{"gene":"ANP32B","run_date":"2026-06-14T07:33:11","timeline":{"discoveries":[],"current_model":"Parse failed"},"narrative":{"mechanistic_narrative":"No mechanistic discoveries found in literature.","teleology":[],"mechanism_profile":null},"prefetch_data":{"uniprot":{"accession":"Q92688","full_name":"Acidic leucine-rich nuclear phosphoprotein 32 family member B","aliases":["Acidic protein rich in leucines","Putative HLA-DR-associated protein I-2","PHAPI2","Silver-stainable protein SSP29"],"length_aa":251,"mass_kda":28.8,"function":"Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription (PubMed:18039846, PubMed:20015864). Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis (PubMed:20015864). Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes (PubMed:18039846, PubMed:20538007). Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1 (PubMed:17178712). Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation (By similarity) (Microbial infection) Plays an essential role in influenza A and B viral genome replication (PubMed:31217244, PubMed:33045004). Also plays a role in foamy virus mRNA export from the nucleus to the cytoplasm (PubMed:21159877)","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/Q92688/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ANP32B","classification":"Not Classified","n_dependent_lines":20,"n_total_lines":1208,"dependency_fraction":0.016556291390728478},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"H2AFZ","stoichiometry":0.2},{"gene":"KPNA1","stoichiometry":0.2},{"gene":"KPNA6","stoichiometry":0.2},{"gene":"PARP1","stoichiometry":0.2},{"gene":"SAR1B","stoichiometry":0.2},{"gene":"SRP9","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/ANP32B","total_profiled":1310},"omim":[{"mim_id":"619823","title":"ACIDIC NUCLEAR PHOSPHOPROTEIN 32 FAMILY, MEMBER B; ANP32B","url":"https://www.omim.org/entry/619823"},{"mim_id":"600832","title":"ACIDIC NUCLEAR PHOSPHOPROTEIN 32 FAMILY, MEMBER A; ANP32A","url":"https://www.omim.org/entry/600832"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Centrosome","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ANP32B"},"hgnc":{"alias_symbol":["SSP29","PHAPI2","APRIL"],"prev_symbol":[]},"alphafold":{"accession":"Q92688","domains":[{"cath_id":"3.80.10.10","chopping":"4-146","consensus_level":"medium","plddt":95.5453,"start":4,"end":146}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q92688","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q92688-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q92688-F1-predicted_aligned_error_v6.png","plddt_mean":79.0},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ANP32B","jax_strain_url":"https://www.jax.org/strain/search?query=ANP32B"},"sequence":{"accession":"Q92688","fasta_url":"https://rest.uniprot.org/uniprotkb/Q92688.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q92688/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q92688"}},"corpus_meta":[{"pmid":"30996088","id":"PMC_30996088","title":"Fundamental Contribution and Host Range Determination of ANP32A and ANP32B in Influenza A Virus Polymerase Activity.","date":"2019","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/30996088","citation_count":70,"is_preprint":false},{"pmid":"20015864","id":"PMC_20015864","title":"Downregulation of ANP32B, a novel substrate of caspase-3, enhances caspase-3 activation and apoptosis induction in myeloid leukemic cells.","date":"2009","source":"Carcinogenesis","url":"https://pubmed.ncbi.nlm.nih.gov/20015864","citation_count":50,"is_preprint":false},{"pmid":"18039846","id":"PMC_18039846","title":"Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5.","date":"2007","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/18039846","citation_count":43,"is_preprint":false},{"pmid":"37074204","id":"PMC_37074204","title":"Mammalian ANP32A and ANP32B Proteins Drive Differential Polymerase Adaptations in Avian Influenza