BAIT

RPT3

YNT1, YTA2, proteasome regulatory particle base subunit RPT3, L000002556, L000002537, YDR394W
ATPase of the 19S regulatory particle of the 26S proteasome; one of ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; substrate of N-acetyltransferase B
Saccharomyces cerevisiae (S288c)
PREY

RPN12

NIN1, proteasome regulatory particle lid subunit RPN12, L000001251, YFR052W
Subunit of the 19S regulatory particle of the 26S proteasome lid; synthetically lethal with RPT1, which is an ATPase component of the 19S regulatory particle; physically interacts with Nob1p and Rpn3p; protein abundance increases in response to DNA replication stress
GO Process (1)
GO Function (0)
GO Component (2)
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.

Michaelis AC, Brunner AD, Zwiebel M, Meier F, Strauss MT, Bludau I, Mann M

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

  • 6.0 [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.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPN12 RPT3
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
-
RPN12 RPT3
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
-
RPT3 RPN12
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
-
RPN12 RPT3
Cross-Linking-MS (XL-MS)
Cross-Linking-MS (XL-MS)

An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).

Low-BioGRID
3730311
RPT3 RPN12
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-0.3907BioGRID
1927708
RPN12 RPT3
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-0.4044BioGRID
1932117

Curated By

  • BioGRID