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

SEM1

DSS1, HOD1, proteasome regulatory particle lid subunit SEM1, L000003539, L000004647, YDR363W-A
Component of lid subcomplex of 26S proteasome regulatory subunit; involved in mRNA export mediated by TREX-2 complex (Sac3p-Thp1p); assumes different conformations in different contexts, functions as molecular glue stabilizing the Rpn3p/Rpn7p regulatory heterodimer, and tethers it to lid helical bundle; ortholog of human DSS1; protein abundance increases in response to DNA replication stress
Saccharomyces cerevisiae (S288c)

Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Publication

A Single α Helix Drives Extensive Remodeling of the Proteasome Lid and Completion of Regulatory Particle Assembly.

Tomko RJ, Taylor DW, Chen ZA, Wang HW, Rappsilber J, Hochstrasser M

Most short-lived eukaryotic proteins are degraded by the proteasome. A proteolytic core particle (CP) capped by regulatory particles (RPs) constitutes the 26S proteasome complex. RP biogenesis culminates with the joining of two large subcomplexes, the lid and base. In yeast and mammals, the lid appears to assemble completely before attaching to the base, but how this hierarchical assembly is enforced ... [more]

Cell Oct. 08, 2015; 163(2);432-44 [Pubmed: 26451487]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPN5 SEM1
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.

Low-BioGRID
-
SEM1 RPN5
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.

Low-BioGRID
-
RPN5 SEM1
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
-
RPN5 SEM1
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.

High10BioGRID
3612910
SEM1 RPN5
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.

Low-BioGRID
-
RPN5 SEM1
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.

Low-BioGRID
-
SEM1 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-0.5282BioGRID
2036558
RPN5 SEM1
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-0.1839BioGRID
1966175

Curated By

  • BioGRID