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http://purl.uniprot.org/citations/21120624http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21120624http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21120624http://www.w3.org/2000/01/rdf-schema#comment"Covalent modifications of the Pellino-1 protein are essential for transmitting innate immune response signals downstream, as the phosphorylation and polyubiquitination of Pellino-1 mediated by the IRAK proteins appear to have roles in regulating Pellino-1 function. In this study, we demonstrate that the Pellino-1 protein is post-translationally modified by small-ubiquitin-related modifier-1 (SUMO-1). Sumoylation assays with Pellino-1 and SUMO-1 expression plasmids reveal that the Pellino-1 protein is sumoylated in vitro and in vivo. Treatment of SUMO-1 specific protease 1 (SENP1) inhibited the sumoylation of the Pellino-1 protein and a GST pull-down assay as well as a yeast two hybrid assay showed that Pellino-1 binds to the SUMO-conjugating enzyme, Ubc9. Furthermore, we identified the five lysine residues of the Pellino-1 protein where SUMO-1 covalently attaches. Some of the sumoylated sites overlap with previously identified ubiquitination sites, suggesting competition between sumoylation and ubiquitination, as well as suggesting that the sumoylated Pellino-1 protein may have a cellular function distinct from previously identified functions."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.org/dc/terms/identifier"doi:10.1007/s10059-011-0006-x"xsd:string
http://purl.uniprot.org/citations/21120624http://purl.org/dc/terms/identifier"doi:10.1007/s10059-011-0006-x"xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Kim J.H."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Kim J.H."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Jung S.M."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Jung S.M."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Lee Y.S."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Lee Y.S."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Park S.H."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Park S.H."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Choi C.Y."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Choi C.Y."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Kwon J.Y."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Kwon J.Y."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Sung K.S."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/author"Sung K.S."xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/name"Mol. Cells"xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/name"Mol. Cells"xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/pages"85-89"xsd:string
http://purl.uniprot.org/citations/21120624http://purl.uniprot.org/core/pages"85-89"xsd:string