{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Leznicki P"],"funding":["European Molecular Biology Organization","Fundação para a Ciência e a Tecnologia","European Research Council","University of Manchester","Tenovus","Medical Research Council"],"pagination":["jcs212753"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6031330"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["131(10)"],"pubmed_abstract":["Protein ubiquitylation is a dynamic post-translational modification that can be reversed by deubiquitylating enzymes (DUBs). It is unclear how the small number (∼100) of DUBs present in mammalian cells regulate the thousands of different ubiquitylation events. Here, we analysed annotated transcripts of human DUBs and found ∼300 ribosome-associated transcripts annotated as protein coding, which thus increases the total number of DUBs. By using USP35, a poorly studied DUB, as a case study, we provide evidence that alternative isoforms contribute to the functional expansion of DUBs. We show that there are two different USP35 isoforms that localise to different intracellular compartments and have distinct functions. Our results reveal that isoform 1 is an anti-apoptotic factor that inhibits st"],"journal":["Journal of cell science"],"pubmed_title":["Expansion of DUB functionality generated by alternative isoforms - USP35, a case study."],"pmcid":["PMC6031330"],"funding_grant_id":["IF/00595/2014","677623","3057","MC_UU_12016/6"],"pubmed_authors":["Schlattl A","Pathak D","Leznicki P","Bader G","Boehmelt G","Kulathu Y","Spevak W","Natarajan J","Bordone MC","Abdul Rehman SA","Zoephel A","Weidlich S","Barbosa-Morais NL"],"additional_accession":[]},"is_claimable":false,"name":"Expansion of DUB functionality generated by alternative isoforms - USP35, a case study.","description":"Protein ubiquitylation is a dynamic post-translational modification that can be reversed by deubiquitylating enzymes (DUBs). It is unclear how the small number (∼100) of DUBs present in mammalian cells regulate the thousands of different ubiquitylation events. Here, we analysed annotated transcripts of human DUBs and found ∼300 ribosome-associated transcripts annotated as protein coding, which thus increases the total number of DUBs. By using USP35, a poorly studied DUB, as a case study, we provide evidence that alternative isoforms contribute to the functional expansion of DUBs. We show that there are two different USP35 isoforms that localise to different intracellular compartments and have distinct functions. Our results reveal that isoform 1 is an anti-apoptotic factor that inhibits st","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 May","modification":"2026-04-29T18:09:36.481Z","creation":"2019-03-27T00:07:21Z"},"accession":"S-EPMC6031330","cross_references":{"pubmed":["29685892"],"doi":["10.1242/jcs.212753"]}}