BAIT
RPS2
RPS4, SUP138, SUP38, SUP44, ribosomal 40S subunit protein S2, rp12, Ys5, S5, S4, S2, L000002205, YGL123W
Protein component of the small (40S) subunit; essential for control of translational accuracy; phosphorylation by C-terminal domain kinase I (CTDK-I) enhances translational accuracy; methylated on one or more arginine residues by Hmt1p; homologous to mammalian ribosomal protein S2 and bacterial S5
GO Process (2)
GO Function (2)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
ALD6
ALD1, aldehyde dehydrogenase (NADP(+)) ALD6, L000003206, YPL061W
Cytosolic aldehyde dehydrogenase; activated by Mg2+ and utilizes NADP+ as the preferred coenzyme; required for conversion of acetaldehyde to acetate; constitutively expressed; locates to the mitochondrial outer surface upon oxidative stress
GO Process (3)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- cytosol [IDA, IMP]
- mitochondrion [IDA]
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
Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.
Dedicated chaperones protect newly synthesized ribosomal proteins (r-proteins) from aggregation and accompany them on their way to assembly into nascent ribosomes. Currently, only nine of the ?80 eukaryotic r-proteins are known to be guarded by such chaperones. In search of new dedicated r-protein chaperones, we performed a tandem-affinity purification based screen and looked for factors co-enriched with individual small subunit ... [more]
Nucleic Acids Res. Dec. 26, 2018; 47(13);6984-7002 [Pubmed: 31062022]
Throughput
- High Throughput
Curated By
- BioGRID