<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rossio V</submitter><funding>NIGMS NIH HHS</funding><pagination>108737</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9679738</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>45</volume><pubmed_abstract>The Ubiquitin-Proteasome System (UPS) regulates many cellular processes in eukaryotic cells. Ubiquitylation by the UPS mainly directs proteins to proteasomal degradation, but it can also have non-degradative functions, such as regulating protein activity or localization. The small protein ubiquitin is conjugated to its substrates via a cascade of E1-E2-E3 enzymes. Dysregulation of the UPS has been implicated in the genesis and progression of many diseases, such as neurodegenerative diseases and cancer; thus, the UPS components are attractive targets for developing pharmaceutical drugs. E2s, or ubiquitin conjugating enzymes, are central players of the UPS. E2s function in tandem with specific ubiquitin ligases (E3s) to transfer ubiquitin to substrates. Here, we present the first proteome st</pubmed_abstract><journal>Data in brief</journal><pubmed_title>Quantitative proteome dataset profiling of &lt;i>UBC4&lt;/i> and &lt;i>UBC5&lt;/i> deletion strains in &lt;i>Saccharomyces cerevisiae&lt;/i>.</pubmed_title><pmcid>PMC9679738</pmcid><funding_grant_id>R01 GM132129</funding_grant_id><pubmed_authors>Paulo JA</pubmed_authors><pubmed_authors>Rossio V</pubmed_authors></additional><is_claimable>false</is_claimable><name>Quantitative proteome dataset profiling of &lt;i>UBC4&lt;/i> and &lt;i>UBC5&lt;/i> deletion strains in &lt;i>Saccharomyces cerevisiae&lt;/i>.</name><description>The Ubiquitin-Proteasome System (UPS) regulates many cellular processes in eukaryotic cells. Ubiquitylation by the UPS mainly directs proteins to proteasomal degradation, but it can also have non-degradative functions, such as regulating protein activity or localization. The small protein ubiquitin is conjugated to its substrates via a cascade of E1-E2-E3 enzymes. Dysregulation of the UPS has been implicated in the genesis and progression of many diseases, such as neurodegenerative diseases and cancer; thus, the UPS components are attractive targets for developing pharmaceutical drugs. E2s, or ubiquitin conjugating enzymes, are central players of the UPS. E2s function in tandem with specific ubiquitin ligases (E3s) to transfer ubiquitin to substrates. Here, we present the first proteome st</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2026-04-08T11:57:44.969Z</modification><creation>2025-04-07T06:20:27.343Z</creation></dates><accession>S-EPMC9679738</accession><cross_references><pubmed>36426069</pubmed><doi>10.1016/j.dib.2022.108737</doi></cross_references></HashMap>