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http://purl.uniprot.org/citations/17370265http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17370265http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17370265http://www.w3.org/2000/01/rdf-schema#comment"Ubiquitination plays an essential role in maintaining cellular homeostasis by regulating a multitude of essential processes. The ability to identify ubiquitinated proteins by MS currently relies on a strategy in which ubiquitinated peptides are identified by a 114.1 Da diglycine (GG) tag on lysine residues, which is derived from the C-terminus of ubiquitin, following trypsin digestion. In the following study, we report a more comprehensive approach for mapping ubiquitination sites by trypsin digestion and MS/MS analysis. We demonstrate that ubiquitination sites can be identified by signature peptides containing a GG-tag (114.1 Da) and an LRGG-tag (383.2 Da) on internal lysine residues as well as a GG-tag found on the C-terminus of ubiquitinated peptides. Application of this MS-based approach enabled the identification of 96 ubiquitination sites from proteins purified from human MCF-7 breast cancer cells, representing a 2.4-fold increase in the number of ubiquitination sites that could be identified over standard methods. Our improved MS-based strategy will aid future studies which aim to identify and/or characterize ubiquitinated proteins in human cells."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.org/dc/terms/identifier"doi:10.1002/pmic.200600410"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.org/dc/terms/identifier"doi:10.1002/pmic.200600410"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Smith J.C."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Smith J.C."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Figeys D."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Figeys D."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Denis N.J."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Denis N.J."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Lambert J.-P."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Lambert J.-P."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Vasilescu J."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/author"Vasilescu J."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/name"Proteomics"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/name"Proteomics"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/pages"868-874"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/pages"868-874"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/title"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/title"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/17370265http://purl.uniprot.org/core/volume"7"xsd:string