{"gene":"SNRPD3","run_date":"2026-06-10T07:46:37","timeline":{"discoveries":[{"year":2005,"finding":"Symmetrical dimethylarginine (sDMA) post-translational modification of SmD3 C-terminal arginines is NOT required for snRNP assembly or nuclear transport; mutating the modified arginines to leucines in SmD3 did not interfere with assembly or nuclear import of the transiently expressed variant.","method":"Site-directed mutagenesis (arginine-to-leucine substitutions) of SmD3, transient expression, and assessment of snRNP assembly and nuclear transport","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — clean mutagenesis with cellular localization/assembly readout, single lab, single study","pmids":["16236255"],"is_preprint":false},{"year":2004,"finding":"SmD3 carries symmetrical dimethylarginine at specific C-terminal residues (including position 112), and this modification is an essential component of a major autoepitope recognized by a subpopulation of anti-Sm antibodies in SLE patients.","method":"Immobilized synthetic peptide ELISA using dimethylated vs. unmodified SmD3 peptides to map autoantibody reactivity","journal":"Arthritis research & therapy","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — peptide-based ELISA, replicated across multiple SLE cohorts, but indirect (antibody-binding assay, not biochemical modification mapping)","pmids":["15642139"],"is_preprint":false},{"year":2012,"finding":"Haploinsufficiency of SmD3 (one allele disrupted by proviral insertion) reduces snRNA U4 and U5 levels, decreases snoRNA expression and snoRNA-containing intron lariat abundance, implicating SmD3 as a critical regulator of intronic noncoding RNA biogenesis upstream of metabolic stress response pathways, while still supporting pre-mRNA splicing.","method":"Retroviral promoter trap mutagenesis to generate SmD3 haploinsufficient CHO cell lines; Northern blot and quantitative analysis of snRNAs, snoRNAs, and intron lariats","journal":"Molecular and cellular biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — defined genetic model (haploinsufficiency), multiple RNA readouts, single lab","pmids":["22869524"],"is_preprint":false},{"year":2014,"finding":"Yeast SmD3 residues Glu37/Asp38 contact Yhc1 (yeast U1-C) Arg21 to fortify the U1 snRNP–5' splice site complex; mutations at this interface synergize with mud2Δ and bypass the essential DEAD-box ATPase Prp28, consistent with destabilization of U1•5'SS interaction.","method":"Structure-guided mutagenesis of yeast SmD3 and Yhc1 combined with genetic interaction (synthetic lethality/suppression) assays in yeast","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — structure-guided mutagenesis plus multiple orthogonal genetic epistasis tests (synthetic lethality, suppression of prp28Δ), single lab but rigorous","pmids":["24497193"],"is_preprint":false},{"year":2015,"finding":"The RNA-binding triad of SmD3 (Ser-Asn-Arg) participates in snRNA binding with built-in redundancy with SmB's triad; simultaneous mutation of Asn or Arg in both SmD3 and SmB is lethal. SmD3 C-terminal truncations and RNA-site mutations are lethal in cells lacking U2 snRNP subunit Lea1, placing SmD3 function at the U1–U2 snRNP interface.","method":"Systematic alanine mutagenesis of SmD3 RNA-binding residues combined with synthetic lethality/genetic interaction assays (mud2Δ, lea1Δ, mud1Δ, nam8Δ) in yeast","journal":"RNA (New York, N.Y.)","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — systematic mutagenesis plus multiple orthogonal genetic epistasis tests across U1 and U2 snRNP components, single lab","pmids":["25897024"],"is_preprint":false},{"year":2019,"finding":"Drosophila SmD3 binds ribosomal protein RpL18 (a large ribosome subunit regulator), as identified by LC-MS/MS, and controls both spliceosome and ribosome subunit expression levels and function via RpL18, revealing a physical and functional crosstalk between the spliceosome and ribosome.","method":"Liquid chromatography-tandem mass spectrometry (LC-MS/MS) identification of SmD3-interacting proteins; genetic manipulation in Drosophila and in vitro assays in Schneider 2 cells","journal":"FASEB journal","confidence":"Medium","confidence_rationale":"Tier 3 / Weak — MS-based interaction identification, single lab, limited biochemical follow-up reported in abstract","pmids":["30921522"],"is_preprint":false},{"year":2023,"finding":"MYCN directly binds SNRPD3 protein and the protein arginine methyltransferase PRMT5, leading to increased SNRPD3 arginine methylation; this MYCN–SNRPD3–PRMT5 complex maintains a balanced range of alternative splicing (including of cell cycle regulators BIRC5 and CDK10) required for neuroblastoma cell growth.","method":"Co-immunoprecipitation (MYCN–SNRPD3 and SNRPD3–PRMT5 interaction), RNA-seq for splicing analysis, SNRPD3 knockdown/MYCN overexpression functional assays, PRMT5 inhibitor (JNJ-64619178) treatment","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — Co-IP for protein interactions, RNA-seq for splicing readout, pharmacological validation, single lab, multiple orthogonal methods","pmids":["38049564"],"is_preprint":false},{"year":2024,"finding":"The cancer-associated