{"gene":"SNRNP25","run_date":"2026-06-10T07:46:37","timeline":{"discoveries":[{"year":2025,"finding":"Cryo-EM structures of the human U11 snRNP in apo and substrate-bound forms revealed that SNRNP25 specifically recognizes U11 snRNA and bridges the particle architecture: SNRNP25 and SNRNP35 bind U11 snRNA, while PDCD7 bridges SNRNP25 and SNRNP48 at the distal ends of the 13-subunit complex. SNRNP48 and ZMAT5 stabilize binding of the incoming 5' splice site. U12-type 5' splice site recognition is achieved through base-pairing to the 5' end of U11 snRNA and non-canonical base-triple interactions with U11 snRNA stem-loop 3.","method":"Cryo-EM structural reconstruction of 13-subunit human U11 snRNP in apo and substrate-bound forms","journal":"Molecular cell","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-EM structure with substrate-bound form revealing molecular interactions and mechanism of 5' splice site recognition, published in peer-reviewed journal","pmids":["39809272"],"is_preprint":false},{"year":2014,"finding":"The LRP1-SNRNP25 fusion gene (formed by fusion of LRP1 with SNRNP25) is recurrent and osteosarcoma-specific; expression of LRP1-SNRNP25 in SAOS-2 osteosarcoma cells promoted cell migration and invasion, as demonstrated by scratch and Transwell assays.","method":"Transcriptome sequencing, RT-PCR, Sanger sequencing, FISH validation; functional overexpression in SAOS-2 cells with migration/invasion assays","journal":"Journal of hematology & oncology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal validation methods (RNA-seq, RT-PCR, FISH) plus functional cell assays in a single lab study; mechanism attributed to fusion product not native SNRNP25","pmids":["25300797"],"is_preprint":false},{"year":2024,"finding":"The LRP1-SNRNP25 fusion protein (formed by fusion of LRP1 exon 8 with SNRNP25 exon 2) promotes osteosarcoma cell invasion and migration via the pJNK/37LRP/MMP2 signaling pathway. Co-immunoprecipitation confirmed that LRP1-SNRNP25 interacts with pJNK and 37LRP; immunofluorescence showed intracellular colocalization. Overexpression upregulated pJNK, 37LRP, and MMP2 protein levels. siRNA knockdown of 37LRP decreased MMP2, and the pJNK inhibitor SP600125 dose-dependently reduced pJNK/37LRP/MMP2 levels, establishing the upstream/downstream order. In vivo, LRP1-SNRNP25 promoted tumor growth and metastasis.","method":"Whole-genome sequencing; scratch and Transwell assays; western blotting; Co-IP mass spectrometry; Co-IP; immunofluorescence; siRNA knockdown; pharmacological inhibition (SP600125); nude mouse xenograft and metastasis model","journal":"Cell death discovery","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (Co-IP-MS, Co-IP, siRNA, pharmacological inhibitor, in vivo) in a single lab; findings are about the fusion protein, not native SNRNP25","pmids":["38678020"],"is_preprint":false},{"year":2025,"finding":"In mouse, homozygous deletion of the Hbab2(th) locus causes peri-implantation lethality; molecular analysis identified Snrnp25 as the candidate gene most likely responsible for this lethal phenotype, as the deletion removes Snrnp25 but does not extend to Egfr (previously proposed as the cause).","method":"Sequence analysis of deletion boundaries, molecular mapping, genetic analysis of homozygous lethal phenotype","journal":"Mammalian genome","confidence":"Low","confidence_rationale":"Tier 3 / Weak — candidate gene identification by deletion mapping; Snrnp25 proposed as responsible but not functionally confirmed by rescue or conditional knockout","pmids":["40399475"],"is_preprint":false}],"current_model":"SNRNP25 is a minor spliceosome-specific factor that structurally recognizes U11 snRNA within the 13-subunit human U11 snRNP complex, bridging SNRNP35 and PDCD7/SNRNP48 to facilitate U12-type 5' splice site recognition via base-pairing and non-canonical base-triple interactions with U11 snRNA stem-loop 3; in osteosarcoma, a recurrent LRP1-SNRNP25 fusion protein (not the native protein) drives cell invasion and migration through the pJNK/37LRP/MMP2 signaling pathway."