{"gene":"DPF3","run_date":"2026-06-09T23:54:42","timeline":{"discoveries":[{"year":2008,"finding":"DPF3 is a component of the BAF chromatin remodeling complex and its double PHD finger domain binds methylated and acetylated lysine residues on histone H3 and H4, representing the first plant homeodomain shown to bind acetylated lysines. Morpholino knockdown of dpf3 in zebrafish caused incomplete cardiac looping, reduced ventricular contractility, and disassembled muscular fibers due to transcriptional deregulation of structural and regulatory proteins. Promoter analysis identified Dpf3 as a downstream transcriptional target of Mef2a.","method":"Co-immunoprecipitation with BAF complex, histone-binding assays (pull-down with methylated/acetylated histone peptides), zebrafish morpholino knockdown with phenotypic and transcriptional readouts, promoter luciferase analysis","journal":"Genes & development","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP with BAF complex, direct histone-binding assays, in vivo loss-of-function in zebrafish with defined cellular phenotype, replicated across multiple model organisms","pmids":["18765789"],"is_preprint":false},{"year":2001,"finding":"DPF3 (Cerd4) encodes two major protein isoforms: a full-length isoform containing all d4 family domains and a truncated XZ isoform lacking the C-terminal tandem PHD fingers. Expression is restricted mainly to retina and cerebellum in chicken and mouse, with distinct developmental kinetics for each isoform.","method":"cDNA cloning from chicken and mouse libraries, Northern blot, RT-PCR for isoform expression analysis, genomic structure determination","journal":"Mammalian genome","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — molecular cloning and expression characterization across two species, single lab but multiple methods","pmids":["11845289"],"is_preprint":false},{"year":2017,"finding":"DPF3 is a brown fat-selective component of the BAF chromatin remodeling complex required for brown fat gene programming and mitochondrial function. EBF2 physically interacts with BRG1/BAF complex, and DPF3 is a direct transcriptional target of EBF2. Loss of DPF3 in brown adipocytes reduced chromatin accessibility at EBF2-bound enhancers and decreased basal and catecholamine-stimulated expression of brown fat-selective genes.","method":"ChIP-seq, Co-immunoprecipitation (EBF2 with BRG1/BAF), siRNA knockdown of DPF3 in brown adipocytes, ATAC-seq for chromatin accessibility, gene expression analysis","journal":"Genes & development","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP, ChIP-seq, ATAC-seq, and loss-of-function with defined molecular and cellular phenotypes, multiple orthogonal methods in single rigorous study","pmids":["28428261"],"is_preprint":false},{"year":2013,"finding":"DPF3 is a transcriptional target of STAT5: both STAT5a and STAT5b bind the DPF3 promoter upon IL-3 stimulation, and knockdown of Stat5a/Stat5b in Ba/F3 cells reduces Dpf3 expression.","method":"Chromatin immunoprecipitation (ChIP) for STAT5 at DPF3 promoter, IL-3 stimulation assays, shRNA knockdown of Stat5a/Stat5b with RT-PCR/Western blot readout","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — ChIP demonstrating direct STAT5 binding plus loss-of-function confirmation, single lab with two orthogonal methods","pmids":["24155890"],"is_preprint":false},{"year":2019,"finding":"Downregulation of DPF3 in breast cancer cells promotes proliferation and motility, and this is mechanistically linked to activation of the JAK2/STAT3 signaling pathway as measured by phosphorylation of JAK2 and STAT3.","method":"siRNA knockdown and overexpression of DPF3 in breast cancer cell lines, MTT proliferation assay, wound healing and transwell invasion assays, Western blot for JAK2/STAT3 phosphorylation","journal":"Biochemical and biophysical research communications","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single set of methods, pathway placement via Western blot only without mechanistic dissection of how DPF3 regulates JAK2/STAT3","pmids":["31076105"],"is_preprint":false},{"year":2021,"finding":"A germline risk SNP (rs4903064) at 14q24 confers allele-specific increased expression of DPF3. Overexpression of DPF3 in renal cell lines increases cell growth rates and alters chromatin accessibility and gene expression, leading to inhibition of apoptosis and activation of oncogenic pathways including STAT3. siRNA knockdown of multiple DPF3-deregulated genes reduces growth.","method":"Massively parallel reporter assay, luciferase assays, eQTL analysis, DPF3 overexpression in renal cell lines with growth assays, ATAC-seq, gene expression profiling, siRNA knockdown of downstream targets","journal":"American journal of human genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal functional methods (reporter assay, ATAC-seq, overexpression/KD with cellular phenotype), single lab","pmids":["34390653"],"is_preprint":false},{"year":2022,"finding":"The renal cancer risk SNP rs4903064 resides within an active enhancer region that creates a novel HIF-binding motif. Allele-specific HIF binding to this locus was confirmed by ChIP of HIF subunits in primary renal cells, and HIF-mediated DPF3 upregulation was dependent on the presence of the risk allele. DPF3 deletion in proximal tubular cells retarded cell growth.","method":"ChIP for HIF subunits in primary renal cells and tumor tissue, luciferase enhancer assays, eQTL analysis in patient cohort, CRISPR/siRNA-mediated DPF3 deletion with proliferation assay","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — ChIP demonstrating allele-specific