{"gene":"RBM7","run_date":"2026-06-10T06:43:36","timeline":{"discoveries":[{"year":2015,"finding":"The RRM domain of RBM7 mediates U-rich pyrimidine RNA sequence binding within the NEXT complex; two critical phenylalanine residues in the RRM are required for RNA interaction and for NEXT complex association with snRNAs in vivo. RBM7/NEXT depletion causes accumulation of mature and 3'-end extended forms of snRNAs, implicating NEXT in snRNA surveillance/snRNP biogenesis.","method":"Crystal structure of RBM7 RRM; site-directed mutagenesis of phenylalanine residues; RNA-binding assays; RIP; depletion experiments with RNA-seq readout","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure combined with mutagenesis and in vivo RIP validating RNA-binding mechanism, single lab but multiple orthogonal methods","pmids":["25852104"],"is_preprint":false},{"year":2016,"finding":"A proline-rich segment of ZCCHC8 is the direct interaction site for the RRM of RBM7, incorporating RBM7 into the NEXT complex. The same RRM of RBM7 can also bind a structurally similar proline-rich segment of the splicing factor SAP145, suggesting dual interactions linking the exosome to the spliceosome.","method":"Crystal structure of RBM7 RRM–ZCCHC8 proline-rich segment complex at 2.0 Å; biochemical binding assays; sequence/structural comparison with SAP145","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Moderate — high-resolution crystal structure plus biochemical validation of binding interfaces, single lab with multiple orthogonal methods","pmids":["27905398"],"is_preprint":false},{"year":2014,"finding":"RBM7 is phosphorylated by the p38MAPK/MK2 axis at serine 136 (S136). This phosphorylation strongly decreases RBM7's RNA-binding capacity. Inhibition of p38MAPK or the S136A mutation increases RBM7–RNA association. Phosphorylation of RBM7 during stress increases stability of PROMPTs (e.g., proRBM39, proEXT1, proDNAJB4) without changing their transcription rate, indicating that p38MAPK/MK2 modulates the noncoding transcriptome by blocking RBM7-mediated exosome targeting.","method":"In vitro kinase assay; phospho-site mapping (S136); RNA-binding assays with RBM7-S136A mutant; RNAPII ChIP; PROMPT stability measurements; overexpression of phospho-mutant","journal":"RNA (New York, N.Y.)","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — in vitro kinase assay identifying the site plus mutagenesis rescue and functional RNA-binding readout, single lab with multiple orthogonal methods","pmids":["25525152"],"is_preprint":false},{"year":2019,"finding":"Following genotoxic stress, p38MAPK activation triggers enhanced binding of RBM7 to core subunits of the 7SK snRNP, releasing P-TEFb from the inhibitory 7SK snRNP complex. Released P-TEFb relocates to chromatin to promote RNA Pol II pause release, driving transcription of short DDR genes and non-coding RNAs. Disruption of the RBM7–P-TEFb axis causes hypersensitivity to DNA-damaging agents via apoptosis.","method":"Co-immunoprecipitation of RBM7 with 7SK snRNP components; chromatin fractionation of P-TEFb; RNA Pol II ChIP; 4sU-seq; loss-of-function with apoptosis readout; genotoxic stress treatments","journal":"Molecular cell","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP, chromatin fractionation, Pol II ChIP, and functional rescue in a single focused study","pmids":["30824372"],"is_preprint":false},{"year":2016,"finding":"Crystal structure of the isolated RRM domain of human RBM7 was determined at 2.5 Å resolution, revealing a ring-shaped pentameric assembly (attributed to crystal packing). The structure required molecular replacement using RBM8 and CBP20 RRM structures as search models.","method":"X-ray crystallography at 2.5 Å; molecular replacement","journal":"Acta crystallographica. Section F, Structural biology communications","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution crystal structure but reported without functional validation; single paper, structural data only","pmids":["27139832"],"is_preprint":false},{"year":2020,"finding":"RBM7 binds noncoding RNAs that form subnuclear bodies including NEAT1 speckles. Dysregulated (elevated) RBM7 expression leads to nuclear degradation of NEAT1 speckles, dispersion of the DNA repair protein BRCA1, and triggering of apoptosis in lung epithelial cells, which then produce CXCL12 to recruit pro-fibrotic SatMs.","method":"Rbm7 conditional knockout mouse (bleomycin fibrosis model); RNA immunoprecipitation for NEAT1 binding; immunofluorescence for BRCA1 dispersion; apoptosis assays; CXCL12 measurement","journal":"Immunity","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo KO with defined cellular phenotype and RIP for binding, but mechanistic steps (NEAT1 → BRCA1 dispersion → apoptosis) rely partly on correlative evidence within a single study","pmids":["32187520"],"is_preprint":false},{"year":2020,"finding":"RBM7 directly binds AU-rich elements (AREs) in the 3'-UTR of CDK1 mRNA, stabilizing it and lengthening its half-life. This stabilization promotes breast cancer cell proliferation and G1-S progression; CDK1 overexpression rescues the proliferative defect caused by RBM7 knockdown, whereas a mutant CDK1 unable to bind AREs does not.","method":"RIP assay; mRNA half-life assay (actinomycin D); RBM7 knockdown/overexpression with CDK1 rescue; in vitro and in vivo (xenograft) proliferation assays","journal":"NPJ breast cancer","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — RIP