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http://purl.uniprot.org/citations/21738226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21738226http://www.w3.org/2000/01/rdf-schema#comment"Rad51 is a key enzyme involved in DNA double-strand break repair by homologous recombination. Here, we show that in response to DNA damage, budding yeast Rad51 is phosphorylated on Ser 192 in a manner that is primarily mediated by the DNA-damage-responsive protein kinase Mec1. We show that mutating Rad51 Ser 192 to Ala or Glu confers hypersensitivity to DNA damage and homologous-recombination defects. Furthermore, biochemical analyses indicate that Ser 192 is required for Rad51 adenosine triphosphate hydrolysis and DNA-binding activity in vitro, whereas mutation of Ser 192 does not interfere with Rad51 multimer formation. These data suggest a model in which Mec1-mediated phosphorylation of Rad51 Ser 192 in response to DNA damage controls Rad51 activity and DNA repair by homologous recombination."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.org/dc/terms/identifier"doi:10.1038/embor.2011.127"xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/author"Jackson S.P."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/author"Rice P.A."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/author"Sung P."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/author"Flott S."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/author"Kwon Y."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/author"Pigli Y.Z."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/name"EMBO Rep"xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/pages"833-839"xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/title"Regulation of Rad51 function by phosphorylation."xsd:string
http://purl.uniprot.org/citations/21738226http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/21738226http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21738226
http://purl.uniprot.org/citations/21738226http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21738226
http://purl.uniprot.org/uniprot/P25454#attribution-E11670E0FEA493932C3ABF0CD2574325http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21738226
http://purl.uniprot.org/uniprot/#_A0A8H8ULW3-mappedCitation-21738226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21738226
http://purl.uniprot.org/uniprot/#_P25454-mappedCitation-21738226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21738226
http://purl.uniprot.org/uniprot/A0A8H8ULW3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21738226
http://purl.uniprot.org/uniprot/P25454http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21738226