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http://purl.uniprot.org/citations/12150977http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12150977http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12150977http://www.w3.org/2000/01/rdf-schema#comment"Small ubiquitin-related modifier-1 (SUMO-1) is a protein that is covalently modified to various cellular proteins and protects cells against both anti-Fas and TNF-induced cell death. Previously, we reported that the C-terminus of Daxx interacted with Ubc9, an E2 type SUMO-1 conjugating enzyme, as well as with SUMO-1. In BOSC23 cells expressing FLAG-Daxx together with HA-SUMO-1, 110 and 130kDa Daxx appeared and the 130kDa band bound to both anti-HA and anti-FLAG antibodies. This means that Daxx can be covalently modified by SUMO-1. Substitution of K630 and K631 abrogated the modification of Daxx by SUMO-1, implying that K630 and K631 were essential for sumoylation. Daxx (K630, 631A) and Daxx (K634, 636, 637A) in which the putative C-terminal nuclear localization signals (NLSs) were disrupted appeared in the nucleus, suggesting that the C-terminal NLS was not functional. Daxx (K630, 631A), the sumoylation defective mutant, was able to interact with PML and co-localized with PML in the PML oncogenic domains (PODs). Thus, our data show that sumoylation status of Daxx does not affect its presence in PODs."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(02)00699-x"xsd:string
http://purl.uniprot.org/citations/12150977http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(02)00699-x"xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/author"Jang M.-S."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/author"Jang M.-S."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/author"Ryu S.-W."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/author"Ryu S.-W."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/pages"495-500"xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/pages"495-500"xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/title"Modification of Daxx by small ubiquitin-related modifier-1."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/title"Modification of Daxx by small ubiquitin-related modifier-1."xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/volume"295"xsd:string
http://purl.uniprot.org/citations/12150977http://purl.uniprot.org/core/volume"295"xsd:string
http://purl.uniprot.org/citations/12150977http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12150977
http://purl.uniprot.org/citations/12150977http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12150977
http://purl.uniprot.org/citations/12150977http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12150977
http://purl.uniprot.org/citations/12150977http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12150977