},"narrative":{"mechanistic_narrative":"SNRNP25 is a minor (U12-type) spliceosome factor that functions as a structural subunit of the 13-subunit human U11 snRNP, where it directs recognition of U12-type 5' splice sites [PMID:39809272]. Within the particle, SNRNP25 specifically recognizes U11 snRNA and, together with SNRNP35, anchors the snRNA, while PDCD7 bridges SNRNP25 and SNRNP48 at the distal ends of the complex; 5' splice site recognition is achieved through base-pairing to the 5' end of U11 snRNA and non-canonical base-triple interactions with U11 snRNA stem-loop 3 [PMID:39809272]. A recurrent, osteosarcoma-specific LRP1-SNRNP25 fusion gene — distinct from the native protein — drives tumor cell migration, invasion, growth, and metastasis through the pJNK/37LRP/MMP2 signaling axis [PMID:25300797, PMID:38678020]. Beyond these structural and oncogenic-fusion findings, the native cellular and organismal roles of SNRNP25 remain largely uncharacterized in the available corpus.","teleology":[{"year":2014,"claim":"Established that SNRNP25 participates in a recurrent, cancer-specific gene fusion, providing the first functional link between the locus and disease even though the activity is carried by the fusion rather than the native protein.","evidence":"Transcriptome sequencing, RT-PCR, Sanger sequencing and FISH validation, plus overexpression in SAOS-2 osteosarcoma cells with scratch and Transwell migration/invasion assays","pmids":["25300797"],"confidence":"Medium","gaps":["Activity attributed to the LRP1-SNRNP25 fusion, not native SNRNP25","Single-lab study without mechanistic pathway dissection","No insight into native SNRNP25 function"]},{"year":2024,"claim":"Resolved the downstream signaling mechanism of the LRP1-SNRNP25 fusion, ordering pJNK upstream of 37LRP and MMP2 to explain its pro-metastatic phenotype.","evidence":"Whole-genome sequencing, Co-IP and Co-IP-MS, immunofluorescence colocalization, siRNA knockdown, pharmacological JNK inhibition (SP600125), and nude mouse xenograft/metastasis models","pmids":["38678020"],"confidence":"Medium","gaps":["Mechanism concerns the fusion protein, not native SNRNP25","Single-lab findings without independent replication","Structural basis of fusion-pJNK/37LRP interaction not resolved"]},{"year":2025,"claim":"Defined the structural role of native SNRNP25 in the minor spliceosome, showing it recognizes U11 snRNA and organizes particle architecture for U12-type 5' splice site selection.","evidence":"Cryo-EM reconstruction of the 13-subunit human U11 snRNP in apo and substrate-bound forms","pmids":["39809272"],"confidence":"High","gaps":["Functional consequences of disrupting SNRNP25 in cells not tested","Dynamics of substrate loading and catalysis not captured beyond the recognition step","No genetic loss-of-function validation in the structural context"]},{"year":2025,"claim":"Proposed SNRNP25 as the gene underlying a peri-implantation lethal mouse deletion, hinting at an essential developmental requirement for the locus.","evidence":"Deletion-boundary sequence analysis and molecular mapping of the homozygous-lethal Hbab2(th) locus","pmids":["40399475"],"confidence":"Low","gaps":["Candidate identification only — not confirmed by rescue or conditional knockout","Causal contribution of Snrnp25 versus other deleted elements unresolved","Mechanism connecting SNRNP25 loss to peri-implantation lethality unknown"]},{"year":null,"claim":"Whether native SNRNP25 loss-of-function disrupts minor-intron splicing in cells and accounts for the proposed embryonic essentiality remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No cellular knockdown/knockout phenotype for native SNRNP25 reported","No demonstrated splicing defect upon SNRNP25 depletion","Link between structural role and organismal essentiality unestablished"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[0]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[0]}],"complexes":["U11 snRNP","minor spliceosome"],"partners":["SNRNP35","PDCD7","SNRNP48","ZMAT5"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9BV90","full_name":"U11/U12 small nuclear ribonucleoprotein 25 kDa protein","aliases":["Minus-99 