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http://purl.uniprot.org/citations/8702753http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8702753http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8702753http://www.w3.org/2000/01/rdf-schema#comment"p62 is a novel cellular protein which was initially identified as a phosphotyrosine-independent ligand of the SH2 domain of p56(lck). In the yeast two-hybrid system, p62 specifically interacted with ubiquitin in vivo. Furthermore, p62 bound to ubiquitin-conjugated Sepharose beads in vitro and was efficiently competed by soluble ubiquitin. The interaction was independent of ATP hydrolysis, and its dissociation did not require a reducing agent. Thus, p62 binds to ubiquitin noncovalently. Further analysis showed that the C-terminal 80 amino acids of p62 were indispensable for its interaction with ubiquitin. However, p62 has homology neither with ubiquitin C-terminal hydrolases nor with the S5a subunit of the 26 S proteasome complex, the only proteins known to bind to ubiquitin noncovalently. These results suggest that p62 belongs to a new class of ubiquitin-binding proteins and that p62 affects signal transduction at least partly through ubiquitination-mediated protein degradation."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.34.20235"xsd:string
http://purl.uniprot.org/citations/8702753http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.34.20235"xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Shin J."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Shin J."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Strominger J.L."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Strominger J.L."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Vadlamudi R.K."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Vadlamudi R.K."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Joung I."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/author"Joung I."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/pages"20235-20237"xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/pages"20235-20237"xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/title"p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/title"p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins."xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8702753http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8702753http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8702753
http://purl.uniprot.org/citations/8702753http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8702753