Reference: Apodaca J, et al. (2005) Analysis of ubiquitin chain-binding proteins by two-hybrid methods. Methods Enzymol 399:157-64

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Abstract


Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Apodaca J, Ahn J, Kim I, Rao H
Additional Lit For
RAD23 | DSK2 | UBI4

Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 2 entries for 4 genes

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InteractorInteractorAssayAnnotationActionModification

#LPPI|Likely protein-protein interaction

RAD23UBI4Two-hybridmanually curatedBait-HitNo Modification
UFD2DSK2Two-hybridmanually curatedHit-BaitNo Modification
Showing 1 to 2 of 2 entries