SNRPD3 G96V substitution confers resistance to hypoxia by altering splicing of DNM1L mRNA (encoding DRP1), leading to excessive mitochondrial fragmentation; DRP1 inhibitor Mdivi-1 reverses the fragmentation and attenuates hypoxia resistance in mutant cells.","method":"RNA-seq splicing analysis in wild-type vs. G96V cells under hypoxia; mitochondrial morphology imaging; DRP1 inhibitor (Mdivi-1) treatment assay","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — RNA-seq with functional validation by inhibitor rescue, single lab, single study","pmids":["38241813"],"is_preprint":false},{"year":2024,"finding":"PRMT5 inhibition or knockdown of the PRMT5-SNRP adapter protein pICln causes SNRPD3 protein to be detained on chromatin together with incompletely processed polyadenylated transcripts (GRIPPs), indicating that PRMT5-mediated arginine methylation of Sm proteins including SNRPD3 is required for homeostatic chromatin dissociation and RNA processing completion.","method":"Nascent and total transcriptomics, spike-in controlled fractionated cell transcriptomics, fractionated cell proteomics; PRMT5 inhibition and pICln knockdown; inducible isogenic wild-type and arginine-mutant SNRPB as controls","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal omics methods plus genetic controls, but preprint not yet peer-reviewed","pmids":["bio_10.1101_2024.08.09.607355"],"is_preprint":true},{"year":2021,"finding":"CRISPRi knockdown of SNRPD3 in human tumor cells (A549, U251) induces apoptosis (in murine cells) or senescence/mitotic catastrophe depending on p53 status, and overexpression of SNRPD3 rescues cells from mitotic catastrophe, establishing SNRPD3 as essential for cell viability.","method":"CRISPRi knockdown, inducible shRNA expression, SNRPD3 overexpression rescue experiment in human and murine cell lines","journal":"Molecular therapy. Nucleic acids","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CRISPRi knockdown with defined phenotypic readout and rescue by overexpression, single lab, two orthogonal perturbation methods","pmids":["34703654"],"is_preprint":false},{"year":2026,"finding":"SNRPD3 promotes endometrial cancer cell proliferation, migration, and invasion by preventing intron retention in SREBF1 mRNA; silencing SNRPD3 increases SREBF1 intron retention, and SREBF1 depletion abolishes the proliferative and lipid-metabolic advantage conferred by SNRPD3 overexpression.","method":"SNRPD3 knockdown and overexpression in EC cell lines; RNA-seq/splicing analysis; xenograft and PDX tumor models; ASO-mediated silencing","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RNA-seq splicing analysis, genetic epistasis (SREBF1 rescue), in vivo xenograft and PDX models, single lab","pmids":["41924775"],"is_preprint":false}],"current_model":"SNRPD3 (SmD3) is a core Sm-ring component of the spliceosome whose C-terminal symmetrical dimethylarginine modification (installed by PRMT5) is required for homeostatic chromatin dissociation and productive RNA processing but is dispensable for snRNP assembly and nuclear import; within U1 snRNP, SmD3 residues Glu37/Asp38 contact U1-C/Yhc1 Arg21 to stabilize the U1–5' splice site complex, while its RNA-binding triad acts redundantly with SmB to engage snRNA; SmD3 levels regulate U4/U5 snRNA abundance and thereby control intronic snoRNA biogenesis; in cancer contexts, SNRPD3 forms a complex with MYCN and PRMT5 to maintain balanced alternative splicing of cell-cycle regulators, and a G96V somatic mutation alters DNM1L/DRP1 splicing to drive mitochondrial hyperfragmentation and hypoxia resistance."},"narrative":{"mechanistic_narrative":"SNRPD3 (SmD3) is a core Sm-ring protein of the spliceosome that contributes directly to snRNP function and is essential for cell viability [PMID:25897024, PMID:34703654]. Within U1 snRNP, SmD3 residues Glu37/Asp38 contact the U1-C (Yhc1) residue Arg21 to stabilize the U1 snRNP–5' splice site complex, and its Ser-Asn-Arg RNA-binding triad engages snRNA redundantly with the equivalent triad of SmB, placing SmD3 function at the U1–U2 snRNP interface [PMID:24497193, PMID:25897024]. SmD3 levels regulate the abundance of U4 and U5 snRNAs and thereby control intronic snoRNA biogenesis and intron lariat accumulation while still supporting pre-mRNA splicing [PMID:22869524]. SmD3 carries symmetrical dimethylarginine modifications on its C-terminal arginines; these are dispensable for snRNP assembly and nuclear import [PMID:16236255] but, when blocked by PRMT5 inhibition or loss of the adapter pICln, cause SmD3 to be detained on chromatin together with incompletely processed transcripts, indicating a role in homeostatic chromatin dissociation and RNA-processing completion [PMID:bio_10.1101_2024.08.09.607355]. In cancer, SNRPD3 forms a complex with MYCN and PRMT5 that maintains balanced alternative splicing of cell-cycle regulators required for neuroblastoma growth [PMID:38049564], and a somatic G96V substitution rewires DNM1L/DRP1 splicing to drive mitochondrial hyperfragmentation and hypoxia resistance [PMID:38241813]; SNRPD3 also promotes endometrial cancer progression by preventing SREBF1 intron retention [PMID:41924775].","teleology":[{"year":2004,"claim":"Established that SmD3 carries symmetrical dimethylarginine on specific C-terminal residues and that this modification is clinically relevant as a target of anti-Sm autoantibodies in lupus.","evidence":"Peptide ELISA comparing dimethylated vs. unmodified SmD3 peptides against SLE patient sera","pmids":["15642139"],"confidence":"Medium","gaps":["Antibody-binding assay rather than direct biochemical mapping of the modification","Functional role of the sDMA modification not addressed"]},{"year":2005,"claim":"Resolved whether the C-terminal arginine methylation is needed for the canonical Sm-protein lifecycle, showing it is dispensable for snRNP assembly and nuclear import.","evidence":"Arginine-to-leucine mutagenesis of SmD3 with transient expression and assembly/import readouts","pmids":["16236255"],"confidence":"Medium","gaps":["Did not identify what the modification IS required for","Single lab, single readout system"]},{"year":2012,"claim":"Linked SmD3 dosage to noncoding RNA biogenesis, showing haploinsufficiency selectively reduces U4/U5 snRNAs, snoRNAs, and intron lariats while sparing bulk splicing.","evidence":"Promoter-trap haploinsufficient CHO cells with Northern blot quantification of snRNAs, snoRNAs, and lariats","pmids":["22869524"],"confidence":"Medium","gaps":["Mechanism by which SmD3 dosage selectively limits U4/U5 unclear","Single cell-line model"]},{"year":2014,"claim":"Defined a direct structural role for SmD3 in spliceosome activation by mapping the Glu37/Asp38–Yhc1 Arg21 contact that fortifies the U1–5'SS complex.","evidence":"Structure-guided mutagenesis of yeast SmD3 and Yhc1 with synthetic lethality and prp28 bypass genetic tests","pmids":["24497193"],"confidence":"High","gaps":["Demonstrated in yeast; human U1 interface inferred","Does not address SmD3 contribution beyond U1"]},{"year":2015,"claim":"Established that SmD3's RNA-binding triad engages snRNA redundantly with SmB and that SmD3 function lies at the U1–U2 snRNP interface.","evidence":"Systematic alanine mutagenesis of SmD3 RNA-binding residues with genetic interaction tests against U1/U2 components in yeast","pmids":["25897024"],"confidence":"High","gaps":["Redundancy mapped genetically, not structurally resolved in the assembled spliceosome","Yeast system"]},{"year":2019,"claim":"Uncovered crosstalk between the spliceosome and the ribosome via a physical SmD3–RpL18 interaction controlling both spliceosome and ribosome subunit levels.","evidence":"LC-MS/MS interactome and genetic manipulation in Drosophila and S2 cells","pmids":["30921522"],"confidence":"Medium","gaps":["Limited biochemical follow-up on the interaction","Human relevance not tested"]},{"year":2021,"claim":"Demonstrated that SNRPD3 is essential for tumor cell viability, with p53-dependent senescence/mitotic catastrophe upon knockdown.","evidence":"CRISPRi and inducible shRNA knockdown with overexpression rescue in human and murine cell lines","pmids":["34703654"],"confidence":"Medium","gaps":["Specific splicing targets mediating viability not defined","p53-dependence mechanism not resolved"]},{"year":2023,"claim":"Placed SNRPD3 in an oncogenic MYCN–SNRPD3–PRMT5 complex that tunes alternative splicing of cell-cycle regulators to support neuroblastoma growth.","evidence":"Co-IP of MYCN–SNRPD3 and SNRPD3–PRMT5, RNA-seq splicing analysis, knockdown/overexpression and PRMT5 inhibitor treatment","pmids":["38049564"],"confidence":"Medium","gaps":["Direct vs. bridged nature of MYCN–SNRPD3 binding not dissected","Single tumor type"]},{"year":2024,"claim":"Showed that a somatic SNRPD3 G96V mutation rewires DNM1L/DRP1 splicing to drive mitochondrial fragmentation and hypoxia resistance.","evidence":"RNA-seq splicing analysis in wild-type vs. G96V cells under hypoxia, mitochondrial imaging, and Mdivi-1 rescue","pmids":["38241813"],"confidence":"Medium","gaps":["How a single substitution alters DNM1L splice-site selection mechanistically unknown","Single study"]},{"year":2024,"claim":"Defined the functional requirement for arginine methylation, showing PRMT5/pICln loss detains SNRPD3 on chromatin with unprocessed transcripts, linking the modification to homeostatic chromatin dissociation.","evidence":"Spike-in fractionated transcriptomics and proteomics with PRMT5 inhibition, pICln knockdown, and arginine-mutant Sm controls (preprint)","pmids":["bio_10.1101_2024.08.09.607355"],"confidence":"Medium","gaps":["Preprint, not yet peer-reviewed","Direct measurement on SNRPD3 inferred largely from SNRPB controls"]},{"year":2026,"claim":"Extended SNRPD3's pro-tumorigenic splicing role to endometrial cancer via prevention of SREBF1 intron retention driving lipid metabolism.","evidence":"SNRPD3 knockdown/overexpression with RNA-seq, SREBF1 epistasis, and xenograft/PDX models","pmids":["41924775"],"confidence":"Medium","gaps":["How SNRPD3 selectively controls SREBF1 intron retention not defined","Generality across cancers unclear"]},{"year":null,"claim":"It remains unresolved how SNRPD3's general Sm-ring function is reconciled with its selective control of specific splicing events (DNM1L, SREBF1, BIRC5/CDK10) that drive distinct cancer phenotypes.