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http://purl.uniprot.org/citations/18707152http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18707152http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18707152http://www.w3.org/2000/01/rdf-schema#comment"Protein dynamics is regulated by an elaborate interplay between different post-translational modifications. Ubiquitin and ubiquitin-like proteins (Ubls) are small proteins that are covalently conjugated to target proteins with important functional consequences. One such modifier is SUMO, which mainly modifies nuclear proteins. SUMO contains a unique N-terminal arm not present in ubiquitin and other Ubls, which functions in the formation of SUMO polymers. Here, we unambiguously show that serine 2 of the endogenous SUMO-1 N-terminal protrusion is phosphorylated in vivo using very high mass accuracy mass spectrometry at both the MS and the MS/MS level and complementary fragmentation techniques. Strikingly, we detected the same phosphorylation in yeast, Drosophila and human cells, suggesting an evolutionary conserved function for this modification. The nearly identical human SUMO-2 and SUMO-3 isoforms differ in serine 2; thus, only SUMO-3 could be phosphorylated at this position. Our finding that SUMO can be modified may point to an additional level of complexity through modifying a protein-modifier."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.org/dc/terms/identifier"doi:10.1021/pr800368m"xsd:string
http://purl.uniprot.org/citations/18707152http://purl.org/dc/terms/identifier"doi:10.1021/pr800368m"xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Matic I."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Matic I."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Mann M."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Mann M."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Macek B."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Macek B."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Walther T.C."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Walther T.C."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Hilger M."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/author"Hilger M."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/name"J. Proteome Res."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/name"J. Proteome Res."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/pages"4050-4057"xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/pages"4050-4057"xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/title"Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/title"Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution."xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/18707152http://purl.uniprot.org/core/volume"7"xsd:string