Virus.","date":"2023","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/37074204","citation_count":39,"is_preprint":false},{"pmid":"38750014","id":"PMC_38750014","title":"Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.","date":"2024","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/38750014","citation_count":38,"is_preprint":false},{"pmid":"20538007","id":"PMC_20538007","title":"Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.","date":"2010","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/20538007","citation_count":34,"is_preprint":false},{"pmid":"24823948","id":"PMC_24823948","title":"ANP32B is a nuclear target of henipavirus M proteins.","date":"2014","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/24823948","citation_count":28,"is_preprint":false},{"pmid":"36170346","id":"PMC_36170346","title":"BRD4 PROTAC degrader MZ1 exerts anticancer effects in acute myeloid leukemia by targeting c-Myc and ANP32B genes.","date":"2022","source":"Cancer biology & therapy","url":"https://pubmed.ncbi.nlm.nih.gov/36170346","citation_count":27,"is_preprint":false},{"pmid":"26844697","id":"PMC_26844697","title":"ANP32B deficiency impairs proliferation and suppresses tumor progression by regulating AKT phosphorylation.","date":"2016","source":"Cell death & disease","url":"https://pubmed.ncbi.nlm.nih.gov/26844697","citation_count":24,"is_preprint":false},{"pmid":"33882408","id":"PMC_33882408","title":"Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c.","date":"2021","source":"Redox biology","url":"https://pubmed.ncbi.nlm.nih.gov/33882408","citation_count":23,"is_preprint":false},{"pmid":"30890743","id":"PMC_30890743","title":"The acidic protein rich in leucines Anp32b is an immunomodulator of inflammation in mice.","date":"2019","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/30890743","citation_count":17,"is_preprint":false},{"pmid":"31444273","id":"PMC_31444273","title":"ANP32A and ANP32B are key factors in the Rev-dependent CRM1 pathway for nuclear export of HIV-1 unspliced mRNA.","date":"2019","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/31444273","citation_count":16,"is_preprint":false},{"pmid":"28486557","id":"PMC_28486557","title":"Downregulation of ANP32B exerts anti-apoptotic effects in hepatocellular carcinoma.","date":"2017","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/28486557","citation_count":16,"is_preprint":false},{"pmid":"9285060","id":"PMC_9285060","title":"Cloning and characterization of a new silver-stainable protein SSP29, a member of the LRR family.","date":"1997","source":"Biochemistry and molecular biology international","url":"https://pubmed.ncbi.nlm.nih.gov/9285060","citation_count":14,"is_preprint":false},{"pmid":"31793855","id":"PMC_31793855","title":"Interaction of host cellular factor ANP32B with matrix proteins of different paramyxoviruses.","date":"2020","source":"The Journal of general virology","url":"https://pubmed.ncbi.nlm.nih.gov/31793855","citation_count":14,"is_preprint":false},{"pmid":"34359074","id":"PMC_34359074","title":"ANP32B-mediated repression of p53 contributes to maintenance of normal and CML stem cells.","date":"2021","source":"Blood","url":"https://pubmed.ncbi.nlm.nih.gov/34359074","citation_count":13,"is_preprint":false},{"pmid":"22705300","id":"PMC_22705300","title":"Acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) contributes to retinoic acid-induced differentiation of leukemic cells.","date":"2012","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/22705300","citation_count":13,"is_preprint":false},{"pmid":"34524075","id":"PMC_34524075","title":"A natural variant in ANP32B impairs influenza virus replication in human cells.","date":"2021","source":"The Journal of general virology","url":"https://pubmed.ncbi.nlm.nih.gov/34524075","citation_count":12,"is_preprint":false},{"pmid":"38383388","id":"PMC_38383388","title":"Super enhancer related gene ANP32B promotes the proliferation of acute myeloid leukemia by enhancing MYC through histone acetylation.","date":"2024","source":"Cancer cell international","url":"https://pubmed.ncbi.nlm.nih.gov/38383388","citation_count":9,"is_preprint":false},{"pmid":"37137487","id":"PMC_37137487","title":"ANP32B suppresses B-cell acute lymphoblastic leukemia through activation of PU.1 in