{"id":"2f9af20b-0bf5-5f3f-8456-ec36bb3e5099","stable_key":"ec174d5a-4903-5745-8646-df0e9d4265e8:shmt2-loss-mito-translation","predicate":"deletion_reduces","statement":"SHMT2 deletion reduced synthesis of mitochondrially encoded proteins while cytosolic protein labeling was preserved.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"6aa607ab-ca65-55a4-849f-1e78ec8fa07f","mechanism_event_label":"The translation defect was concentrated in mitochondria.","subject":{"id":"a5e9f537-a6cd-570d-a81e-774125a0e1e0","slug":"human-shmt2-gene","display_name":"Human SHMT2 gene","entity_type_key":"gene"},"object":{"id":"d78e2378-bcf6-5ac1-8419-53ea41ff1ac0","slug":"mitochondrial-protein-translation","display_name":"Mitochondrial protein translation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"6aa607ab-ca65-55a4-849f-1e78ec8fa07f","stable_key":"ec174d5a-4903-5745-8646-df0e9d4265e8:shmt2-loss-mito-translation-event","event_type":"biochemical_relationship","label":"The translation defect was concentrated in mitochondria.","description":"SHMT2 deletion reduced synthesis of mitochondrially encoded proteins while cytosolic protein labeling was preserved.","status":"provisional","compartment":{"slug":"mitochondria","display_name":"Mitochondria"},"participants":[{"entity":{"id":"2559e210-62e5-5cd8-bc77-538a9aecd7c8","slug":"shmt2","display_name":"SHMT2","entity_type_key":"protein"},"role":"deleted enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"a5e9f537-a6cd-570d-a81e-774125a0e1e0","slug":"human-shmt2-gene","display_name":"Human SHMT2 gene","entity_type_key":"gene"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"d78e2378-bcf6-5ac1-8419-53ea41ff1ac0","slug":"mitochondrial-protein-translation","display_name":"Mitochondrial protein translation","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; 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Study references: [minton-2018] Serine Catabolism by SHMT2 Is Required for Proper Mitochondrial Translation Initiation and Maintenance of Formylmethionyl-tRNAs (2018). https://pubmed.ncbi.nlm.nih.gov/29452640/ DOI: 10.1016/j.molcel.2018.01.024","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"f4ce1a62-9582-5f7a-84f5-a23d0e1bfc68","stable_key":"import-ec174d5a-4903-5745-8646-df0e9d4265e8","title":"Folate and folic acid: mechanisms, deficiency and nutrient interactions (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":"e564d43989ece1006c95cd0748e9af6fe369074599a2eebba0a99ebff864b0dd","revision_id":"76674a33-b2a1-5e41-b71b-44399038ff7c","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}