{"id":"3dd934f7-1bfa-5346-8cf1-7c70aee4b834","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:ep300-lysine-acetylation","predicate":"acetylates","statement":"EP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"74fd13a6-0002-54f9-80c4-12adee36b002","mechanism_event_label":"Acetyl groups can be written onto lysines already present in proteins.","subject":{"id":"9052514f-cb56-57bc-8df8-62b26b2ce3a2","slug":"ep300","display_name":"EP300","entity_type_key":"protein"},"object":{"id":"44399a64-dd8a-5818-a863-b3389c6adf37","slug":"protein-bound-lysine","display_name":"Protein-bound lysine residue","entity_type_key":"protein_state"},"evidence_count":1,"mechanism_event":{"id":"74fd13a6-0002-54f9-80c4-12adee36b002","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:ep300-lysine-acetylation-event","event_type":"biochemical_relationship","label":"Acetyl groups can be written onto lysines already present in proteins.","description":"EP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9052514f-cb56-57bc-8df8-62b26b2ce3a2","slug":"ep300","display_name":"EP300","entity_type_key":"protein"},"role":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"44399a64-dd8a-5818-a863-b3389c6adf37","slug":"protein-bound-lysine","display_name":"Protein-bound lysine residue","entity_type_key":"protein_state"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"b7ed6e4c-e560-5cee-b68f-895f21862e6f","slug":"acetyl-coa","display_name":"Acetyl-CoA","entity_type_key":"small_molecule"},"role":"donor","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"91fc0649-d01a-5156-bb89-b10e003b9b65","slug":"protein-acetyllysine","display_name":"Protein N6-acetyllysine residues","entity_type_key":"protein_state"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"4faa6456-aff8-59eb-9e3f-3326a436e401","slug":"coenzyme-a","display_name":"Coenzyme A","entity_type_key":"small_molecule"},"role":"coproduct","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Human p300 catalytic-domain structure and biochemical assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Acetyl groups can be written onto lysines already present in proteins.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Not specified as a whole tissue; see experimental model.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"616faf52-bc9a-5db9-9c90-245185fb8af8","evidence_kind":"source_excerpt","locator":"Lines 527-535","start_line":527,"end_line":535,"excerpt":"### ep300-lysine-acetylation\nEP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain.\nPlain language: Acetyl groups can be written onto lysines already present in proteins.\nCondition category: normal\norganism: Human\ntissue_or_cell_type: Not specified as a whole tissue; see experimental model.\nexperimental_model: Human p300 catalytic-domain structure and biochemical assays.\nlimitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.\n[p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546","model_system":"Human p300 catalytic-domain structure and biochemical assays.","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact quote from the accompanying curation document, not from publisher text. Original study references: [p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"7633bde7-dcc9-5086-91c6-a45eb96857f3","stable_key":"import-c3df3634-4c3a-5099-a5d9-e4f6344c1084","title":"L-Lysine: mechanism-first literature curation (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"93998d47c21525409ba82f1c82ededf2893dff15fbe61c7deffc175b0e298e97","revision_id":"3897e31f-6624-59e1-a053-8a81b7361632","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}