mice.","date":"2023","source":"Cancer science","url":"https://pubmed.ncbi.nlm.nih.gov/37137487","citation_count":7,"is_preprint":false},{"pmid":"29106904","id":"PMC_29106904","title":"Prothymosin α interacts with SET, ANP32A and ANP32B and other cytoplasmic and mitochondrial proteins in proliferating cells.","date":"2017","source":"Archives of biochemistry and biophysics","url":"https://pubmed.ncbi.nlm.nih.gov/29106904","citation_count":5,"is_preprint":false},{"pmid":"36642319","id":"PMC_36642319","title":"ANP32B promotes lung cancer progression by regulating VDAC1.","date":"2023","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/36642319","citation_count":4,"is_preprint":false},{"pmid":"38192816","id":"PMC_38192816","title":"ANP32B promotes colorectal cancer cell progression and reduces cell sensitivity to PRAP1 inhibitor through up-regulating HPF1.","date":"2023","source":"Heliyon","url":"https://pubmed.ncbi.nlm.nih.gov/38192816","citation_count":3,"is_preprint":false},{"pmid":"26558540","id":"PMC_26558540","title":"BALB/c-congenic ANP32B-deficient mice reveal a modifying locus that determines viability.","date":"2015","source":"Experimental animals","url":"https://pubmed.ncbi.nlm.nih.gov/26558540","citation_count":3,"is_preprint":false},{"pmid":"38266312","id":"PMC_38266312","title":"ANP32B inhibition suppresses the growth of prostate cancer cells by regulating c-Myc signaling.","date":"2024","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/38266312","citation_count":1,"is_preprint":false},{"pmid":"39504945","id":"PMC_39504945","title":"Anp32b Deficiency Suppresses Ocular Development by Repression of Pax6.","date":"2024","source":"Ophthalmic research","url":"https://pubmed.ncbi.nlm.nih.gov/39504945","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.09.16.613268","title":"A single ancestral  <i>ANP32</i>  locus in ticks creates multiple protein variants that all support the Thogoto virus polymerase","date":"2024-09-17","source":"bioRxiv","url":"https://doi.org/10.1101/2024.09.16.613268","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":14821,"output_tokens":3130,"usd":0.045706,"stage1_stop_reason":"refusal"},"stage2":{"model":"","input_tokens":0,"output_tokens":0,"usd":0.0},"total_usd":0.045706,"stage1_batch_id":"msgbatch_015cW3C55o5xm8EPaM1UvcZR","stage2_batch_id":"msgbatch_018NDJHPntdYJzBohpB6hHKo","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1997,\n      \"finding\": \"ANP32B (SSP29) localizes to the nucleoplasm and partially translocates to nucleoli after heat shock; it interacts with RNA polymerase I, suggesting a role in regulating ribosomal RNA biosynthesis. The protein has leucine-rich repeats near the N-terminus and acidic clusters at the C-terminus.\",\n      \"method\": \"Ag-NOR staining, subcellular fractionation, interaction with RNA polymerase I (co-purification)\",\n      \"journal\": \"Biochemistry and molecular biology international\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single method for each finding, no functional mutagenesis\",\n      \"pmids\": [\"9285060\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2007,\n      \"finding\": \"ANP32B functions as a histone chaperone that is recruited to gene promoters through direct interaction with the DNA-binding transcription factor KLF5, resulting in promoter region-specific histone incorporation, inhibition of histone acetylation, and transcriptional repression of a KLF5 downstream gene. Phorbol ester treatment regulates this mechanism.\",\n      \"method\": \"Co-immunoprecipitation, chromatin immunoprecipitation, reporter assays, nucleosome assembly assay, overexpression/knockdown\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus ChIP plus functional reporter assay in single lab\",\n      \"pmids\": [\"18039846\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"ANP32B is a direct substrate of caspase-3, cleaved at the sequence Ala-Glu-Val-Asp after Asp-163, generating an ~17 kDa fragment during apoptosis. Knockdown of ANP32B enhances caspase-3 activation and apoptosis, indicating ANP32B acts as a negative regulator of apoptosis.