BAIT

RPN5

NAS5, proteasome regulatory particle lid subunit RPN5, L000004451, L000004305, YDL147W
Subunit of the CSN and 26S proteasome lid complexes; similar to mammalian p55 subunit and to another S. cerevisiae regulatory subunit, Rpn7p; Rpn5p is an essential protein; the COP9 signalosome is also known as the CSN
GO Process (2)
GO Function (0)
GO Component (4)
Saccharomyces cerevisiae (S288c)
PREY

PRE10

proteasome core particle subunit alpha 7, L000003146, YOR362C
Alpha 7 subunit of the 20S proteasome; protein abundance increases in response to DNA replication stress
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

Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome.

Yu Z, Kleifeld O, Lande-Atir A, Bsoul M, Kleiman M, Krutauz D, Book A, Vierstra RD, Hofmann K, Reis N, Glickman MH, Pick E

Subunit composition and architectural structure of the 26S proteasome lid is strictly conserved between all eukaryotes. This eight-subunit complex bears high similarity to the eukaryotic translation initiation factor 3 (eIF3) and to the COP9 signalosome (CSN) which together define the PCI troika. In some unicellular eukaryotes, the latter two complexes lack key subunits, questioning the conservation of their structural design. ... [more]

Unknown Feb. 02, 2011; 0(0); [Pubmed: 21289098]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPN5 PRE10
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.

High7BioGRID
3612874
PRE10 RPN5
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
3730155
PRE10 RPN5
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-0.089BioGRID
442857
RPN5 PRE10
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-0.089BioGRID
442858
PRE10 RPN5
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-0.3114BioGRID
1954393
RPN5 PRE10
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-0.2874BioGRID
1924229

Curated By

  • BioGRID