plus mRNA stability assay plus genetic rescue, single lab, multiple methods but no in vitro reconstitution","pmids":["33145401"],"is_preprint":false},{"year":2024,"finding":"RBM7 controls the alternative splicing of MFGE8, promoting inclusion of exon 7 to produce the long isoform MFGE8-L over the truncated isoform MFGE8-S. MFGE8-L attenuates STAT1 phosphorylation and alters cell adhesion molecules to inhibit breast cancer migration and invasion, whereas MFGE8-S (lacking the second F5/8 type C domain) has the opposite effect. RBM7 also negatively regulates the NF-κB cascade; RBM7 silencing enhances HUVEC tube formation that is blocked by an NF-κB inhibitor.","method":"RBM7 knockdown/overexpression; RT-PCR splicing assays; lung metastasis mouse model; STAT1 phosphorylation Western blot; NF-κB pathway analysis; HUVEC tube formation assay","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — multiple functional assays (splicing, signaling, in vivo metastasis) in single lab; mechanism of splicing regulation by RBM7 not biochemically reconstituted","pmids":["38995840"],"is_preprint":false},{"year":2025,"finding":"RBM7 directly interacts with FBXL16 mRNA and destabilizes it, reducing FBXL16 protein levels. This suppresses mitochondrial dysfunction and ferroptosis in TMZ-resistant glioblastoma cells. FBXL16 knockdown reverses ferroptosis and chemosensitivity induced by RBM7 loss, placing RBM7 upstream of FBXL16 in a resistance pathway.","method":"Co-immunoprecipitation; RNA immunoprecipitation; actinomycin D mRNA stability assay; RBM7 knockdown with ferroptosis/mitochondrial readouts; xenograft model","journal":"Molecular genetics and genomics : MGG","confidence":"Medium","confidence_rationale":"Tier 3 / Weak — RIP and mRNA stability assay support direct binding, single lab, no in vitro reconstitution of destabilization mechanism","pmids":["41381783"],"is_preprint":false},{"year":2016,"finding":"A homozygous loss-of-function mutation in RBM7 in a patient with SMA-like motor neuropathy causes altered RNA metabolism in primary fibroblasts. Knockdown of rbm7 in zebrafish produces motor neuron and cerebellar defects, overlapping with those seen for exosc8/exosc3 knockdown, placing RBM7 in the same essential RNA-processing pathway required for neuronal differentiation.","method":"Patient fibroblast RNA-seq; zebrafish rbm7 morpholino knockdown with motor neuron/cerebellar phenotype readout; genetic epistasis comparison with exosc8/exosc3","journal":"Human molecular genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo loss-of-function in zebrafish with defined neuronal phenotype plus patient RNA-seq, but mechanism is inferred from pathway overlap rather than direct biochemical dissection","pmids":["27193168"],"is_preprint":false}],"current_model":"RBM7 is an RNA-recognition motif (RRM)-containing subunit of the nuclear exosome targeting (NEXT) complex that binds U-rich/AU-rich RNA sequences and directs non-coding RNAs (PROMPTs, snRNAs, NEAT1) to the nuclear exosome for degradation; its RNA-binding activity is negatively regulated by p38MAPK/MK2-mediated phosphorylation at S136, and during genotoxic stress RBM7 additionally activates P-TEFb by displacing it from the inhibitory 7SK snRNP to promote RNA Pol II pause release and a pro-survival transcriptional response, while also stabilizing select mRNAs (CDK1, FBXL16) and controlling alternative splicing (MFGE8) to influence cell proliferation, ferroptosis, and cancer metastasis."},"narrative":{"mechanistic_narrative":"RBM7 is an RNA-recognition motif (RRM)-containing subunit of the nuclear exosome targeting (NEXT) complex that recognizes U-rich pyrimidine and AU-rich RNA sequences and directs non-coding and structured RNAs toward the nuclear exosome for surveillance and degradation [PMID:25852104]. Its RRM both binds RNA—through two critical phenylalanine residues—and tethers RBM7 into NEXT by docking onto a proline-rich segment of ZCCHC8, with the same surface able to engage a structurally similar segment of the splicing factor SAP145, linking exosome targeting to the spliceosome [PMID:25852104, PMID:27905398]. Through this activity RBM7/NEXT carries out snRNA 3'-end surveillance and degradation of PROMPTs [PMID:25852104, PMID:25525152]. RBM7's RNA-binding output is gated by stress signaling: p38MAPK/MK2 phosphorylates RBM7 at S136, reducing RNA association and consequently stabilizing PROMPTs without altering their transcription [PMID:25525152]; under genotoxic stress p38MAPK activation additionally redirects RBM7 to the 7SK snRNP, where it displaces and activates P-TEFb to promote RNA Pol II pause release and a pro-survival DNA-damage transcriptional program [PMID:30824372]. Beyond non-coding RNA turnover, RBM7 shapes specific protein-coding outputs—stabilizing CDK1 mRNA via 3'-UTR AU-rich elements to drive cell-cycle progression [PMID:33145401], destabilizing FBXL16 mRNA to suppress ferroptosis [PMID:41381783], and controlling MFGE8 alternative splicing to restrain migration and invasion [PMID:38995840]—thereby influencing proliferation, cancer metastasis, and chemoresistance. A homozygous loss-of-function RBM7 mutation underlies an SMA-like motor neuropathy, with patient and zebrafish phenotypes placing RBM7 in the same essential RNA-processing pathway as exosome core subunits [PMID:27193168].","teleology":[{"year":2014,"claim":"Established that RBM7's central RNA-binding activity is a regulated