{"id":"198d2989-09d4-5218-8e2a-1bfc85b72620","stable_key":"e69ef6a0-0e23-5eac-aca1-cf333781b962:ino-pten-pip3","predicate":"dephosphorylates","statement":"Human PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c0a60368-2f53-5a7d-a002-c630dca98f37","mechanism_event_label":"A phosphatase reverses a signaling-lipid phosphorylation step.","subject":{"id":"206cddf4-abc9-556d-9bad-e0004dde122b","slug":"pten","display_name":"PTEN (human phosphatase and tensin homolog)","entity_type_key":"protein"},"object":{"id":"cd6dd4cf-a6ba-5d9b-ac42-dd15fd901757","slug":"phosphatidylinositol-345-trisphosphate","display_name":"Phosphatidylinositol 3,4,5-trisphosphate (PIP3)","entity_type_key":"lipid"},"evidence_count":1,"mechanism_event":{"id":"c0a60368-2f53-5a7d-a002-c630dca98f37","stable_key":"e69ef6a0-0e23-5eac-aca1-cf333781b962:ino-pten-pip3-event","event_type":"biochemical_relationship","label":"A phosphatase reverses a signaling-lipid phosphorylation step.","description":"Human PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"af38e50f-cdfb-5d4b-a6fb-f742d1b23d41","slug":"phosphatidylinositol-4-5-bisphosphate","display_name":"Phosphatidylinositol 4,5-bisphosphate","entity_type_key":"lipid"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"206cddf4-abc9-556d-9bad-e0004dde122b","slug":"pten","display_name":"PTEN (human phosphatase and tensin homolog)","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"cd6dd4cf-a6ba-5d9b-ac42-dd15fd901757","slug":"phosphatidylinositol-345-trisphosphate","display_name":"Phosphatidylinositol 3,4,5-trisphosphate (PIP3)","entity_type_key":"lipid"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/inositol-research/9593664.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248\", \"start_char\": 0, \"end_char\": 1012, \"text_sha256\": \"118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Phosphatase assays and human cell expression","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Wild-type versus catalytic-mutant PTEN","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Inositol research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"inositol","display_name":"Inositol (stereoisomer family)","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Human protein and HEK293 cells","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A phosphatase reverses a signaling-lipid phosphorylation step.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified enzyme and cultured cells","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"82e9f1cc-93f4-52e3-9716-b86c37f0770b","evidence_kind":"source_excerpt","locator":"Lines 717-728","start_line":717,"end_line":728,"excerpt":"### ino-pten-pip3\nHuman PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2.\nCondition category: normal\nnutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A phosphatase reverses a signaling-lipid phosphorylation step.\norganism: Human protein and HEK293 cells\ntissue_or_cell_type: Purified enzyme and cultured cells\nexperimental_model: Phosphatase assays and human cell expression\nlimitations: Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN.\nexposure: Wild-type versus catalytic-mutant PTEN\nevidence_span: {\"source_cache\": \"artifacts/inositol-research/9593664.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248\", \"start_char\": 0, \"end_char\": 1012, \"text_sha256\": \"118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248\"}\n[ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375","model_system":"Phosphatase assays and human cell expression","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"d590c659-b774-50e6-9f1d-aff61d5f7c9c","stable_key":"import-e69ef6a0-0e23-5eac-aca1-cf333781b962","title":"Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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