromatin organization [IMP]
- regulation of transcriptional start site selection at RNA polymerase II promoter [IGI]
- termination of RNA polymerase I transcription [IGI]
- termination of RNA polymerase II transcription [IGI, IMP]
- transcription elongation from RNA polymerase II promoter [IGI, IPI]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
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 social and structural architecture of the yeast protein interactome.
Cellular functions are mediated by protein-protein interactions, and mapping the interactome provides fundamental insights into biological systems. Affinity purification coupled to mass spectrometry is an ideal tool for such mapping, but it has been difficult to identify low copy number complexes, membrane complexes and complexes that are disrupted by protein tagging. As a result, our current knowledge of the interactome ... [more]
Nature Nov. 15, 2023; (); [Pubmed: 37968396]
Quantitative Score
- 2.0 [Score_FDR+correlation]
Throughput
- High Throughput
Additional Notes
- Protein interactions were identified using statistically significant enrichment of the proteins in the forward and reverse pull-downs, as well as making use of the profile similarities of interacting proteins in a correlation analysis. High confidence interactions have a total score >=2. This score is a sum of the FDR score of the forward pull-down + FDR score of the reverse pull-down + correlation score.
Curated By
- BioGRID