node, by showing that stress-activated p38MAPK/MK2 phosphorylates RBM7 at S136 to switch off exosome targeting of non-coding RNAs.","evidence":"In vitro kinase assay, S136 phospho-site mapping, S136A mutant RNA-binding assays, and PROMPT stability measurements","pmids":["25525152"],"confidence":"High","gaps":["Does not resolve how phosphorylation structurally disrupts the RRM-RNA interface","Scope of the phospho-regulated noncoding transcriptome beyond tested PROMPTs not defined"]},{"year":2015,"claim":"Defined the molecular basis of RBM7 RNA recognition, showing the RRM binds U-rich pyrimidine sequences via two phenylalanines and that this activity underlies NEXT-mediated snRNA surveillance.","evidence":"Crystal structure of RBM7 RRM, phenylalanine mutagenesis, RNA-binding assays, RIP, and depletion with RNA-seq","pmids":["25852104"],"confidence":"High","gaps":["Structure of RRM bound to RNA not solved","Full set of physiological RNA targets of NEXT not enumerated"]},{"year":2016,"claim":"Showed how RBM7 is physically incorporated into NEXT and revealed a potential exosome-spliceosome link, by mapping the RRM to a proline-rich segment of ZCCHC8 and a similar segment of SAP145.","evidence":"2.0 Å crystal structure of RBM7 RRM–ZCCHC8 complex with biochemical binding assays and structural comparison","pmids":["27905398"],"confidence":"High","gaps":["Functional consequence of the RBM7-SAP145 interaction in vivo not established","Whether RNA binding and ZCCHC8 binding are mutually exclusive not resolved"]},{"year":2016,"claim":"Provided an additional structural view of the isolated RBM7 RRM, but without functional consequence beyond the existing model.","evidence":"X-ray crystallography at 2.5 Å with molecular replacement","pmids":["27139832"],"confidence":"Medium","gaps":["Pentameric assembly attributed to crystal packing, not biologically validated","No functional validation accompanying the structure"]},{"year":2016,"claim":"Connected RBM7 to human disease and confirmed its essential role in RNA processing, by linking a homozygous loss-of-function mutation to motor neuropathy and recapitulating neuronal defects in zebrafish overlapping exosome-subunit phenotypes.","evidence":"Patient fibroblast RNA-seq, zebrafish morpholino knockdown with neuronal phenotype, and epistasis with exosc8/exosc3","pmids":["27193168"],"confidence":"Medium","gaps":["Disease mechanism inferred from pathway overlap rather than direct biochemical dissection","Single patient; allelic spectrum not defined"]},{"year":2019,"claim":"Revealed a moonlighting function distinct from RNA degradation, showing that genotoxic stress redirects RBM7 to the 7SK snRNP to release and activate P-TEFb, driving Pol II pause release and a pro-survival response.","evidence":"Reciprocal Co-IP with 7SK snRNP, chromatin fractionation of P-TEFb, Pol II ChIP, 4sU-seq, and loss-of-function apoptosis readout","pmids":["30824372"],"confidence":"High","gaps":["How phosphorylation state of RBM7 coordinates NEXT versus 7SK engagement not resolved","Direct binding partner within 7SK snRNP for RBM7 not pinpointed structurally"]},{"year":2020,"claim":"Extended RBM7 function to subnuclear body homeostasis, showing it binds NEAT1 and that elevated RBM7 degrades NEAT1 speckles, disperses BRCA1, and drives apoptosis with downstream pro-fibrotic signaling.","evidence":"Rbm7 conditional knockout mouse bleomycin model, RIP for NEAT1, BRCA1 immunofluorescence, apoptosis assays, and CXCL12 measurement","pmids":["32187520"],"confidence":"Medium","gaps":["NEAT1→BRCA1 dispersion→apoptosis chain rests partly on correlative evidence","Direct degradation of NEAT1 by RBM7-NEXT not biochemically reconstituted"]},{"year":2020,"claim":"Established a stabilizing, mRNA-specific role for RBM7, showing direct binding to AU-rich elements in CDK1 mRNA lengthens its half-life to drive cell-cycle progression and proliferation.","evidence":"RIP, actinomycin D mRNA half-life assay, CDK1 rescue with ARE-mutant control, and xenograft proliferation assays","pmids":["33145401"],"confidence":"Medium","gaps":["Mechanism of stabilization versus its known destabilizing/degradative roles not reconciled","No in vitro reconstitution of CDK1 mRNA stabilization"]},{"year":2024,"claim":"Identified a splicing-regulatory function, showing RBM7 promotes MFGE8 exon-7 inclusion to favor a migration-inhibitory isoform and negatively regulates NF-κB signaling.","evidence":"RBM7 knockdown/overexpression, RT-PCR splicing assays, STAT1 phospho Western blot, HUVEC tube formation, and lung metastasis mouse model","pmids":["38995840"],"confidence":"Medium","gaps":["Mechanism by which RBM7 directs splice-site selection not biochemically reconstituted","Direct binding of RBM7 to MFGE8 pre-mRNA not mapped"]},{"year":2025,"claim":"Demonstrated an mRNA-destabilizing role with metabolic consequences, showing RBM7 binds and destabilizes FBXL16 mRNA to suppress mitochondrial dysfunction and ferroptosis in chemoresistant glioblastoma.","evidence":"Co-IP, RIP, actinomycin D mRNA stability assay, FBXL16 knockdown rescue with ferroptosis readouts, and xenograft model","pmids":["41381783"],"confidence":"Medium","gaps":["Destabilization mechanism not reconstituted in vitro","Whether NEXT/exosome mediates FBXL16 mRNA decay not established"]},{"year":null,"claim":"How RBM7 partitions between its NEXT/exosome degradative role, its 7SK/P-TEFb transcriptional role, and its sequence-specific