BAIT

MCM7

CDC47, MCM DNA helicase complex subunit MCM7, L000002760, YBR202W
Component of the Mcm2-7 hexameric helicase complex; MCM2-7 primes origins of DNA replication in G1 and becomes an active ATP-dependent helicase that promotes DNA melting and elongation in S-phase; forms an Mcm4p-6p-7p subcomplex
Saccharomyces cerevisiae (S288c)
PREY

TPI1

triose-phosphate isomerase TPI1, L000002326, YDR050C
Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human TPI causes a rare autosomal disease
GO Process (1)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

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

A pipeline for determining protein-protein interactions and proximities in the cellular milieu.

Subbotin RI, Chait BT

It remains extraordinarily challenging to elucidate endogenous protein-protein interactions and proximities within the cellular milieu. The dynamic nature and the large range of affinities of these interactions augment the difficulty of this undertaking. Among the most useful tools for extracting such information are those based on affinity capture of target bait proteins in combination with mass spectrometric readout of the ... [more]

Mol. Cell Proteomics Nov. 01, 2014; 13(11);2824-35 [Pubmed: 25172955]

Throughput

  • High Throughput

Curated By

  • BioGRID