Unknown

Dataset Information

0

Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress.


ABSTRACT: The data described here provide the first large-scale analysis of lysine 63 (K63)-linked polyubiquitin targets. Protein ubiquitination is a prominent post-translational modification, and a variety of ubiquitin chains exists, serving a multitude of functions [1]. The chains differ by the lysine residue by which the ubiquitin monomers are linked. We used yeast Saccharomyces cerevisiae subjected to oxidative stress as a model to study K63 ubiquitination. K63 ubiquitinated targets were pulled-down by the K63-TUBE system (Tandem Ubiquitin Binding Entities) and analyzed by SILAC-based mass spectrometry [2]. The data are associated to the research article 'K63 polyubiquitination is a new modulator of the oxidative stress response' [3]. The mass spectrometry and the analysis dataset have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000960.

SUBMITTER: Silva GM 

PROVIDER: S-EPMC4510443 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress.

Silva Gustavo Monteiro GM   Vogel Christine C  

Data in brief 20150521


The data described here provide the first large-scale analysis of lysine 63 (K63)-linked polyubiquitin targets. Protein ubiquitination is a prominent post-translational modification, and a variety of ubiquitin chains exists, serving a multitude of functions [1]. The chains differ by the lysine residue by which the ubiquitin monomers are linked. We used yeast Saccharomyces cerevisiae subjected to oxidative stress as a model to study K63 ubiquitination. K63 ubiquitinated targets were pulled-down b  ...[more]

Similar Datasets

| S-EPMC4318705 | biostudies-literature
| S-EPMC7823279 | biostudies-literature
| S-EPMC7486741 | biostudies-literature
2005-09-20 | GSE2744 | GEO
| S-EPMC3547818 | biostudies-literature
| S-EPMC6423473 | biostudies-literature
| S-EPMC8284302 | biostudies-literature
| S-EPMC4471591 | biostudies-literature
| S-EPMC6837444 | biostudies-literature
2015-01-26 | PXD000979 | Pride