protein"],"length_aa":132,"mass_kda":15.3,"function":"","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/Q9BV90/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/SNRNP25","classification":"Common Essential","n_dependent_lines":1202,"n_total_lines":1208,"dependency_fraction":0.9950331125827815},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/SNRNP25","total_profiled":1310},"omim":[],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Cytokinetic bridge","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"skeletal muscle","ntpm":123.3}],"url":"https://www.proteinatlas.org/search/SNRNP25"},"hgnc":{"alias_symbol":["U11/U12-25K"],"prev_symbol":["C16orf33"]},"alphafold":{"accession":"Q9BV90","domains":[{"cath_id":"-","chopping":"1-37","consensus_level":"medium","plddt":82.6695,"start":1,"end":37},{"cath_id":"3.10.20.90","chopping":"41-132","consensus_level":"medium","plddt":93.7391,"start":41,"end":132}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9BV90","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9BV90-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9BV90-F1-predicted_aligned_error_v6.png","plddt_mean":90.75},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SNRNP25","jax_strain_url":"https://www.jax.org/strain/search?query=SNRNP25"},"sequence":{"accession":"Q9BV90","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9BV90.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9BV90/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9BV90"}},"corpus_meta":[{"pmid":"16782894","id":"PMC_16782894","title":"Active chromatin hub of the mouse alpha-globin locus forms in a transcription factory of clustered housekeeping genes.","date":"2006","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/16782894","citation_count":91,"is_preprint":false},{"pmid":"26738504","id":"PMC_26738504","title":"Roles of low-density lipoprotein receptor-related protein 1 in tumors.","date":"2016","source":"Chinese journal of cancer","url":"https://pubmed.ncbi.nlm.nih.gov/26738504","citation_count":53,"is_preprint":false},{"pmid":"25300797","id":"PMC_25300797","title":"Recurrent LRP1-SNRNP25 and KCNMB4-CCND3 fusion genes promote tumor cell motility in human osteosarcoma.","date":"2014","source":"Journal of hematology & oncology","url":"https://pubmed.ncbi.nlm.nih.gov/25300797","citation_count":29,"is_preprint":false},{"pmid":"25418192","id":"PMC_25418192","title":"Investigation of osteosarcoma genomics and its impact on targeted therapy: an international collaboration to conquer human osteosarcoma.","date":"2014","source":"Chinese journal of cancer","url":"https://pubmed.ncbi.nlm.nih.gov/25418192","citation_count":10,"is_preprint":false},{"pmid":"38678020","id":"PMC_38678020","title":"The fusion gene LRP1-SNRNP25 drives invasion and migration by activating the pJNK/37LRP/MMP2 signaling pathway in osteosarcoma.","date":"2024","source":"Cell death discovery","url":"https://pubmed.ncbi.nlm.nih.gov/38678020","citation_count":8,"is_preprint":false},{"pmid":"39809272","id":"PMC_39809272","title":"Structural basis of 5' splice site recognition by the minor spliceosome.","date":"2025","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/39809272","citation_count":7,"is_preprint":false},{"pmid":"40399475","id":"PMC_40399475","title":"Snrnp25 is a candidate for the peri-implantation lethal phenotype of the Hba deletions.","date":"2025","source":"Mammalian genome : official journal of the International Mammalian Genome Society","url":"https://pubmed.ncbi.nlm.nih.gov/40399475","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5800,"output_tokens":1377,"usd":0.019027,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8043,"output_tokens":2016,"usd":0.045308,"stage2_stop_reason":"end_turn"},"total_usd":0.064335,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2025,\n      \"finding\": \"Cryo-EM structures of the human U11 snRNP in apo and substrate-bound forms revealed that SNRNP25 specifically recognizes U11 snRNA and bridges the particle architecture: SNRNP25 and SNRNP35 bind U11 snRNA, while PDCD7 bridges SNRNP25 and SNRNP48 at the distal ends of the 13-subunit complex. SNRNP48 and ZMAT5 stabilize binding of the incoming 5' splice site. U12-type 5' splice site recognition is achieved through base-pairing to the 5' end of U11 snRNA and non-canonical base-triple interactions with U11 snRNA stem-loop 3.