mRNA stabilization/destabilization and splicing activities—and how phosphorylation orchestrates these switches—remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unified model reconciling opposing stabilizing and destabilizing mRNA effects","Determinants of target selection across these distinct activities unknown","Structural basis for stress-dependent reassignment of RBM7 from NEXT to 7SK not defined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[0,2,5,6,8]},{"term_id":"GO:0140098","term_label":"catalytic activity, acting on RNA","supporting_discovery_ids":[0,6,8]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,3,5]},{"term_id":"GO:0005654","term_label":"nucleoplasm","supporting_discovery_ids":[3,5]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[0,2,6,8]},{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[3]},{"term_id":"R-HSA-8953897","term_label":"Cellular responses to stimuli","supporting_discovery_ids":[2,3]}],"complexes":["NEXT complex","7SK snRNP"],"partners":["ZCCHC8","SAP145","P-TEFB"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9Y580","full_name":"RNA-binding protein 7","aliases":["RNA-binding motif protein 7"],"length_aa":266,"mass_kda":30.5,"function":"RNA-binding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation (PubMed:25189701, PubMed:25525152, PubMed:25578728, PubMed:25852104, PubMed:27871484). NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs (PubMed:25189701, PubMed:25852104, PubMed:27871484). Binds preferentially polyuridine sequences and associates with newly synthesized RNAs, including pre-mRNAs and short-lived exosome substrates such as promoter upstream transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products from small nuclear RNAs (snRNAs) (PubMed:25189701, PubMed:25525152, PubMed:25578728, PubMed:25852104). Participates in several biological processes including DNA damage response (DDR) and stress response (PubMed:25525152, PubMed:30824372). During stress response, activation of the p38MAPK-MK2 pathway decreases RBM7-RNA-binding and subsequently the RNA exosome degradation activities, thereby modulating the turnover of non-coding transcriptome (PubMed:25525152). Participates in DNA damage response (DDR), through its interaction with MEPCE and LARP7, the core subunits of 7SK snRNP complex, that release the positive transcription elongation factor b (P-TEFb) complex from the 7SK snRNP. In turn, activation of P-TEFb complex induces the transcription of P-TEFb-dependent DDR genes to promote cell viability (PubMed:30824372)","subcellular_location":"Nucleus, nucleoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/Q9Y580/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/RBM7","classification":"Not Classified","n_dependent_lines":22,"n_total_lines":1208,"dependency_fraction":0.018211920529801324},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000076053","cell_line_id":"CID001491","localizations":[{"compartment":"nucleoplasm","grade":3},{"compartment":"nucleolus_fc_dfc","grade":1}],"interactors":[{"gene":"SKIV2L2","stoichiometry":10.0},{"gene":"SFPQ","stoichiometry":10.0},{"gene":"NONO","stoichiometry":10.0},{"gene":"HNRNPH1","stoichiometry":0.2},{"gene":"PRMT9","stoichiometry":0.2},{"gene":"EXOSC5","stoichiometry":0.2},{"gene":"EXOSC2","stoichiometry":0.2},{"gene":"EXOSC7","stoichiometry":0.2},{"gene":"EXOSC10","stoichiometry":0.2},{"gene":"SNRPA","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID001491","total_profiled":1310},"omim":[{"mim_id":"619104","title":"RNA-BINDING MOTIF PROTEIN 47; RBM47","url":"https://www.omim.org/entry/619104"},{"mim_id":"616381","title":"ZINC FINGER CCHC DOMAIN-CONTAINING PROTEIN 8; ZCCHC8","url":"https://www.omim.org/entry/616381"},{"mim_id":"612413","title":"RNA-BINDING MOTIF PROTEIN 7; RBM7","url":"https://www.omim.org/entry/612413"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Nucleoplasm","reliability":"Enhanced"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"bone marrow","ntpm":37.5}],"url":"https://www.proteinatlas.org/search/RBM7"},"hgnc":{"alias_symbol":[],"prev_symbol":[]},"alphafold":{"accession":"Q9Y580","domains":[{"cath_id":"3.30.70.330","chopping":"2-85","consensus_level":"high","plddt":96.867,"start":2,"end":85}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9Y580","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9Y580-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9Y580-F1-predicted_aligned_error_v6.png","plddt_mean":65.25},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=RBM7","jax_strain_url":"https://www.jax.org/strain/search?query=RBM7"},"sequence":{"accession":"Q9Y580","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9Y580.