\",\n      \"method\": \"In vitro caspase cleavage assay, site-directed mutagenesis, caspase-3 inhibitor (Z-DEVD-fmk), caspase-3-deficient MCF-7 cells, siRNA knockdown\",\n      \"journal\": \"Carcinogenesis\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro cleavage assay combined with mutagenesis and genetic (caspase-3-deficient cell) validation, multiple orthogonal methods\",\n      \"pmids\": [\"20015864\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"The LRR domain of ANP32B possesses histone chaperone activity and adopts a curved structure with a parallel beta-sheet on the concave side; interaction with core histones H3-H4 occurs on this concave surface, with both acidic and hydrophobic residues critical for histone binding.\",\n      \"method\": \"NMR solution structure, in vitro histone binding assays, mutagenesis of concave surface residues\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — NMR structure with functional mutagenesis and in vitro binding assays, multiple orthogonal methods in single study\",\n      \"pmids\": [\"20538007\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"ANP32B interacts with Hendra virus (HeV) and Nipah virus (NiV) matrix (M) proteins and causes nuclear accumulation of HeV M protein; this ANP32B-dependent nuclear accumulation was observed both in plasmid-driven expression and in NiV-infected cells.\",\n      \"method\": \"Co-immunoprecipitation of tagged HeV M protein complexes followed by mass spectrometry identification of ANP32B; overexpression of ANP32B with nuclear accumulation readout; NiV infection model\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — MS-identified interaction confirmed by overexpression functional consequence in both plasmid and infection contexts, single lab\",\n      \"pmids\": [\"24823948\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"ANP32B deficiency downregulates AKT phosphorylation, linking ANP32B to cell proliferation control; Anp32b-knockout mouse embryo fibroblasts and knockdown cancer cells show slower proliferation and G1 arrest.\",\n      \"method\": \"Anp32b knockout mouse model, RNAi knockdown, Western blotting for phospho-AKT, in vitro and in vivo growth assays\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic KO and RNAi with defined molecular readout (p-AKT), single lab\",\n      \"pmids\": [\"26844697\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Human ANP32B (and ANP32A) are each individually indispensable for human influenza A virus RNA replication; double knockout of both is required to abolish replication, showing redundancy. Neither supports avian viral polymerase. In chicken ANP32B, amino acids 129–130 are responsible for the loss of viral replication support and reduced interaction with the viral polymerase complex.\",\n      \"method\": \"Double-knockout cell lines, reconstitution with individual ANP32A/B, minigenome polymerase activity assay, mutagenesis at residues 129–130, co-immunoprecipitation with viral polymerase\",\n      \"journal\": \"Journal of virology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — genetic KO plus reconstitution plus mutagenesis plus Co-IP, multiple orthogonal approaches in single study\",\n      \"pmids\": [\"30996088\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"ANP32B (and ANP32A) interact with both HIV-1 Rev and CRM1 and mediate nuclear export of unspliced/partially spliced HIV-1 mRNA via the Rev-CRM1 pathway; double knockout of ANP32A and ANP32B causes nuclear accumulation of unspliced viral mRNA and loss of Gag expression, which is rescued by reconstitution of either protein.\",\n      \"method\": \"Double-knockout cell lines, reconstitution, nuclear/cytoplasmic RNA fractionation, co-immunoprecipitation with Rev and CRM1, Western blotting for Gag\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic KO, reconstitution, reciprocal Co-IPs and RNA fractionation, multiple orthogonal methods\",\n      \"pmids\": [\"31444273\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"ANP32B interacts specifically with henipavirus and several other paramyxovirus M proteins (NDV, SeV, MeV, CDV), but not pneumovirus M. The NLS of ANP32B is dispensable for HeV M binding. Neither the acidic region nor the leucine-rich repeats of ANP32 alone mediate the henipavirus M interaction. NDV M and SeV M accumulate in the nucleus ANP32B-dependently, while morbillivirus M proteins do not despite the ability to form complexes.