{"id":"9fa2931e-7606-5a9b-b713-e0d4e1135155","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-dars1-translation","predicate":"loads_aspartate_onto","statement":"Human cytosolic DARS1 catalyzes attachment of aspartate to its cognate tRNA; its 2.25-angstrom homodimer structure defines the cytosolic enzyme separately from mitochondrial DARS2.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"886158c5-8e83-5316-96ef-676d9d97ef9f","mechanism_event_label":"Aspartate must be placed on the correct transfer RNA to enter proteins.","subject":{"id":"565857c6-072c-55f5-a50b-63e5627a3f20","slug":"dars1","display_name":"Human cytosolic aspartyl-tRNA synthetase / DARS1","entity_type_key":"protein"},"object":{"id":"2d849182-b9b4-5843-8f84-2bba5f5fe861","slug":"human-cytosolic-trna-asp","display_name":"Human cytosolic aspartate tRNA","entity_type_key":"rna"},"evidence_count":1,"mechanism_event":{"id":"886158c5-8e83-5316-96ef-676d9d97ef9f","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-dars1-translation-event","event_type":"observed_relationship","label":"Aspartate must be placed on the correct transfer RNA to enter proteins.","description":"Human cytosolic DARS1 catalyzes attachment of aspartate to its cognate tRNA; its 2.25-angstrom homodimer structure defines the cytosolic enzyme separately from mitochondrial DARS2.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"565857c6-072c-55f5-a50b-63e5627a3f20","slug":"dars1","display_name":"Human cytosolic aspartyl-tRNA synthetase / DARS1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"2d849182-b9b4-5843-8f84-2bba5f5fe861","slug":"human-cytosolic-trna-asp","display_name":"Human cytosolic aspartate tRNA","entity_type_key":"rna"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"0a0923d3-72b7-5d6a-bf3a-5a7a3071a09b","slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human recombinant cytosolic enzyme structural study.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural suggestions about release from the multisynthetase complex are not treated as demonstrated nutrient signaling.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Aspartate must be placed on the correct transfer RNA to enter proteins.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23609930/ · DOI 10.1002/prot.24306","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a8945763-7352-5c7a-bbe8-f63224c0b61d","evidence_kind":"source_excerpt","locator":"Lines 354-360","start_line":354,"end_line":360,"excerpt":"## l-aspartate-dars1-translation\nAspartate must be placed on the correct transfer RNA to enter proteins.\nHuman cytosolic DARS1 catalyzes attachment of aspartate to its cognate tRNA; its 2.25-angstrom homodimer structure defines the cytosolic enzyme separately from mitochondrial DARS2.\nModel: Human recombinant cytosolic enzyme structural study.\nLimitations: Structural suggestions about release from the multisynthetase complex are not treated as demonstrated nutrient signaling.\nEvidence access: Primary full text\nCrystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23609930/ · DOI 10.1002/prot.24306","model_system":"Human recombinant cytosolic enzyme structural study.","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":"67970dcb-34e0-5b0a-8c86-d8c3cc183444","stable_key":"import-e37461ea-ea5d-5e2c-8091-138305f6dd70","title":"L-Aspartate: redox transfer, nitrogen partitioning 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. Not publisher full text.","file_path":"","sha256":"a2791036b8f554be57d0b40892634bb9c900fa03e7e4c9c95ca08428ed52d614","revision_id":"150613bb-a227-5ec9-9f5c-fb13f5da50c8","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}