BAIT

RPN11

MPR1, proteasome regulatory particle lid subunit RPN11, L000002976, L000002965, YFR004W
Metalloprotease subunit of 19S regulatory particle; part of 26S proteasome lid; couples the deubiquitination and degradation of proteasome substrates; involved, independent of catalytic activity, in fission of mitochondria and peroxisomes; protein abundance increases in response to DNA replication stress
Saccharomyces cerevisiae (S288c)
PREY

RNR4

CRT3, PSO3, ribonucleotide-diphosphate reductase subunit RNR4, L000002819, S000029396, L000004184, YGR180C
Ribonucleotide-diphosphate reductase (RNR) small subunit; the RNR complex catalyzes the rate-limiting step in dNTP synthesis and is regulated by DNA replication and DNA damage checkpoint pathways via localization of the small subunits; relocalizes from nucleus to cytoplasm upon DNA replication stress; RNR4 has a paralog, RNR2, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (3)
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

Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy.

Kaake RM, Milenkovic T, Przulj N, Kaiser P, Huang L

Ubiquitin-proteasome dependent protein degradation plays a fundamental role in the regulation of the eukaryotic cell cycle. Cell cycle transitions between different phases are tightly regulated to prevent uncontrolled cell proliferation, which is characteristic of cancer cells. To understand cell cycle phase specific regulation of the 26S proteasome and reveal the molecular mechanisms underlying the ubiquitin-proteasome degradation pathway during cell cycle ... [more]

J. Proteome Res. Apr. 05, 2010; 9(4);2016-29 [Pubmed: 20170199]

Throughput

  • High Throughput

Additional Notes

  • Proteasome interacting proteins (PIPs) were identified using QTAX (quantitative analysis of tandem affinity purified in vivo cross-linked (X) protein complexes). TAP-tagged Rpn11 and in vivo formaldehyde cross-linking were used in the experiment.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPN11 RNR4
Affinity Capture-MS
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.

High-BioGRID
-
RNR4 RPN11
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2006BioGRID
2045659

Curated By

  • BioGRID