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9Y580/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9Y580"}},"corpus_meta":[{"pmid":"30824372","id":"PMC_30824372","title":"P-TEFb Activation by RBM7 Shapes a Pro-survival Transcriptional Response to Genotoxic Stress.","date":"2019","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/30824372","citation_count":72,"is_preprint":false},{"pmid":"25852104","id":"PMC_25852104","title":"RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3'-end extended forms of snRNAs.","date":"2015","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/25852104","citation_count":58,"is_preprint":false},{"pmid":"27905398","id":"PMC_27905398","title":"Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.","date":"2016","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/27905398","citation_count":43,"is_preprint":false},{"pmid":"27193168","id":"PMC_27193168","title":"Altered RNA metabolism due to a homozygous RBM7 mutation in a patient with spinal motor neuropathy.","date":"2016","source":"Human molecular genetics","url":"https://pubmed.ncbi.nlm.nih.gov/27193168","citation_count":39,"is_preprint":false},{"pmid":"32187520","id":"PMC_32187520","title":"Dysregulated Expression of the Nuclear Exosome Targeting Complex Component Rbm7 in Nonhematopoietic Cells Licenses the Development of Fibrosis.","date":"2020","source":"Immunity","url":"https://pubmed.ncbi.nlm.nih.gov/32187520","citation_count":38,"is_preprint":false},{"pmid":"25525152","id":"PMC_25525152","title":"p38MAPK/MK2-mediated phosphorylation of RBM7 regulates the human nuclear exosome targeting complex.","date":"2014","source":"RNA (New York, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/25525152","citation_count":34,"is_preprint":false},{"pmid":"33145401","id":"PMC_33145401","title":"Oncogenic action of the exosome cofactor RBM7 by stabilization of CDK1 mRNA in breast cancer.","date":"2020","source":"NPJ breast cancer","url":"https://pubmed.ncbi.nlm.nih.gov/33145401","citation_count":25,"is_preprint":false},{"pmid":"38995840","id":"PMC_38995840","title":"RBM7 deficiency promotes breast cancer metastasis by coordinating MFGE8 splicing switch and NF-kB pathway.","date":"2024","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/38995840","citation_count":9,"is_preprint":false},{"pmid":"34165514","id":"PMC_34165514","title":"Novel insights into the pathogenesis of lung fibrosis: the RBM7-NEAT1-CXCL12-SatM axis at fibrosis onset.","date":"2021","source":"International immunology","url":"https://pubmed.ncbi.nlm.nih.gov/34165514","citation_count":5,"is_preprint":false},{"pmid":"27139832","id":"PMC_27139832","title":"RRM domain of human RBM7: purification, crystallization and structure determination.","date":"2016","source":"Acta crystallographica. Section F, Structural biology communications","url":"https://pubmed.ncbi.nlm.nih.gov/27139832","citation_count":5,"is_preprint":false},{"pmid":"32187513","id":"PMC_32187513","title":"Rbm7 in Structural Cells: A NEAT Way to Control Fibrosis.","date":"2020","source":"Immunity","url":"https://pubmed.ncbi.nlm.nih.gov/32187513","citation_count":4,"is_preprint":false},{"pmid":"41381783","id":"PMC_41381783","title":"RBM7 suppresses mitochondrial dysfunction and ferroptosis by destabilizing FBXL16 mRNA to enhance Temozolomide resistance in glioblastoma.","date":"2025","source":"Molecular genetics and genomics : MGG","url":"https://pubmed.ncbi.nlm.nih.gov/41381783","citation_count":0,"is_preprint":false},{"pmid":"31002802","id":"PMC_31002802","title":"Activation of P-TEFb by RBM7: To Live or Let Die.","date":"2019","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/31002802","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7412,"output_tokens":3030,"usd":0.033843,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10416,"output_tokens":3972,"usd":0.07569,"stage2_stop_reason":"end_turn"},"total_usd":0.109533,"stage1_batch_id":"msgbatch_01CNoDbkChHEkgrJnL7BwtGJ","stage2_batch_id":"msgbatch_016Y4x9E9Wg5VQDANj9quSQD","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2015,\n      \"finding\": \"The RRM domain of RBM7 mediates U-rich pyrimidine RNA sequence binding within the NEXT complex; two critical phenylalanine residues in the RRM are required for RNA interaction and for NEXT complex association with snRNAs in vivo. RBM7/NEXT depletion causes accumulation of mature and 3'-end extended forms of snRNAs, implicating NEXT in snRNA surveillance/snRNP biogenesis.\",\n      \"method\": \"Crystal structure of RBM7 RRM; site-directed mutagenesis of phenylalanine residues; RNA-binding assays; RIP; depletion experiments with RNA-seq readout\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure combined with mutagenesis and in vivo RIP validating RNA-binding mechanism, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"25852104\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"A proline-rich segment of ZCCHC8 is the direct interaction site for the RRM of RBM7, incorporating RBM7 into the NEXT complex. The same RRM of RBM7 can also bind a structurally similar proline-rich segment of the splicing factor SAP145, suggesting dual interactions linking the exosome to the spliceosome.\",\n      \"method\": \"Crystal structure of RBM7 RRM–ZCCHC8 proline-rich segment complex at 2.0 Å; biochemical binding assays; sequence/structural comparison with SAP145\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — high-resolution crystal structure plus biochemical validation of binding interfaces, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"27905398\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"RBM7 is phosphorylated by the p38MAPK/MK2 axis at serine 136 (S136). This phosphorylation strongly decreases RBM7's RNA-binding capacity. Inhibition of p38MAPK or the S136A mutation increases RBM7–RNA association. Phosphorylation of RBM7 during stress increases stability of PROMPTs (e.g., proRBM39, proEXT1, proDNAJB4) without changing their transcription rate, indicating that p38MAPK/MK2 modulates the noncoding transcriptome by blocking RBM7-mediated exosome targeting.