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http://purl.uniprot.org/citations/8576256http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8576256http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8576256http://www.w3.org/2000/01/rdf-schema#comment"The ubiquitin/proteasome system is the main eukaryotic nonlysosomal protein degradation system. Substrate selectivity of this pathway is thought to be mediated in part by members of a large family of ubiquitin-conjugating (E2) enzymes, which catalyze the covalent attachment of ubiquitin to proteolytic substrates. E2 enzymes have a conserved approximately 150-residue so-called UBC domain, which harbors the cysteine residue required for enzyme-ubiquitin thioester formation. Some E2 enzymes possess additional carboxyl-terminal extensions that are involved in substrate specificity and intracellular localization of the enzyme. Here we describe a novel family of E2 enzymes from higher eukaryotes (Drosophila, mouse, and man) that have amino-terminal extensions but lack carboxyl-terminal extensions. We have identified four different variants of these enzymes that have virtually identical UBC domains (94% identity) but differ in their amino-terminal extensions. In yeast, these enzymes can partially complement mutants deficient in the UBC4 E2 enzyme. This indicates that members of this novel E2 family may operate in UBC4-related proteolytic pathways."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.5.2789"xsd:string
http://purl.uniprot.org/citations/8576256http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.5.2789"xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Matuschewski K."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Matuschewski K."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Jentsch S."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Jentsch S."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Hauser H.P."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Hauser H.P."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Treier M."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/author"Treier M."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/pages"2789-2794"xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/pages"2789-2794"xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/title"Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/title"Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions."xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8576256http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8576256http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8576256
http://purl.uniprot.org/citations/8576256http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8576256