\",\n      \"method\": \"Cryo-EM structural reconstruction of 13-subunit human U11 snRNP in apo and substrate-bound forms\",\n      \"journal\": \"Molecular cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-EM structure with substrate-bound form revealing molecular interactions and mechanism of 5' splice site recognition, published in peer-reviewed journal\",\n      \"pmids\": [\"39809272\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"The LRP1-SNRNP25 fusion gene (formed by fusion of LRP1 with SNRNP25) is recurrent and osteosarcoma-specific; expression of LRP1-SNRNP25 in SAOS-2 osteosarcoma cells promoted cell migration and invasion, as demonstrated by scratch and Transwell assays.\",\n      \"method\": \"Transcriptome sequencing, RT-PCR, Sanger sequencing, FISH validation; functional overexpression in SAOS-2 cells with migration/invasion assays\",\n      \"journal\": \"Journal of hematology & oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal validation methods (RNA-seq, RT-PCR, FISH) plus functional cell assays in a single lab study; mechanism attributed to fusion product not native SNRNP25\",\n      \"pmids\": [\"25300797\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The LRP1-SNRNP25 fusion protein (formed by fusion of LRP1 exon 8 with SNRNP25 exon 2) promotes osteosarcoma cell invasion and migration via the pJNK/37LRP/MMP2 signaling pathway. Co-immunoprecipitation confirmed that LRP1-SNRNP25 interacts with pJNK and 37LRP; immunofluorescence showed intracellular colocalization. Overexpression upregulated pJNK, 37LRP, and MMP2 protein levels. siRNA knockdown of 37LRP decreased MMP2, and the pJNK inhibitor SP600125 dose-dependently reduced pJNK/37LRP/MMP2 levels, establishing the upstream/downstream order. In vivo, LRP1-SNRNP25 promoted tumor growth and metastasis.\",\n      \"method\": \"Whole-genome sequencing; scratch and Transwell assays; western blotting; Co-IP mass spectrometry; Co-IP; immunofluorescence; siRNA knockdown; pharmacological inhibition (SP600125); nude mouse xenograft and metastasis model\",\n      \"journal\": \"Cell death discovery\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (Co-IP-MS, Co-IP, siRNA, pharmacological inhibitor, in vivo) in a single lab; findings are about the fusion protein, not native SNRNP25\",\n      \"pmids\": [\"38678020\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"In mouse, homozygous deletion of the Hbab2(th) locus causes peri-implantation lethality; molecular analysis identified Snrnp25 as the candidate gene most likely responsible for this lethal phenotype, as the deletion removes Snrnp25 but does not extend to Egfr (previously proposed as the cause).\",\n      \"method\": \"Sequence analysis of deletion boundaries, molecular mapping, genetic analysis of homozygous lethal phenotype\",\n      \"journal\": \"Mammalian genome\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — candidate gene identification by deletion mapping; Snrnp25 proposed as responsible but not functionally confirmed by rescue or conditional knockout\",\n      \"pmids\": [\"40399475\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SNRNP25 is a minor spliceosome-specific factor that structurally recognizes U11 snRNA within the 13-subunit human U11 snRNP complex, bridging SNRNP35 and PDCD7/SNRNP48 to facilitate U12-type 5' splice site recognition via base-pairing and non-canonical base-triple interactions with U11 snRNA stem-loop 3; in osteosarcoma, a recurrent LRP1-SNRNP25 fusion protein (not the native protein) drives cell invasion and migration through the pJNK/37LRP/MMP2 signaling pathway.