| http://purl.uniprot.org/keywords/491 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Concept |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/1064 |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/391 |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Concept |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/9998 |
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| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#comment | "A heterodimeric membrane protein composed of two non-covalently linked alpha and beta polypeptide chains, both major histocompatibility complex (MHC)-encoded. Each MHC molecule consists of an extracellular peptide-binding cleft followed by an immunoglobulin (Ig)-like domain and transmembrane and cytoplasmic domains. The amino-terminal alpha-1 and beta-1 segments interact to form the peptide-binding cleft. Expressed on professional antigen presenting cells, displays peptides derived from endocytosed proteins for recognition by CD4-positive helper T cells. By scanning MHC II molecules, CD4-positive T cells activate effector mechanisms that eliminate extracellular microbes."xsd:string |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#seeAlso | http://purl.obolibrary.org/obo/GO_0042613 |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2000/01/rdf-schema#seeAlso | http://purl.obolibrary.org/obo/GO_0002504 |
| http://purl.uniprot.org/keywords/491 | http://www.w3.org/2004/02/skos/core#prefLabel | "MHC II"xsd:string |
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