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model linking SmD3 to selective intron retention/exon choice","Mechanism connecting arginine methylation status to transcript-specific outcomes unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[3,4]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[3,4]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,8]},{"term_id":"GO:0005694","term_label":"chromosome","supporting_discovery_ids":[8]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[2,3,4]},{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[6,10]}],"complexes":["Sm core ring","U1 snRNP","MYCN-SNRPD3-PRMT5 complex"],"partners":["SNRPB","SNRPC","PRMT5","MYCN","CLNS1A","RPL18"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P62318","full_name":"Small nuclear ribonucleoprotein Sm D3","aliases":["snRNP core protein D3"],"length_aa":126,"mass_kda":13.9,"function":"Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (By similarity)","subcellular_location":"Cytoplasm, cytosol; Nucleus","url":"https://www.uniprot.org/uniprotkb/P62318/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/SNRPD3","classification":"Common Essential","n_dependent_lines":383,"n_total_lines":383,"dependency_fraction":1.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"SNRPA","stoichiometry":10.0},{"gene":"SNRPB","stoichiometry":10.0},{"gene":"SNRPC","stoichiometry":10.0},{"gene":"SNRPF","stoichiometry":10.0},{"gene":"CLNS1A","stoichiometry":4.0},{"gene":"RBM39","stoichiometry":4.0},{"gene":"SNRPD2","stoichiometry":4.0},{"gene":"CAPZB","stoichiometry":0.2},{"gene":"CPSF6","stoichiometry":0.2},{"gene":"RBM42","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/SNRPD3","total_profiled":1310},"omim":[{"mim_id":"617909","title":"LSM10, U7 SMALL NUCLEAR RNA-ASSOCIATED PROTEIN; LSM10","url":"https://www.omim.org/entry/617909"},{"mim_id":"616587","title":"SIR2 ANTIPHAGE-LIKE PROTEIN 1; SIRAL1","url":"https://www.omim.org/entry/616587"},{"mim_id":"611734","title":"WD REPEAT-CONTAINING PROTEIN 77; WDR77","url":"https://www.omim.org/entry/611734"},{"mim_id":"603542","title":"SMALL NUCLEAR RIBONUCLEOPROTEIN POLYPEPTIDE G; SNRPG","url":"https://www.omim.org/entry/603542"},{"mim_id":"603541","title":"SMALL NUCLEAR RIBONUCLEOPROTEIN POLYPEPTIDE F; SNRPF","url":"https://www.omim.org/entry/603541"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Nuclear bodies","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/SNRPD3"},"hgnc":{"alias_symbol":["SMD3","Sm-D3"],"prev_symbol":[]},"alphafold":{"accession":"P62318","domains":[{"cath_id":"2.30.30.100","chopping":"4-88","consensus_level":"high","plddt":94.656,"start":4,"end":88}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P62318","model_url":"https://alphafold.ebi.ac.uk/files/AF-P62318-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P62318-F1-predicted_aligned_error_v6.png","plddt_mean":82.81},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SNRPD3","jax_strain_url":"https://www.jax.org/strain/search?query=SNRPD3"},"sequence":{"accession":"P62318","fasta_url":"https://rest.uniprot.org/uniprotkb/P62318.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P62318/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P62318"}},"corpus_meta":[{"pmid":"15642139","id":"PMC_15642139","title":"Identification of a SmD3 epitope with a single symmetrical dimethylation of an arginine residue as a specific target of a subpopulation of anti-Sm antibodies.","date":"2004","source":"Arthritis research & therapy","url":"https://pubmed.ncbi.nlm.nih.gov/15642139","citation_count":59,"is_preprint":false},{"pmid":"9488472","id":"PMC_9488472","title":"The Drosophila gene for antizyme requires ribosomal frameshifting for expression and contains an intronic gene for snRNP Sm D3 on the opposite strand.","date":"1998","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/9488472","citation_count":34,"is_preprint":false},{"pmid":"15642993","id":"PMC_15642993","title":"Improved serological differentiation between systemic lupus erythematosus and mixed connective tissue disease by use of an SmD3 peptide-based immunoassay.","date":"2005","source":"Clinical and diagnostic laboratory immunology","url":"https://pubmed.ncbi.nlm.nih.gov/15642993","citation_count":22,"is_preprint":false},{"pmid":"24497193","id":"PMC_24497193","title":"Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28.","date":"2014","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/24497193","citation_count":20,"is_preprint":false},{"pmid":"22869524","id":"PMC_22869524","title":"SmD3 regulates intronic noncoding RNA biogenesis.","date":"2012","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/22869524","citation_count":18,"is_preprint":false},{"pmid":"30921522","id":"PMC_30921522","title":"Small ribonucleoprotein particle protein SmD3 governs the homeostasis of germline stem cells and the crosstalk between the spliceosome and ribosome signals in Drosophila.","date":"2019","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/30921522","citation_count":18,"is_preprint":false},{"pmid":"25897024","id":"PMC_25897024","title":"Structure-function analysis and genetic interactions of the