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http://purl.uniprot.org/unirules/MF_04051#construct-template-64http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_04051#construct-var-3
http://purl.uniprot.org/unirules/MF_04051#construct-template-64http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_04051#construct-template-64http://spinrdf.org/sp#object"Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus."xsd:string
http://purl.uniprot.org/unirules/MF_04051#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_04051#construct-template-64
http://purl.uniprot.org/unirules/MF_04051#construct-template-list-64http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_04051#construct-template-64