\",\n      \"method\": \"In vitro kinase assay; phospho-site mapping (S136); RNA-binding assays with RBM7-S136A mutant; RNAPII ChIP; PROMPT stability measurements; overexpression of phospho-mutant\",\n      \"journal\": \"RNA (New York, N.Y.)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — in vitro kinase assay identifying the site plus mutagenesis rescue and functional RNA-binding readout, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"25525152\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Following genotoxic stress, p38MAPK activation triggers enhanced binding of RBM7 to core subunits of the 7SK snRNP, releasing P-TEFb from the inhibitory 7SK snRNP complex. Released P-TEFb relocates to chromatin to promote RNA Pol II pause release, driving transcription of short DDR genes and non-coding RNAs. Disruption of the RBM7–P-TEFb axis causes hypersensitivity to DNA-damaging agents via apoptosis.\",\n      \"method\": \"Co-immunoprecipitation of RBM7 with 7SK snRNP components; chromatin fractionation of P-TEFb; RNA Pol II ChIP; 4sU-seq; loss-of-function with apoptosis readout; genotoxic stress treatments\",\n      \"journal\": \"Molecular cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP, chromatin fractionation, Pol II ChIP, and functional rescue in a single focused study\",\n      \"pmids\": [\"30824372\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Crystal structure of the isolated RRM domain of human RBM7 was determined at 2.5 Å resolution, revealing a ring-shaped pentameric assembly (attributed to crystal packing). The structure required molecular replacement using RBM8 and CBP20 RRM structures as search models.\",\n      \"method\": \"X-ray crystallography at 2.5 Å; molecular replacement\",\n      \"journal\": \"Acta crystallographica. Section F, Structural biology communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution crystal structure but reported without functional validation; single paper, structural data only\",\n      \"pmids\": [\"27139832\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"RBM7 binds noncoding RNAs that form subnuclear bodies including NEAT1 speckles. Dysregulated (elevated) RBM7 expression leads to nuclear degradation of NEAT1 speckles, dispersion of the DNA repair protein BRCA1, and triggering of apoptosis in lung epithelial cells, which then produce CXCL12 to recruit pro-fibrotic SatMs.\",\n      \"method\": \"Rbm7 conditional knockout mouse (bleomycin fibrosis model); RNA immunoprecipitation for NEAT1 binding; immunofluorescence for BRCA1 dispersion; apoptosis assays; CXCL12 measurement\",\n      \"journal\": \"Immunity\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo KO with defined cellular phenotype and RIP for binding, but mechanistic steps (NEAT1 → BRCA1 dispersion → apoptosis) rely partly on correlative evidence within a single study\",\n      \"pmids\": [\"32187520\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"RBM7 directly binds AU-rich elements (AREs) in the 3'-UTR of CDK1 mRNA, stabilizing it and lengthening its half-life. This stabilization promotes breast cancer cell proliferation and G1-S progression; CDK1 overexpression rescues the proliferative defect caused by RBM7 knockdown, whereas a mutant CDK1 unable to bind AREs does not.\",\n      \"method\": \"RIP assay; mRNA half-life assay (actinomycin D); RBM7 knockdown/overexpression with CDK1 rescue; in vitro and in vivo (xenograft) proliferation assays\",\n      \"journal\": \"NPJ breast cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — RIP plus mRNA stability assay plus genetic rescue, single lab, multiple methods but no in vitro reconstitution\",\n      \"pmids\": [\"33145401\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"RBM7 controls the alternative splicing of MFGE8, promoting inclusion of exon 7 to produce the long isoform MFGE8-L over the truncated isoform MFGE8-S. MFGE8-L attenuates STAT1 phosphorylation and alters cell adhesion molecules to inhibit breast cancer migration and invasion, whereas MFGE8-S (lacking the second F5/8 type C domain) has the opposite effect. RBM7 also negatively regulates the NF-κB cascade; RBM7 silencing enhances HUVEC tube formation that is blocked by an NF-κB inhibitor.\",\n      \"method\": \"RBM7 knockdown/overexpression; RT-PCR splicing assays; lung metastasis mouse model; STAT1 phosphorylation Western blot; NF-κB pathway analysis; HUVEC tube formation assay\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — multiple functional assays (splicing, signaling, in vivo metastasis) in single lab; mechanism of splicing regulation by RBM7 not biochemically reconstituted\",\n      \"pmids\": [\"38995840\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"RBM7 directly interacts with FBXL16 mRNA and destabilizes it, reducing FBXL16 protein levels. This suppresses mitochondrial dysfunction and ferroptosis in TMZ-resistant glioblastoma cells. FBXL16 knockdown reverses ferroptosis and chemosensitivity induced by RBM7 loss, placing RBM7 upstream of FBXL16 in a resistance pathway.\",\n      \"method\": \"Co-immunoprecipitation; RNA immunoprecipitation; actinomycin D mRNA stability assay; RBM7 knockdown with ferroptosis/mitochondrial readouts; xenograft model\",\n      \"journal\": \"Molecular genetics and genomics : MGG\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Weak — RIP and mRNA stability assay support direct binding, single lab, no in vitro reconstitution of destabilization mechanism\",\n      \"pmids\": [\"41381783\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"A homozygous loss-of-function mutation in RBM7 in a patient with SMA-like motor neuropathy causes altered RNA metabolism in primary fibroblasts. Knockdown of rbm7 in zebrafish produces motor neuron and cerebellar defects, overlapping with those seen for exosc8/exosc3 knockdown, placing RBM7 in the same essential RNA-processing pathway required for neuronal differentiation.