Yhc1, SmD3, SmB, and Snp1 subunits of yeast U1 snRNP and genetic interactions of SmD3 with U2 snRNP subunit Lea1.","date":"2015","source":"RNA (New York, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/25897024","citation_count":17,"is_preprint":false},{"pmid":"34925413","id":"PMC_34925413","title":"Arabidopsi s Spliceosome Factor SmD3 Modulates Immunity to Pseudomonas syringae Infection.","date":"2021","source":"Frontiers in plant science","url":"https://pubmed.ncbi.nlm.nih.gov/34925413","citation_count":14,"is_preprint":false},{"pmid":"38049564","id":"PMC_38049564","title":"MYCN and SNRPD3 cooperate to maintain a balance of alternative splicing events that drives neuroblastoma progression.","date":"2023","source":"Oncogene","url":"https://pubmed.ncbi.nlm.nih.gov/38049564","citation_count":10,"is_preprint":false},{"pmid":"12072471","id":"PMC_12072471","title":"P elements inserted in the vicinity of or within the Drosophila snRNP SmD3 gene nested in the first intron of the Ornithine Decarboxylase Antizyme gene affect only the expression of SmD3.","date":"2002","source":"Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/12072471","citation_count":10,"is_preprint":false},{"pmid":"34703654","id":"PMC_34703654","title":"Non-targeting control for MISSION shRNA library silences SNRPD3 leading to cell death or permanent growth arrest.","date":"2021","source":"Molecular therapy. Nucleic acids","url":"https://pubmed.ncbi.nlm.nih.gov/34703654","citation_count":9,"is_preprint":false},{"pmid":"16236255","id":"PMC_16236255","title":"The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport.","date":"2005","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/16236255","citation_count":6,"is_preprint":false},{"pmid":"38241813","id":"PMC_38241813","title":"Cancer-associated SNRPD3 mutation confers resistance to hypoxia, which is attenuated by DRP1 inhibition.","date":"2024","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/38241813","citation_count":2,"is_preprint":false},{"pmid":"41924775","id":"PMC_41924775","title":"SNRPD3 promotes endometrial cancer progression via regulating SREBF1 intron retention.","date":"2026","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/41924775","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.09.25.678492","title":"Symmetrical Dimethylarginine as the Central Antigenic Determinant of Anti-Smith Autoantibodies in Systemic Lupus Erythematosus","date":"2025-09-28","source":"bioRxiv","url":"https://doi.org/10.1101/2025.09.25.678492","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.08.09.607355","title":"Productive mRNA Chromatin Escape is Promoted by PRMT5 Methylation of SNRPB","date":"2024-08-10","source":"bioRxiv","url":"https://doi.org/10.1101/2024.08.09.607355","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.08.23.609445","title":"Recontextualizing Eukaryogenesis via Computational Analysis of RNA Processing in 16,449 Archaeal Genomes","date":"2024-08-24","source":"bioRxiv","url":"https://doi.org/10.1101/2024.08.23.609445","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":11428,"output_tokens":3060,"usd":0.040092,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10446,"output_tokens":3718,"usd":0.07259,"stage2_stop_reason":"end_turn"},"total_usd":0.112682,"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\": 2005,\n      \"finding\": \"Symmetrical dimethylarginine (sDMA) post-translational modification of SmD3 C-terminal arginines is NOT required for snRNP assembly or nuclear transport; mutating the modified arginines to leucines in SmD3 did not interfere with assembly or nuclear import of the transiently expressed variant.\",\n      \"method\": \"Site-directed mutagenesis (arginine-to-leucine substitutions) of SmD3, transient expression, and assessment of snRNP assembly and nuclear transport\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean mutagenesis with cellular localization/assembly readout, single lab, single study\",\n      \"pmids\": [\"16236255\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"SmD3 carries symmetrical dimethylarginine at specific C-terminal residues (including position 112), and this modification is an essential component of a major autoepitope recognized by a subpopulation of anti-Sm antibodies in SLE patients.\",\n      \"method\": \"Immobilized synthetic peptide ELISA using dimethylated vs. unmodified SmD3 peptides to map autoantibody reactivity\",\n      \"journal\": \"Arthritis research & therapy\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — peptide-based ELISA, replicated across multiple SLE cohorts, but indirect (antibody-binding assay, not biochemical modification mapping)\",\n      \"pmids\": [\"15642139\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Haploinsufficiency of SmD3 (one allele disrupted by proviral insertion) reduces snRNA U4 and U5 levels, decreases snoRNA expression and snoRNA-containing intron lariat abundance, implicating SmD3 as a critical regulator of intronic noncoding RNA biogenesis upstream of metabolic stress response pathways, while still supporting pre-mRNA splicing.