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http://purl.uniprot.org/unirules/MF_04048#construct-template-139http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_04048#construct-var-17
http://purl.uniprot.org/unirules/MF_04048#construct-template-139http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_04048#construct-template-139http://spinrdf.org/sp#object"Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Minor capsid protein 6 contains one L domain: a PPXY motif which binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4. In adenoviruses, this motif seems to play a role in microtubule-dependent intracellular trafficking toward the nucleus during virus entry into host cell and in suppression of DAXX-mediated repression of the immediate early E1A promoter."xsd:string
http://purl.uniprot.org/unirules/MF_04048#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_04048#construct-template-139
http://purl.uniprot.org/unirules/MF_04048#construct-template-list-139http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_04048#construct-template-139