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http://purl.uniprot.org/keywords/1165http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Concept
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/keywords/1164
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/keywords/1162
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/keywords/1160
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Concept
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/keywords/9999
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#comment"Viral protein involved in virus internalization by the host cell via clathrin-mediated endocytosis. In response to an internalization signal, clathrin is assembled on the inside face of the cell membrane to form characteristic invaginations or clathrin coated pits that pinch off through the action of DNM1/Dynamin-1 or DNM2/Dynamin-2. The virus bound to its host cell receptor is internalized into clathrin-coated vesicles (CCV). Endocytic CCV deliver their viral content to early endosomes. The endosomal acidic pH and/or receptor binding usually induces structural modifications of the virus surface proteins that lead to penetration of the endosomal membrane via fusion or permeabilization mechanisms."xsd:string
http://purl.uniprot.org/keywords/1165http://www.w3.org/2000/01/rdf-schema#seeAlsohttp://purl.obolibrary.org/obo/GO_0075512
http://purl.uniprot.org/keywords/1165http://www.w3.org/2004/02/skos/core#prefLabel"Clathrin-mediated endocytosis of virus by host"xsd:string
http://purl.uniprot.org/keywords/1165http://www.w3.org/2004/02/skos/core#altLabel"Virion endocytosis by clathrin-coated vesicle"xsd:string
http://purl.uniprot.org/keywords/1165http://purl.uniprot.org/core/categoryhttp://purl.uniprot.org/keywords/9999
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http://purl.uniprot.org/uniprot/A0A7S5UAV8http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A887EZ35http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A897TC49http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A7S5LHD6http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A893BCH8http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
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http://purl.uniprot.org/uniprot/A0A0D5BI02http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A887F1C3http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A891EZW1http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/A0A7S5HB32http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165
http://purl.uniprot.org/uniprot/Q80KE2http://purl.uniprot.org/core/classifiedWithhttp://purl.uniprot.org/keywords/1165