\",\n      \"method\": \"Retroviral promoter trap mutagenesis to generate SmD3 haploinsufficient CHO cell lines; Northern blot and quantitative analysis of snRNAs, snoRNAs, and intron lariats\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — defined genetic model (haploinsufficiency), multiple RNA readouts, single lab\",\n      \"pmids\": [\"22869524\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Yeast SmD3 residues Glu37/Asp38 contact Yhc1 (yeast U1-C) Arg21 to fortify the U1 snRNP–5' splice site complex; mutations at this interface synergize with mud2Δ and bypass the essential DEAD-box ATPase Prp28, consistent with destabilization of U1•5'SS interaction.\",\n      \"method\": \"Structure-guided mutagenesis of yeast SmD3 and Yhc1 combined with genetic interaction (synthetic lethality/suppression) assays in yeast\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — structure-guided mutagenesis plus multiple orthogonal genetic epistasis tests (synthetic lethality, suppression of prp28Δ), single lab but rigorous\",\n      \"pmids\": [\"24497193\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"The RNA-binding triad of SmD3 (Ser-Asn-Arg) participates in snRNA binding with built-in redundancy with SmB's triad; simultaneous mutation of Asn or Arg in both SmD3 and SmB is lethal. SmD3 C-terminal truncations and RNA-site mutations are lethal in cells lacking U2 snRNP subunit Lea1, placing SmD3 function at the U1–U2 snRNP interface.\",\n      \"method\": \"Systematic alanine mutagenesis of SmD3 RNA-binding residues combined with synthetic lethality/genetic interaction assays (mud2Δ, lea1Δ, mud1Δ, nam8Δ) in yeast\",\n      \"journal\": \"RNA (New York, N.Y.)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — systematic mutagenesis plus multiple orthogonal genetic epistasis tests across U1 and U2 snRNP components, single lab\",\n      \"pmids\": [\"25897024\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Drosophila SmD3 binds ribosomal protein RpL18 (a large ribosome subunit regulator), as identified by LC-MS/MS, and controls both spliceosome and ribosome subunit expression levels and function via RpL18, revealing a physical and functional crosstalk between the spliceosome and ribosome.\",\n      \"method\": \"Liquid chromatography-tandem mass spectrometry (LC-MS/MS) identification of SmD3-interacting proteins; genetic manipulation in Drosophila and in vitro assays in Schneider 2 cells\",\n      \"journal\": \"FASEB journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Weak — MS-based interaction identification, single lab, limited biochemical follow-up reported in abstract\",\n      \"pmids\": [\"30921522\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"MYCN directly binds SNRPD3 protein and the protein arginine methyltransferase PRMT5, leading to increased SNRPD3 arginine methylation; this MYCN–SNRPD3–PRMT5 complex maintains a balanced range of alternative splicing (including of cell cycle regulators BIRC5 and CDK10) required for neuroblastoma cell growth.\",\n      \"method\": \"Co-immunoprecipitation (MYCN–SNRPD3 and SNRPD3–PRMT5 interaction), RNA-seq for splicing analysis, SNRPD3 knockdown/MYCN overexpression functional assays, PRMT5 inhibitor (JNJ-64619178) treatment\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — Co-IP for protein interactions, RNA-seq for splicing readout, pharmacological validation, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"38049564\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The cancer-associated SNRPD3 G96V substitution confers resistance to hypoxia by altering splicing of DNM1L mRNA (encoding DRP1), leading to excessive mitochondrial fragmentation; DRP1 inhibitor Mdivi-1 reverses the fragmentation and attenuates hypoxia resistance in mutant cells.\",\n      \"method\": \"RNA-seq splicing analysis in wild-type vs. G96V cells under hypoxia; mitochondrial morphology imaging; DRP1 inhibitor (Mdivi-1) treatment assay\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — RNA-seq with functional validation by inhibitor rescue, single lab, single study\",\n      \"pmids\": [\"38241813\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PRMT5 inhibition or knockdown of the PRMT5-SNRP adapter protein pICln causes SNRPD3 protein to be detained on chromatin together with incompletely processed polyadenylated transcripts (GRIPPs), indicating that PRMT5-mediated arginine methylation of Sm proteins including SNRPD3 is required for homeostatic chromatin dissociation and RNA processing completion.\",\n      \"method\": \"Nascent and total transcriptomics, spike-in controlled fractionated cell transcriptomics, fractionated cell proteomics; PRMT5 inhibition and pICln knockdown; inducible isogenic wild-type and arginine-mutant SNRPB as controls\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal omics methods plus genetic controls, but preprint not yet peer-reviewed\",\n      \"pmids\": [\"bio_10.1101_2024.08.09.607355\"],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"CRISPRi knockdown of SNRPD3 in human tumor cells (A549, U251) induces apoptosis (in murine cells) or senescence/mitotic catastrophe depending on p53 status, and overexpression of SNRPD3 rescues cells from mitotic catastrophe, establishing SNRPD3 as essential for cell viability.