\",\n      \"method\": \"Specific co-purification (M-ANP32B but not M-ANP32A complexes), domain deletion mutants, nuclear accumulation assay with ANP32B overexpression, nuclear export inhibition\",\n      \"journal\": \"The Journal of general virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal domain-deletion pulldowns plus functional nuclear accumulation assay, single lab\",\n      \"pmids\": [\"31793855\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"ANP32B inhibits PP2A phosphatase activity (designated I3PP2A); upon camptothecin-induced DNA damage, cytochrome c translocates from mitochondria to the nucleus and binds the C-terminal low-complexity acidic region (LCAR) of ANP32B, inducing long-range allosteric changes in the N-terminal LRR domain that regulate ANP32B-dependent PP2A inhibition. The nucleosome assembly activity of ANP32B is unaffected by cytochrome c binding.\",\n      \"method\": \"Co-immunoprecipitation of endogenous ANP32B with endogenous cytochrome c, PP2A activity assay, biophysical binding assays (ITC), nuclear fractionation, domain-specific binding mapping\",\n      \"journal\": \"Redox biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — endogenous Co-IP, PP2A enzymatic assay, ITC biophysics in single lab\",\n      \"pmids\": [\"33882408\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"ANP32B forms a repressive complex with p53 and inhibits p53 transcriptional activity in hematopoietic cells; conditional deletion of Anp32b in hematopoietic cells impairs HSC repopulation and post-injury regeneration, and these defects are rescued by p53 deletion.\",\n      \"method\": \"Conditional knockout mice, co-immunoprecipitation (ANP32B-p53 complex), p53 transcriptional reporter assay, genetic rescue (p53 deletion), bone marrow transplantation/repopulation assays\",\n      \"journal\": \"Blood\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — Co-IP of complex, genetic epistasis rescue with p53 KO, functional reconstitution in vivo, multiple orthogonal methods\",\n      \"pmids\": [\"34359074\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"A naturally occurring human variant ANP32B-D130A is less able to support influenza polymerase activity, binds FluPol with lower affinity, exerts a dominant-negative effect over wild-type ANP32B, and interferes with ANP32A; CRISPR-edited cells expressing D130A show attenuated FluPol activity and viral replication, suggesting this variant impairs FluPol dimer formation.\",\n      \"method\": \"CRISPR editing of endogenous ANP32B locus, minigenome polymerase activity assay, co-immunoprecipitation for binding affinity, viral replication assay\",\n      \"journal\": \"The Journal of general virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPR-edited cells plus Co-IP plus functional polymerase assay, single lab\",\n      \"pmids\": [\"34524075\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"PB2-E627K mammalian adaptation strongly favors use of ANP32B over ANP32A, while PB2-D701N shows no such bias. The pro-viral support of ANP32B for PB2-E627K maps to the LCAR tail of ANP32B. Experimental evolution in human cells drove acquisition of PB2-E627K but not in the absence of ANP32B.\",\n      \"method\": \"ANP32B knockout/reconstitution cell lines, minigenome polymerase assay, experimental viral evolution passaging, LCAR domain swap/deletion mutants\",\n      \"journal\": \"Journal of virology\",\n      \"confidence","stage2_raw":"","audit_flag":{"gene":"ANP32B","tier":"GROUNDING","verdict":"Evidence-grounding concern","subtype":"recall_miss","uniprot_band":"rich","rules_fired":"R5","issue":"R5: no narrative despite experimental UniProt FUNCTION (1169 chars) and on-target evidence in corpus (26 on-target corpus titles)"},"evaluation":null}