{"id":"7c5e55a3-b528-5e35-9903-ced6eac65e9d","stable_key":"56f1d914-e7da-595a-af69-c217b2b47407:l-phenylalanine-dnaj-chaperone","predicate":"interacts_with","statement":"DNAJC12 interacted with aromatic amino-acid hydroxylases, including PAH, tyrosine hydroxylase and tryptophan hydroxylases.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"f1fb0f7f-58ca-5b3a-ae28-a0fdc71dd98d","mechanism_event_label":"A shared chaperone supports several amino-acid processing enzymes.","subject":{"id":"2ea64351-1d24-5e9d-9682-1f81f869f479","slug":"dnajc12","display_name":"Human chaperone DNAJC12","entity_type_key":"protein"},"object":{"id":"ea908671-6f85-5342-abe4-1a466a3b0572","slug":"pah","display_name":"Human phenylalanine hydroxylase / PAH","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"f1fb0f7f-58ca-5b3a-ae28-a0fdc71dd98d","stable_key":"56f1d914-e7da-595a-af69-c217b2b47407:l-phenylalanine-dnaj-chaperone-event","event_type":"observed_relationship","label":"A shared chaperone supports several amino-acid processing enzymes.","description":"DNAJC12 interacted with aromatic amino-acid hydroxylases, including PAH, tyrosine hydroxylase and tryptophan hydroxylases.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"2ea64351-1d24-5e9d-9682-1f81f869f479","slug":"dnajc12","display_name":"Human chaperone DNAJC12","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ea908671-6f85-5342-abe4-1a466a3b0572","slug":"pah","display_name":"Human phenylalanine hydroxylase / PAH","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"190407ad-0219-54b5-b05f-7c75f3895ca6","slug":"l-phenylalanine","display_name":"L-Phenylalanine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"e4e0f24b-1e70-573d-b719-039a90191b90","slug":"human-tyrosine-hydroxylase","display_name":"Human tyrosine hydroxylase","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"1c231b90-c106-507a-8766-870ecb40e368","slug":"tetrahydrobiopterin","display_name":"Tetrahydrobiopterin / BH4","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human DNAJC12 deficiency study with functional interaction experiments.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Interaction does not imply identical effects in all tissues or rescue by extra substrate.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-phenylalanine","display_name":"L-Phenylalanine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A shared chaperone supports several amino-acid processing enzymes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Biallelic Mutations in DNAJC12 Cause Hyperphenylalaninemia, Dystonia, and Intellectual Disability. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28132689/ · DOI 10.1016/j.ajhg.2017.01.002","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"4abb4528-e944-5b09-85ae-1b8963b4d039","evidence_kind":"source_excerpt","locator":"Lines 102-108","start_line":102,"end_line":108,"excerpt":"## l-phenylalanine-dnaj-chaperone\nA shared chaperone supports several amino-acid processing enzymes.\nDNAJC12 interacted with aromatic amino-acid hydroxylases, including PAH, tyrosine hydroxylase and tryptophan hydroxylases.\nModel: Human DNAJC12 deficiency study with functional interaction experiments.\nLimitations: Interaction does not imply identical effects in all tissues or rescue by extra substrate.\nEvidence access: Primary abstract\nBiallelic Mutations in DNAJC12 Cause Hyperphenylalaninemia, Dystonia, and Intellectual Disability. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28132689/ · DOI 10.1016/j.ajhg.2017.01.002","model_system":"Human DNAJC12 deficiency study with functional interaction experiments.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"54de7c56-1e60-5d7b-8ef9-852c58ae92ba","stable_key":"import-56f1d914-e7da-595a-af69-c217b2b47407","title":"L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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