\",\n      \"method\": \"Patient fibroblast RNA-seq; zebrafish rbm7 morpholino knockdown with motor neuron/cerebellar phenotype readout; genetic epistasis comparison with exosc8/exosc3\",\n      \"journal\": \"Human molecular genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo loss-of-function in zebrafish with defined neuronal phenotype plus patient RNA-seq, but mechanism is inferred from pathway overlap rather than direct biochemical dissection\",\n      \"pmids\": [\"27193168\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"RBM7 is an RNA-recognition motif (RRM)-containing subunit of the nuclear exosome targeting (NEXT) complex that binds U-rich/AU-rich RNA sequences and directs non-coding RNAs (PROMPTs, snRNAs, NEAT1) to the nuclear exosome for degradation; its RNA-binding activity is negatively regulated by p38MAPK/MK2-mediated phosphorylation at S136, and during genotoxic stress RBM7 additionally activates P-TEFb by displacing it from the inhibitory 7SK snRNP to promote RNA Pol II pause release and a pro-survival transcriptional response, while also stabilizing select mRNAs (CDK1, FBXL16) and controlling alternative splicing (MFGE8) to influence cell proliferation, ferroptosis, and cancer metastasis.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"RBM7 is an RNA-recognition motif (RRM)-containing subunit of the nuclear exosome targeting (NEXT) complex that recognizes U-rich pyrimidine and AU-rich RNA sequences and directs non-coding and structured RNAs toward the nuclear exosome for surveillance and degradation [#0]. Its RRM both binds RNA—through two critical phenylalanine residues—and tethers RBM7 into NEXT by docking onto a proline-rich segment of ZCCHC8, with the same surface able to engage a structurally similar segment of the splicing factor SAP145, linking exosome targeting to the spliceosome [#0, #1]. Through this activity RBM7/NEXT carries out snRNA 3'-end surveillance and degradation of PROMPTs [#0, #2]. RBM7's RNA-binding output is gated by stress signaling: p38MAPK/MK2 phosphorylates RBM7 at S136, reducing RNA association and consequently stabilizing PROMPTs without altering their transcription [#2]; under genotoxic stress p38MAPK activation additionally redirects RBM7 to the 7SK snRNP, where it displaces and activates P-TEFb to promote RNA Pol II pause release and a pro-survival DNA-damage transcriptional program [#3]. Beyond non-coding RNA turnover, RBM7 shapes specific protein-coding outputs—stabilizing CDK1 mRNA via 3'-UTR AU-rich elements to drive cell-cycle progression [#6], destabilizing FBXL16 mRNA to suppress ferroptosis [#8], and controlling MFGE8 alternative splicing to restrain migration and invasion [#7]—thereby influencing proliferation, cancer metastasis, and chemoresistance. A homozygous loss-of-function RBM7 mutation underlies an SMA-like motor neuropathy, with patient and zebrafish phenotypes placing RBM7 in the same essential RNA-processing pathway as exosome core subunits [#9].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Established that RBM7's central RNA-binding activity is a regulated node, by showing that stress-activated p38MAPK/MK2 phosphorylates RBM7 at S136 to switch off exosome targeting of non-coding RNAs.\",\n      \"evidence\": \"In vitro kinase assay, S136 phospho-site mapping, S136A mutant RNA-binding assays, and PROMPT stability measurements\",\n      \"pmids\": [\"25525152\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not resolve how phosphorylation structurally disrupts the RRM-RNA interface\",\n        \"Scope of the phospho-regulated noncoding transcriptome beyond tested PROMPTs not defined\"\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Defined the molecular basis of RBM7 RNA recognition, showing the RRM binds U-rich pyrimidine sequences via two phenylalanines and that this activity underlies NEXT-mediated snRNA surveillance.\",\n      \"evidence\": \"Crystal structure of RBM7 RRM, phenylalanine mutagenesis, RNA-binding assays, RIP, and depletion with RNA-seq\",\n      \"pmids\": [\"25852104\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structure of RRM bound to RNA not solved\",\n        \"Full set of physiological RNA targets of NEXT not enumerated\"\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Showed how RBM7 is physically incorporated into NEXT and revealed a potential exosome-spliceosome link, by mapping the RRM to a proline-rich segment of ZCCHC8 and a similar segment of SAP145.\",\n      \"evidence\": \"2.0 Å crystal structure of RBM7 RRM–ZCCHC8 complex with biochemical binding assays and structural comparison\",\n      \"pmids\": [\"27905398\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Functional consequence of the RBM7-SAP145 interaction in vivo not established\",\n        \"Whether RNA binding and ZCCHC8 binding are mutually exclusive not resolved\"\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Provided an additional structural view of the isolated RBM7 RRM, but without functional consequence beyond the existing model.