BAIT

EUG1

protein disulfide isomerase EUG1, L000000589, YDR518W
Protein disulfide isomerase of the endoplasmic reticulum lumen; EUG1 has a paralog, PDI1, that arose from the whole genome duplication; function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER
GO Process (1)
GO Function (5)
GO Component (1)
Saccharomyces cerevisiae (S288c)
PREY

SIL1

SLS1, YOL031C
Nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; required for protein translocation into the endoplasmic reticulum (ER); homolog of Yarrowia lipolytica SLS1; GrpE-like protein
GO Process (1)
GO Function (1)
GO Component (1)

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

Identifying Interaction Partners of Yeast Protein Disulfide Isomerases Using a Small Thiol-Reactive Cross-Linker: Implications for Secretory Pathway Proteostasis.

Freije BJ, Freije WM, Do TU, Adkins GE, Bruch A, Hurtig JE, Morano KA, Schaffrath R, West JD

Protein disulfide isomerases (PDIs) function in forming the correct disulfide bonds in client proteins, thereby aiding the folding of proteins that enter the secretory pathway. Recently, several PDIs have been identified as targets of organic electrophiles, yet the client proteins of specific PDIs remain largely undefined. Here, we report that PDIs expressed in Saccharomyces cerevisiae are targets of divinyl sulfone ... [more]

Chem Res Toxicol Feb. 21, 2022; 35(2);326-336 [Pubmed: 35084835]

Throughput

  • High Throughput

Additional Notes

  • cross-linked

Curated By

  • BioGRID