\",\n      \"method\": \"CRISPRi knockdown, inducible shRNA expression, SNRPD3 overexpression rescue experiment in human and murine cell lines\",\n      \"journal\": \"Molecular therapy. Nucleic acids\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPRi knockdown with defined phenotypic readout and rescue by overexpression, single lab, two orthogonal perturbation methods\",\n      \"pmids\": [\"34703654\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"SNRPD3 promotes endometrial cancer cell proliferation, migration, and invasion by preventing intron retention in SREBF1 mRNA; silencing SNRPD3 increases SREBF1 intron retention, and SREBF1 depletion abolishes the proliferative and lipid-metabolic advantage conferred by SNRPD3 overexpression.\",\n      \"method\": \"SNRPD3 knockdown and overexpression in EC cell lines; RNA-seq/splicing analysis; xenograft and PDX tumor models; ASO-mediated silencing\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RNA-seq splicing analysis, genetic epistasis (SREBF1 rescue), in vivo xenograft and PDX models, single lab\",\n      \"pmids\": [\"41924775\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SNRPD3 (SmD3) is a core Sm-ring component of the spliceosome whose C-terminal symmetrical dimethylarginine modification (installed by PRMT5) is required for homeostatic chromatin dissociation and productive RNA processing but is dispensable for snRNP assembly and nuclear import; within U1 snRNP, SmD3 residues Glu37/Asp38 contact U1-C/Yhc1 Arg21 to stabilize the U1–5' splice site complex, while its RNA-binding triad acts redundantly with SmB to engage snRNA; SmD3 levels regulate U4/U5 snRNA abundance and thereby control intronic snoRNA biogenesis; in cancer contexts, SNRPD3 forms a complex with MYCN and PRMT5 to maintain balanced alternative splicing of cell-cycle regulators, and a G96V somatic mutation alters DNM1L/DRP1 splicing to drive mitochondrial hyperfragmentation and hypoxia resistance.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SNRPD3 (SmD3) is a core Sm-ring protein of the spliceosome that contributes directly to snRNP function and is essential for cell viability [#4, #9]. Within U1 snRNP, SmD3 residues Glu37/Asp38 contact the U1-C (Yhc1) residue Arg21 to stabilize the U1 snRNP–5' splice site complex, and its Ser-Asn-Arg RNA-binding triad engages snRNA redundantly with the equivalent triad of SmB, placing SmD3 function at the U1–U2 snRNP interface [#3, #4]. SmD3 levels regulate the abundance of U4 and U5 snRNAs and thereby control intronic snoRNA biogenesis and intron lariat accumulation while still supporting pre-mRNA splicing [#2]. SmD3 carries symmetrical dimethylarginine modifications on its C-terminal arginines; these are dispensable for snRNP assembly and nuclear import [#0] but, when blocked by PRMT5 inhibition or loss of the adapter pICln, cause SmD3 to be detained on chromatin together with incompletely processed transcripts, indicating a role in homeostatic chromatin dissociation and RNA-processing completion [#8]. In cancer, SNRPD3 forms a complex with MYCN and PRMT5 that maintains balanced alternative splicing of cell-cycle regulators required for neuroblastoma growth [#6], and a somatic G96V substitution rewires DNM1L/DRP1 splicing to drive mitochondrial hyperfragmentation and hypoxia resistance [#7]; SNRPD3 also promotes endometrial cancer progression by preventing SREBF1 intron retention [#10].\",\n  \"teleology\": [\n    {\n      \"year\": 2004,\n      \"claim\": \"Established that SmD3 carries symmetrical dimethylarginine on specific C-terminal residues and that this modification is clinically relevant as a target of anti-Sm autoantibodies in lupus.\",\n      \"evidence\": \"Peptide ELISA comparing dimethylated vs. unmodified SmD3 peptides against SLE patient sera\",\n      \"pmids\": [\"15642139\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Antibody-binding assay rather than direct biochemical mapping of the modification\", \"Functional role of the sDMA modification not addressed\"]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"Resolved whether the C-terminal arginine methylation is needed for the canonical Sm-protein lifecycle, showing it is dispensable for snRNP assembly and nuclear import.\",\n      \"evidence\": \"Arginine-to-leucine mutagenesis of SmD3 with transient expression and assembly/import readouts\",\n      \"pmids\": [\"16236255\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Did not identify what the modification IS required for\", \"Single lab, single readout system\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Linked SmD3 dosage to noncoding RNA biogenesis, showing haploinsufficiency selectively reduces U4/U5 snRNAs, snoRNAs, and intron lariats while sparing bulk splicing.\",\n      \"evidence\": \"Promoter-trap haploinsufficient CHO cells with Northern blot quantification of snRNAs, snoRNAs, and lariats\",\n      \"pmids\": [\"22869524\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Mechanism by which SmD3 dosage selectively limits U4/U5 unclear\", \"Single cell-line model\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Defined a direct structural role for SmD3 in spliceosome activation by mapping the Glu37/Asp38–Yhc1 Arg21 contact that fortifies the U1–5'SS complex.