{"id":"f2d98cbc-acad-541f-a85f-12f7e65a44d6","stable_key":"6d38d43e-01e4-5641-93be-65654271e242:zinc-enz-ccs-copper","predicate":"delivers_copper_to","statement":"In the purified human protein system, CCS domain 1 was necessary for loading SOD1 with Cu(I).","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"d6df53c9-e730-5555-a924-ed3dd78cc5fd","mechanism_event_label":"SOD1 needs copper delivery as well as zinc binding.","subject":{"id":"51c0049d-9305-553a-ba5d-c1d3b1074801","slug":"ccs","display_name":"Human copper chaperone for SOD1 / CCS","entity_type_key":"protein"},"object":{"id":"19f2bdc0-4888-57d5-860f-119d5d478eb4","slug":"sod1","display_name":"Human copper-zinc superoxide dismutase / SOD1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"d6df53c9-e730-5555-a924-ed3dd78cc5fd","stable_key":"6d38d43e-01e4-5641-93be-65654271e242:zinc-enz-ccs-copper-event","event_type":"biochemical_relationship","label":"SOD1 needs copper delivery as well as zinc binding.","description":"In the purified human protein system, CCS domain 1 was necessary for loading SOD1 with Cu(I).","status":"provisional","compartment":null,"participants":[{"entity":{"id":"162020b5-1fa5-526e-8405-452891245722","slug":"copper-i","display_name":"Copper(I) ion","entity_type_key":"ion"},"role":"transferred_metal","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"49c806c2-7041-5020-8b3b-fa04ffa122ac","slug":"zinc-ion","display_name":"Zinc(II) ion","entity_type_key":"ion"},"role":"distinct_sod1_cofactor","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"51c0049d-9305-553a-ba5d-c1d3b1074801","slug":"ccs","display_name":"Human copper chaperone for SOD1 / CCS","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"19f2bdc0-4888-57d5-860f-119d5d478eb4","slug":"sod1","display_name":"Human copper-zinc superoxide dismutase / SOD1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"true","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human SOD1 and full-length, mutant or truncated human CCS; ESI-MS and NMR","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Human CCS domain constructs and SOD1; ESI-MS and NMR.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Reconstituted human proteins studied in vitro; domain contributions do not imply CCS carries zinc to SOD1 or that zinc supplementation completes copper loading.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Zinc research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"zinc","display_name":"Zinc","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"SOD1 needs copper delivery as well as zinc binding.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[zinc-enz-ccs-2012] Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). (2012). https://pubmed.ncbi.nlm.nih.gov/22869735/ DOI: 10.1073/pnas.1207493109","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified protein; cell-free assay","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"02c48300-3141-5cc1-9ff6-06266a2fdcc7","evidence_kind":"source_excerpt","locator":"Lines 690-701","start_line":690,"end_line":701,"excerpt":"### zinc-enz-ccs-copper\nIn the purified human protein system, CCS domain 1 was necessary for loading SOD1 with Cu(I).\nCondition category: normal\nnutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: SOD1 needs copper delivery as well as zinc binding.\norganism: Homo sapiens\ntissue_or_cell_type: Purified protein; cell-free assay\nexperimental_model: Purified human SOD1 and full-length, mutant or truncated human CCS; ESI-MS and NMR\nlimitations: Reconstituted human proteins studied in vitro; domain contributions do not imply CCS carries zinc to SOD1 or that zinc supplementation completes copper loading.\nexposure: Human CCS domain constructs and SOD1; ESI-MS and NMR.\ncross_nutrient: true\n[zinc-enz-ccs-2012] Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). (2012). https://pubmed.ncbi.nlm.nih.gov/22869735/ DOI: 10.1073/pnas.1207493109","model_system":"Purified human SOD1 and full-length, mutant or truncated human CCS; ESI-MS and NMR","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [zinc-enz-ccs-2012] Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). (2012). https://pubmed.ncbi.nlm.nih.gov/22869735/ DOI: 10.1073/pnas.1207493109","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"c5ee0fee-ce5c-58de-905a-10fb0ea0723c","stable_key":"import-6d38d43e-01e4-5641-93be-65654271e242","title":"Zinc: transport, enzyme loading, 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. 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