RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11583632http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11583632http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11583632http://www.w3.org/2000/01/rdf-schema#comment"Sumoylation of p53 by the ubiquitin-like protein, SUMO-1/sentrin/PIC1, has been shown to stimulate its transcriptional activation activity. The SUMO E3 ligase, a key enzyme in the recognition of substrates to be sumoylated, has not yet been identified. We isolated PIAS1 (protein inhibitor of activated STAT1) as a SUMO-1 binding protein by yeast two-hybrid screening. In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO. PIAS1 that was mutated in the RING finger-like domain bound p53 and SUMO-1, but not Ubc9. PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner. These data suggest that PIAS1 functions as a SUMO ligase, or possibly as a tightly bound regulator of it, toward p53."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(01)00349-5"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(01)00349-5"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/author"Yasuda H."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/author"Yasuda H."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/author"Nishida T."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/author"Nishida T."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/author"Kahyo T."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/author"Kahyo T."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/pages"713-718"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/pages"713-718"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/title"Involvement of PIAS1 in the sumoylation of tumor suppressor p53."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/title"Involvement of PIAS1 in the sumoylation of tumor suppressor p53."xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11583632http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11583632http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11583632
http://purl.uniprot.org/citations/11583632http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11583632
http://purl.uniprot.org/citations/11583632http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11583632
http://purl.uniprot.org/citations/11583632http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11583632