\",\n      \"evidence\": \"Structure-guided mutagenesis of yeast SmD3 and Yhc1 with synthetic lethality and prp28 bypass genetic tests\",\n      \"pmids\": [\"24497193\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Demonstrated in yeast; human U1 interface inferred\", \"Does not address SmD3 contribution beyond U1\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Established that SmD3's RNA-binding triad engages snRNA redundantly with SmB and that SmD3 function lies at the U1–U2 snRNP interface.\",\n      \"evidence\": \"Systematic alanine mutagenesis of SmD3 RNA-binding residues with genetic interaction tests against U1/U2 components in yeast\",\n      \"pmids\": [\"25897024\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Redundancy mapped genetically, not structurally resolved in the assembled spliceosome\", \"Yeast system\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Uncovered crosstalk between the spliceosome and the ribosome via a physical SmD3–RpL18 interaction controlling both spliceosome and ribosome subunit levels.\",\n      \"evidence\": \"LC-MS/MS interactome and genetic manipulation in Drosophila and S2 cells\",\n      \"pmids\": [\"30921522\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Limited biochemical follow-up on the interaction\", \"Human relevance not tested\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Demonstrated that SNRPD3 is essential for tumor cell viability, with p53-dependent senescence/mitotic catastrophe upon knockdown.\",\n      \"evidence\": \"CRISPRi and inducible shRNA knockdown with overexpression rescue in human and murine cell lines\",\n      \"pmids\": [\"34703654\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Specific splicing targets mediating viability not defined\", \"p53-dependence mechanism not resolved\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Placed SNRPD3 in an oncogenic MYCN–SNRPD3–PRMT5 complex that tunes alternative splicing of cell-cycle regulators to support neuroblastoma growth.\",\n      \"evidence\": \"Co-IP of MYCN–SNRPD3 and SNRPD3–PRMT5, RNA-seq splicing analysis, knockdown/overexpression and PRMT5 inhibitor treatment\",\n      \"pmids\": [\"38049564\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Direct vs. bridged nature of MYCN–SNRPD3 binding not dissected\", \"Single tumor type\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Showed that a somatic SNRPD3 G96V mutation rewires DNM1L/DRP1 splicing to drive mitochondrial fragmentation and hypoxia resistance.\",\n      \"evidence\": \"RNA-seq splicing analysis in wild-type vs. G96V cells under hypoxia, mitochondrial imaging, and Mdivi-1 rescue\",\n      \"pmids\": [\"38241813\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"How a single substitution alters DNM1L splice-site selection mechanistically unknown\", \"Single study\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Defined the functional requirement for arginine methylation, showing PRMT5/pICln loss detains SNRPD3 on chromatin with unprocessed transcripts, linking the modification to homeostatic chromatin dissociation.\",\n      \"evidence\": \"Spike-in fractionated transcriptomics and proteomics with PRMT5 inhibition, pICln knockdown, and arginine-mutant Sm controls (preprint)\",\n      \"pmids\": [\"bio_10.1101_2024.08.09.607355\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Preprint, not yet peer-reviewed\", \"Direct measurement on SNRPD3 inferred largely from SNRPB controls\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Extended SNRPD3's pro-tumorigenic splicing role to endometrial cancer via prevention of SREBF1 intron retention driving lipid metabolism.\",\n      \"evidence\": \"SNRPD3 knockdown/overexpression with RNA-seq, SREBF1 epistasis, and xenograft/PDX models\",\n      \"pmids\": [\"41924775\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"How SNRPD3 selectively controls SREBF1 intron retention not defined\", \"Generality across cancers unclear\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unresolved how SNRPD3's general Sm-ring function is reconciled with its selective control of specific splicing events (DNM1L, SREBF1, BIRC5/CDK10) that drive distinct cancer phenotypes.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"No structural model linking SmD3 to selective intron retention/exon choice\", \"Mechanism connecting arginine methylation status to transcript-specific outcomes unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [3, 4]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [3, 4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 8]},\n      {\"term_id\": \"GO:0005694\", \"supporting_discovery_ids\": [8]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [2, 3, 4]},\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [6, 10]}\n    ],\n    \"complexes\": [\"Sm core ring\", \"U1 snRNP\", \"MYCN-SNRPD3-PRMT5 complex\"],\n    \"partners\": [\"SNRPB\", \"SNRPC\", \"PRMT5\", \"MYCN\", \"CLNS1A\", \"RPL18\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}