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http://purl.uniprot.org/citations/25772364http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25772364http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25772364http://www.w3.org/2000/01/rdf-schema#comment"Small ubiquitin-like modifiers play critical roles in the DNA damage response (DDR). To increase our understanding of SUMOylation in the mammalian DDR, we employed a quantitative proteomics approach in order to identify dynamically regulated SUMO-2 conjugates and modification sites upon treatment with the DNA damaging agent methyl methanesulfonate (MMS). We have uncovered a dynamic set of 20 upregulated and 33 downregulated SUMO-2 conjugates, and 755 SUMO-2 sites, of which 362 were dynamic in response to MMS. In contrast to yeast, where a response is centered on homologous recombination, we identified dynamically SUMOylated interaction networks of chromatin modifiers, transcription factors, DNA repair factors, and nuclear body components. SUMOylated chromatin modifiers include JARID1B/KDM5B, JARID1C/KDM5C, p300, CBP, PARP1, SetDB1, and MBD1. Whereas SUMOylated JARID1B was ubiquitylated by the SUMO-targeted ubiquitin ligase RNF4 and degraded by the proteasome in response to DNA damage, JARID1C was SUMOylated and recruited to the chromatin to demethylate histone H3K4."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2015.02.033"xsd:string
http://purl.uniprot.org/citations/25772364http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2015.02.033"xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Hendriks I.A."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Hendriks I.A."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Olsen J.V."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Olsen J.V."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Vertegaal A.C."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Vertegaal A.C."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Treffers L.W."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Treffers L.W."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Verlaan-de Vries M."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/author"Verlaan-de Vries M."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/pages"1778-1791"xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/pages"1778-1791"xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/title"SUMO-2 orchestrates chromatin modifiers in response to DNA damage."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/title"SUMO-2 orchestrates chromatin modifiers in response to DNA damage."xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/25772364http://purl.uniprot.org/core/volume"10"xsd:string