{"id":"39d99acf-4fab-566e-9c86-c8752835b8e2","stable_key":"research:selenof-binds-uggt1","predicate":"binds","statement":"SELENOF associates with human UGGT1 in binding and photo-crosslinking experiments involving ER glycoprotein quality-control proteins.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"literature_reviewed:direct_experimental","direction":"positive","is_public":true,"mechanism_event_id":"0fc767d2-a75f-5d9d-acea-70118ee209e4","mechanism_event_label":"SELENOF partners with a protein-folding inspection enzyme.","subject":{"id":"08dbecc5-e947-558d-b52f-f0d702a06471","slug":"selenof","display_name":"SELENOF","entity_type_key":"protein"},"object":{"id":"2a6ee8f2-b1a3-5e8f-93b2-4a9fd603b06e","slug":"uggt1","display_name":"UGGT1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"0fc767d2-a75f-5d9d-acea-70118ee209e4","stable_key":"research:selenof-binds-uggt1","event_type":"experimentally_scoped_interaction","label":"SELENOF partners with a protein-folding inspection enzyme.","description":"SELENOF associates with human UGGT1 in binding and photo-crosslinking experiments involving ER glycoprotein quality-control proteins.","status":"active","compartment":{"slug":"endoplasmic-reticulum","display_name":"Endoplasmic reticulum"},"participants":[{"entity":{"id":"08dbecc5-e947-558d-b52f-f0d702a06471","slug":"selenof","display_name":"SELENOF","entity_type_key":"protein"},"role":"regulator","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"2a6ee8f2-b1a3-5e8f-93b2-4a9fd603b06e","slug":"uggt1","display_name":"UGGT1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Recombinant SELENOF and truncated human UGGT1 binding/crosslinking assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Binding is directly measured; exact physiological glycoprotein substrates and obligatory disulfide-repair steps are not established by this result.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Human protein constructs","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"3f24644b-e984-5c75-837a-88d2d531766c","evidence_kind":"curated_literature_summary","locator":"lines 1053-1062","start_line":1053,"end_line":1062,"excerpt":"## selenof-binds-uggt1\n\nSELENOF partners with a protein-folding inspection enzyme.\n\nSELENOF associates with human UGGT1 in binding and photo-crosslinking experiments involving ER glycoprotein quality-control proteins.\n\nExperimental model: Recombinant SELENOF and truncated human UGGT1 binding/crosslinking assays.\nOrganism: Human protein constructs\nLimitations: Binding is directly measured; exact physiological glycoprotein substrates and obligatory disulfide-repair steps are not established by this result.\nPrimary reference: [Analysis of Selenoprotein F Binding to UDP-Glucose:Glycoprotein Glucosyltransferase by a Photoreactive Crosslinker](https://pubmed.ncbi.nlm.nih.gov/36219527/)","model_system":"Recombinant SELENOF and truncated human UGGT1 binding/crosslinking assays.","directness":"author_interpretation","verification_status":"secondary_verified","notes":"Curated summary; inspect the linked primary papers for original methods and results.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"4f892f13-06ea-5199-a33c-a703f35c80ae","stable_key":"selenium-research-2026-09-17","title":"Selenium: literature corrections and mechanism additions","document_type":"curated_literature_review","citation_label":"Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually","file_path":"","sha256":"0b818b10c1c7120e5caf7f4d4019d7bd025d745692e424f515d3ef903c9ab7f3","revision_id":"80984e03-5f0f-5877-8094-afef7637444e","review_status":"secondary_verified","notes":"Secondary curated summaries of primary experiments, with explicit models and limitations. Not archived primary full text."}}],"relations":[],"conflicts":[],"corrections":[],"research":{"topic":"Protein folding","plain_language":"SELENOF partners with a protein-folding inspection enzyme.","evidence_scope":"direct_experimental","papers":[{"key":"catalog-selenof-2022","title":"Analysis of Selenoprotein F Binding to UDP-Glucose:Glycoprotein Glucosyltransferase by a Photoreactive Crosslinker","url":"https://pubmed.ncbi.nlm.nih.gov/36219527/","doi":null,"year":2022,"model":"Recombinant SELENOF and truncated human UGGT1 binding/crosslinking assays.","summary":"Maps SELENOF association with UGGT1. The exact physiological glycoprotein/disulfide substrate mechanism remains less certain than the interaction."}]}}