PubMed:10207176 / 84-385 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T2","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":103,"end":301},"obj":"Sentence"},{"id":"T2","span":{"begin":0,"end":301},"obj":"Sentence"},{"id":"T2","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"T3","span":{"begin":103,"end":301},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

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{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":112,"end":119},"obj":"http://www.uniprot.org/uniprot/P10153"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":90,"end":93},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T2","span":{"begin":98,"end":101},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T4","span":{"begin":112,"end":119},"obj":"http://www.uniprot.org/uniprot/O35291"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":4,"end":8},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":4,"end":8},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"GO-BP","denotations":[{"id":"T5","span":{"begin":252,"end":260},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T11","span":{"begin":181,"end":211},"obj":"http://purl.obolibrary.org/obo/GO_0043687"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":40,"end":45},"obj":"http://purl.obolibrary.org/obo/GO_0005143"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"EDAM-topics","denotations":[{"id":"T3","span":{"begin":18,"end":23},"obj":"http://edamontology.org/topic_2815"},{"id":"T4","span":{"begin":81,"end":89},"obj":"http://edamontology.org/topic_3168"},{"id":"T5","span":{"begin":81,"end":89},"obj":"http://edamontology.org/topic_0080"},{"id":"T6","span":{"begin":106,"end":111},"obj":"http://edamontology.org/topic_2815"},{"id":"T7","span":{"begin":144,"end":149},"obj":"http://edamontology.org/topic_0158"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"EDAM-DFO","denotations":[{"id":"T3","span":{"begin":81,"end":89},"obj":"http://edamontology.org/data_2044"},{"id":"T4","span":{"begin":81,"end":89},"obj":"http://edamontology.org/operation_3218"},{"id":"T5","span":{"begin":132,"end":143},"obj":"http://edamontology.org/operation_2423"},{"id":"T6","span":{"begin":261,"end":268},"obj":"http://edamontology.org/data_1756"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}

{"project":"NCBITAXON","denotations":[{"id":"T2","span":{"begin":18,"end":23},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":106,"end":111},"obj":"OrganismTaxon"}],"attributes":[{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan."}