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http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.-.-
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.2.-
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#comment"In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). cf. EC 2.3.2.31."xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#comment"Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin."xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#comment"RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein."xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2000/01/rdf-schema#comment"Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase)."xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2004/02/skos/core#prefLabel"RING-type E3 ubiquitin transferase"xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19041308
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22389392
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22842904
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22885007
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23747565
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2004/02/skos/core#altLabel"RING E3 ligase"xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2004/02/skos/core#altLabel"ubiquitin transferase RING E3"xsd:string
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/6.3.2.19
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/6.3.2.21
http://purl.uniprot.org/enzyme/2.3.2.27http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.2.27#SIP0DF5D6CC8B347E0A
http://purl.uniprot.org/enzyme/2.3.2.27http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.3.2.-
http://purl.uniprot.org/uniprot/A0A811SEH8http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.2.27
http://purl.uniprot.org/uniprot/A0A8S0PJQ2http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.2.27
http://purl.uniprot.org/uniprot/A0A8B6CBI8http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.2.27
http://purl.uniprot.org/uniprot/A0A9W9Z212http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.2.27