\",\n      \"evidence\": \"X-ray crystallography at 2.5 Å with molecular replacement\",\n      \"pmids\": [\"27139832\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Pentameric assembly attributed to crystal packing, not biologically validated\",\n        \"No functional validation accompanying the structure\"\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Connected RBM7 to human disease and confirmed its essential role in RNA processing, by linking a homozygous loss-of-function mutation to motor neuropathy and recapitulating neuronal defects in zebrafish overlapping exosome-subunit phenotypes.\",\n      \"evidence\": \"Patient fibroblast RNA-seq, zebrafish morpholino knockdown with neuronal phenotype, and epistasis with exosc8/exosc3\",\n      \"pmids\": [\"27193168\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Disease mechanism inferred from pathway overlap rather than direct biochemical dissection\",\n        \"Single patient; allelic spectrum not defined\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Revealed a moonlighting function distinct from RNA degradation, showing that genotoxic stress redirects RBM7 to the 7SK snRNP to release and activate P-TEFb, driving Pol II pause release and a pro-survival response.\",\n      \"evidence\": \"Reciprocal Co-IP with 7SK snRNP, chromatin fractionation of P-TEFb, Pol II ChIP, 4sU-seq, and loss-of-function apoptosis readout\",\n      \"pmids\": [\"30824372\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"How phosphorylation state of RBM7 coordinates NEXT versus 7SK engagement not resolved\",\n        \"Direct binding partner within 7SK snRNP for RBM7 not pinpointed structurally\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Extended RBM7 function to subnuclear body homeostasis, showing it binds NEAT1 and that elevated RBM7 degrades NEAT1 speckles, disperses BRCA1, and drives apoptosis with downstream pro-fibrotic signaling.\",\n      \"evidence\": \"Rbm7 conditional knockout mouse bleomycin model, RIP for NEAT1, BRCA1 immunofluorescence, apoptosis assays, and CXCL12 measurement\",\n      \"pmids\": [\"32187520\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"NEAT1→BRCA1 dispersion→apoptosis chain rests partly on correlative evidence\",\n        \"Direct degradation of NEAT1 by RBM7-NEXT not biochemically reconstituted\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Established a stabilizing, mRNA-specific role for RBM7, showing direct binding to AU-rich elements in CDK1 mRNA lengthens its half-life to drive cell-cycle progression and proliferation.\",\n      \"evidence\": \"RIP, actinomycin D mRNA half-life assay, CDK1 rescue with ARE-mutant control, and xenograft proliferation assays\",\n      \"pmids\": [\"33145401\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism of stabilization versus its known destabilizing/degradative roles not reconciled\",\n        \"No in vitro reconstitution of CDK1 mRNA stabilization\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Identified a splicing-regulatory function, showing RBM7 promotes MFGE8 exon-7 inclusion to favor a migration-inhibitory isoform and negatively regulates NF-κB signaling.\",\n      \"evidence\": \"RBM7 knockdown/overexpression, RT-PCR splicing assays, STAT1 phospho Western blot, HUVEC tube formation, and lung metastasis mouse model\",\n      \"pmids\": [\"38995840\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism by which RBM7 directs splice-site selection not biochemically reconstituted\",\n        \"Direct binding of RBM7 to MFGE8 pre-mRNA not mapped\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Demonstrated an mRNA-destabilizing role with metabolic consequences, showing RBM7 binds and destabilizes FBXL16 mRNA to suppress mitochondrial dysfunction and ferroptosis in chemoresistant glioblastoma.\",\n      \"evidence\": \"Co-IP, RIP, actinomycin D mRNA stability assay, FBXL16 knockdown rescue with ferroptosis readouts, and xenograft model\",\n      \"pmids\": [\"41381783\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Destabilization mechanism not reconstituted in vitro\",\n        \"Whether NEXT/exosome mediates FBXL16 mRNA decay not established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How RBM7 partitions between its NEXT/exosome degradative role, its 7SK/P-TEFb transcriptional role, and its sequence-specific mRNA stabilization/destabilization and splicing activities—and how phosphorylation orchestrates these switches—remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No unified model reconciling opposing stabilizing and destabilizing mRNA effects\",\n        \"Determinants of target selection across these distinct activities unknown\",\n        \"Structural basis for stress-dependent reassignment of RBM7 from NEXT to 7SK not defined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0, 2, 5, 6, 8]},\n      {\"term_id\": \"GO:0140098\", \"supporting_discovery_ids\": [0, 6, 8]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 3, 5]},\n      {\"term_id\": \"GO:0005654\", \"supporting_discovery_ids\": [3, 5]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [0, 2, 6, 8]},\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"R-HSA-8953897\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"complexes\": [\n      \"NEXT complex\",\n      \"7SK snRNP\"\n    ],\n    \"partners\": [\n      \"ZCCHC8\",\n      \"SAP145\",\n      \"P-TEFb\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}