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SNRNP25 is a minor (U12-type) spliceosome factor that functions as a structural subunit of the 13-subunit human U11 snRNP, where it directs recognition of U12-type 5' splice sites [#0]. Within the particle, SNRNP25 specifically recognizes U11 snRNA and, together with SNRNP35, anchors the snRNA, while PDCD7 bridges SNRNP25 and SNRNP48 at the distal ends of the complex; 5' splice site recognition is achieved through base-pairing to the 5' end of U11 snRNA and non-canonical base-triple interactions with U11 snRNA stem-loop 3 [#0]. A recurrent, osteosarcoma-specific LRP1-SNRNP25 fusion gene — distinct from the native protein — drives tumor cell migration, invasion, growth, and metastasis through the pJNK/37LRP/MMP2 signaling axis [#1, #2]. Beyond these structural and oncogenic-fusion findings, the native cellular and organismal roles of SNRNP25 remain largely uncharacterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Established that SNRNP25 participates in a recurrent, cancer-specific gene fusion, providing the first functional link between the locus and disease even though the activity is carried by the fusion rather than the native protein.\",\n      \"evidence\": \"Transcriptome sequencing, RT-PCR, Sanger sequencing and FISH validation, plus overexpression in SAOS-2 osteosarcoma cells with scratch and Transwell migration/invasion assays\",\n      \"pmids\": [\"25300797\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Activity attributed to the LRP1-SNRNP25 fusion, not native SNRNP25\",\n        \"Single-lab study without mechanistic pathway dissection\",\n        \"No insight into native SNRNP25 function\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Resolved the downstream signaling mechanism of the LRP1-SNRNP25 fusion, ordering pJNK upstream of 37LRP and MMP2 to explain its pro-metastatic phenotype.\",\n      \"evidence\": \"Whole-genome sequencing, Co-IP and Co-IP-MS, immunofluorescence colocalization, siRNA knockdown, pharmacological JNK inhibition (SP600125), and nude mouse xenograft/metastasis models\",\n      \"pmids\": [\"38678020\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Mechanism concerns the fusion protein, not native SNRNP25\",\n        \"Single-lab findings without independent replication\",\n        \"Structural basis of fusion-pJNK/37LRP interaction not resolved\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Defined the structural role of native SNRNP25 in the minor spliceosome, showing it recognizes U11 snRNA and organizes particle architecture for U12-type 5' splice site selection.\",\n      \"evidence\": \"Cryo-EM reconstruction of the 13-subunit human U11 snRNP in apo and substrate-bound forms\",\n      \"pmids\": [\"39809272\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Functional consequences of disrupting SNRNP25 in cells not tested\",\n        \"Dynamics of substrate loading and catalysis not captured beyond the recognition step\",\n        \"No genetic loss-of-function validation in the structural context\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Proposed SNRNP25 as the gene underlying a peri-implantation lethal mouse deletion, hinting at an essential developmental requirement for the locus.\",\n      \"evidence\": \"Deletion-boundary sequence analysis and molecular mapping of the homozygous-lethal Hbab2(th) locus\",\n      \"pmids\": [\"40399475\"],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Candidate identification only — not confirmed by rescue or conditional knockout\",\n        \"Causal contribution of Snrnp25 versus other deleted elements unresolved\",\n        \"Mechanism connecting SNRNP25 loss to peri-implantation lethality unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether native SNRNP25 loss-of-function disrupts minor-intron splicing in cells and accounts for the proposed embryonic essentiality remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No cellular knockdown/knockout phenotype for native SNRNP25 reported\",\n        \"No demonstrated splicing defect upon SNRNP25 depletion\",\n        \"Link between structural role and organismal essentiality unestablished\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [\"U11 snRNP\", \"minor spliceosome\"],\n    \"partners\": [\"SNRNP35\", \"PDCD7\", \"SNRNP48\", \"ZMAT5\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":3,"faith_total":3,"faith_pct":100.0}}