BAIT

PSMD11

Rpn6, S9, p44.5
proteasome (prosome, macropain) 26S subunit, non-ATPase, 11
GO Process (24)
GO Function (1)
GO Component (7)

Gene Ontology Molecular Function

Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

The ubiquitin specific protease-4 (USP4) interacts with the S9/Rpn6 subunit of the proteasome.

Zhao B, Velasco K, Sompallae R, Pfirrmann T, Masucci MG, Lindsten K

The proteasome is the major non-lysosomal proteolytic machine in cells that, through degradation of ubiquitylated substrates, regulates virtually all cellular functions. Numerous accessory proteins influence the activity of the proteasome by recruiting or deubiquitylating proteasomal substrates, or by maintaining the integrity of the complex. Here we show that the ubiquitin specific protease (USP)-4, a deubiquitylating enzyme with specificity for both ... [more]

Biochem. Biophys. Res. Commun. Oct. 26, 2012; 427(3);490-6 [Pubmed: 23022198]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PSMD11 USP4
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
USP4 PSMD11
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Low-BioGRID
-

Curated By

  • BioGRID