| http://purl.uniprot.org/citations/33856219 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33856219 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33856219 | http://www.w3.org/2000/01/rdf-schema#comment | "The formation of condensates in membraneless organelles is thought to be driven by protein phase separation. Arginine methylation and serine/threonine phosphorylation are important in the phase separation process; however, these post-translational modifications are often present in intrinsically disordered regions that are difficult to analyze with standard proteomic techniques. To understand their presence and co-occurrence in condensate-associated proteins, here, we use a multiprotease and multi-tandem mass spectrometry (MS/MS) fragmentation approach, coupled with heavy methyl stable isotope labeling of amino acids in cell culture (SILAC) and phospho- or methyl-peptide enrichment. For Saccharomyces cerevisiae, we report a 50% increase in the known arginine methylproteome, involving 15 proteins that are all condensate-associated. Importantly, some of these proteins have arginine methylation on all predicted sites-providing evidence that this modification can be pervasive. We explored whether arginine-methylated, condensate-associated proteins are also phosphorylated and found 12 such proteins to carry phosphorylated serine or threonine. In Npl3, Ded1, and Sbp1, single peptides were found to carry both modifications, indicating a co-occurrence in close proximity and on the same protein molecule. These co-modifications occur in regions of disorder, whereas arginine methylation is typically on regions of disorder that are also basic. For phosphorylation, its association with charged regions of condensate-associated proteins was less consistent, although some regions with multisite phosphorylation sites were strongly acidic. We conclude that arginine-methylated proteins associated with condensates are typically also modified with protein phosphorylation."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.jproteome.0c00927"xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.jproteome.0c00927"xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/author | "Nguyen A."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/author | "Nguyen A."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/author | "Wilkins M.R."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/author | "Wilkins M.R."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/author | "Hamey J.J."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/author | "Hamey J.J."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/name | "J. Proteome Res."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/name | "J. Proteome Res."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/pages | "2420-2434"xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/pages | "2420-2434"xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/title | "Discovery of arginine methylation, phosphorylation, and their co-occurrence in condensate-associated proteins in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/title | "Discovery of arginine methylation, phosphorylation, and their co-occurrence in condensate-associated proteins in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/volume | "20"xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://purl.uniprot.org/core/volume | "20"xsd:string |
| http://purl.uniprot.org/citations/33856219 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33856219 |
| http://purl.uniprot.org/citations/33856219 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33856219 |
| http://purl.uniprot.org/citations/33856219 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33856219 |
| http://purl.uniprot.org/citations/33856219 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33856219 |