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http://purl.uniprot.org/citations/19608861http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19608861http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19608861http://www.w3.org/2000/01/rdf-schema#comment"Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of lysine acetylation's cellular roles. We used high-resolution mass spectrometry to identify 3600 lysine acetylation sites on 1750 proteins and quantified acetylation changes in response to the deacetylase inhibitors suberoylanilide hydroxamic acid and MS-275. Lysine acetylation preferentially targets large macromolecular complexes involved in diverse cellular processes, such as chromatin remodeling, cell cycle, splicing, nuclear transport, and actin nucleation. Acetylation impaired phosphorylation-dependent interactions of 14-3-3 and regulated the yeast cyclin-dependent kinase Cdc28. Our data demonstrate that the regulatory scope of lysine acetylation is broad and comparable with that of other major posttranslational modifications."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.org/dc/terms/identifier"doi:10.1126/science.1175371"xsd:string
http://purl.uniprot.org/citations/19608861http://purl.org/dc/terms/identifier"doi:10.1126/science.1175371"xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Choudhary C."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Choudhary C."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Gnad F."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Gnad F."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Kumar C."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Kumar C."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Mann M."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Mann M."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Nielsen M.L."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Nielsen M.L."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Olsen J.V."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Olsen J.V."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Rehman M."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Rehman M."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Walther T.C."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/author"Walther T.C."xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/19608861http://purl.uniprot.org/core/name"Science"xsd:string