Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Publication

A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14.

Borodovsky A, Kessler BM, Casagrande R, Overkleeft HS, Wilkinson KD, Ploegh HL

A C-terminally modified ubiquitin (Ub) derivative, ubiquitin vinyl sulfone (UbVS), was synthesized as an active site-directed probe that irreversibly modifies a subset of Ub C-terminal hydrolases (UCHs) and Ub-specific processing proteases (UBPs). Specificity of UbVS for deubiquitylating enzymes (DUBs) is demonstrated not only by inhibition of [(125)I]UbVS labeling with N-ethylmaleimide and Ub aldehyde, but also by genetic analysis. [(125)I]UbVS modifies ... [more]

EMBO J. Sep. 17, 2001; 20(18);5187-96 [Pubmed: 11566882]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
USP14 PSMA4	Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.	Pourhaghighi R (2020)	High	0.7695	BioGRID	2672755

Curated By

BioGRID

Interaction Summary

USP14

Gene Ontology Biological Process

Gene Ontology Molecular Function

cysteine-type endopeptidase activity [IBA]endopeptidase inhibitor activity [ISO]proteasome binding [ISO]ubiquitin thiolesterase activity [IBA, ISO]ubiquitin-specific protease activity [IBA, ISO]

Gene Ontology Cellular Component

PSMA4