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(2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified IPMK","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"8a6ba6fb-77f9-5fa8-bf9d-b270c15e7e08","evidence_kind":"source_excerpt","locator":"Lines 691-702","start_line":691,"end_line":702,"excerpt":"### ino-ipmk-pip3\nHuman IPMK also has PI(4,5)P2 3-kinase activity, producing PI(3,4,5)P3.\nCondition category: normal\nnutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: One enzyme acts on both soluble inositol phosphates and a membrane lipid.\norganism: Human protein\ntissue_or_cell_type: Purified IPMK\nexperimental_model: Crystal structures and targeted human IPMK mutants\nlimitations: Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity.\nexposure: IP3 and PI(4,5)P2 substrate binding and phosphorylation\nevidence_span: {\"source_cache\": \"artifacts/inositol-research/28882892.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db\", \"start_char\": 0, \"end_char\": 1781, \"text_sha256\": \"39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db\"}\n[ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. 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