HIF binding plus functional deletion phenotype, single lab with multiple orthogonal methods","pmids":["35148991"],"is_preprint":false},{"year":2022,"finding":"The short isoform DPF3a specifically interacts with SNIP1, forming a complex with SMAD4 and p300 histone acetyltransferase (HAT) to activate TGF-β target genes. Binding of DPF3a to SNIP1 releases SNIP1's repressive effect on p300 HAT activity, increasing local histone acetylation and activating cell movement-related genes, thereby promoting kidney cancer cell migration in vitro and in vivo.","method":"Co-immunoprecipitation of DPF3a with SNIP1, SMAD4, and p300; HAT activity assay; histone acetylation ChIP; DPF3a overexpression/knockdown in ccRCC cell lines with migration assays; in vivo metastasis mouse model","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP identifying protein complex, enzymatic HAT activity assay, ChIP for histone acetylation, in vitro and in vivo functional validation with defined molecular mechanism","pmids":["35945219"],"is_preprint":false},{"year":2024,"finding":"DPF3 exhibits a non-canonical localization outside the nucleus: it dynamically localizes to centriolar satellites in interphase and to the centrosome, spindle midzone, bridging fiber area, and midbodies during mitosis. Loss of DPF3 causes kinetochore fiber instability, unstable kinetochore-microtubule attachment, defects in chromosome alignment, altered mitotic progression, cell death, and genomic instability. DPF3 also localizes to centriolar satellites at the base of primary cilia and is required for axoneme extension during ciliogenesis.","method":"Immunofluorescence microscopy and live-cell imaging for subcellular localization, siRNA/CRISPR loss-of-function with mitotic phenotype assays (kinetochore fiber stability, chromosome alignment), ciliogenesis assays measuring axoneme length","journal":"Journal of cell science","confidence":"High","confidence_rationale":"Tier 2 / Strong — direct localization experiments with functional consequence via loss-of-function, multiple phenotypic readouts (mitosis, ciliogenesis), orthogonal methods in single rigorous study","pmids":["38661008"],"is_preprint":false}],"current_model":"DPF3 (BAF45c) is a tissue-specific subunit of the BAF/SWI/SNF chromatin remodeling complex whose double PHD finger domain reads both acetylated and methylated histone H3/H4 lysine residues, anchoring the complex to chromatin; it regulates heart/muscle development, brown adipogenesis (downstream of EBF2), and cancer cell migration (via a DPF3a–SNIP1–SMAD4–p300 complex that relieves repression of p300 HAT activity to activate TGF-β target genes); additionally, DPF3 has a non-canonical role at centriolar satellites, centrosomes, and midbodies where it is required for kinetochore-microtubule stability, proper mitotic progression, and ciliogenesis."},"narrative":{"mechanistic_narrative":"DPF3 (BAF45c) is a tissue-restricted, histone-reading subunit of the BAF (SWI/SNF) chromatin remodeling complex that couples chromatin recognition to lineage-specific transcriptional programs in heart, muscle, and adipose tissue [PMID:18765789, PMID:28428261]. Its tandem (double) PHD finger domain directly binds both methylated and acetylated lysines on histones H3 and H4, anchoring the BAF complex to chromatin, and loss of dpf3 in vivo deregulates structural and regulatory genes to produce defective cardiac looping and disrupted muscle fibers [PMID:18765789]. In brown adipocytes, DPF3 is a direct transcriptional target of EBF2 and is required for chromatin accessibility at EBF2-bound enhancers and for catecholamine-responsive brown fat gene expression and mitochondrial function [PMID:28428261]. DPF3 expression is itself driven by upstream signaling inputs, being a transcriptional target of STAT5 downstream of IL-3 [PMID:24155890], and in renal cancer a germline risk allele creates an enhancer HIF-binding motif that drives allele-specific DPF3 overexpression, promoting cell growth and oncogenic chromatin/transcriptional changes [PMID:34390653, PMID:35148991]. Through its short DPF3a isoform, DPF3 also acts in the cytoplasm-to-chromatin TGF-β axis: DPF3a binds SNIP1 within a SMAD4–p300 complex, relieving SNIP1-mediated repression of p300 HAT activity to increase local histone acetylation and activate cell-movement genes that drive kidney cancer migration and metastasis [PMID:35945219]. Beyond its nuclear chromatin role, DPF3 has a non-canonical localization to centriolar satellites, the centrosome, spindle midzone, and midbodies, where it is required for kinetochore-microtubule attachment stability, faithful mitotic progression and genome stability, and for axoneme extension during ciliogenesis [PMID:38661008]. The gene encodes a full-length and a truncated XZ isoform with restricted, developmentally distinct expression [PMID:11845289].","teleology":[{"year":2001,"claim":"Established the gene's isoform structure and tissue restriction, defining a full-length form bearing all d4 domains and a truncated XZ form lacking the C-terminal tandem PHD fingers — the structural basis for later isoform-specific functions.","evidence":"cDNA cloning, Northern blot and RT-PCR isoform expression across chicken and mouse","pmids":["11845289"],"confidence":"Medium","gaps":["No molecular function assigned to either isoform at this stage","Does not establish how the PHD-less XZ isoform differs functionally"]},{"year":2008,"claim":"Defined DPF3's core molecular function as a BAF complex subunit whose double PHD finger reads both methylated and acetylated histone lysines, linking chromatin recognition to cardiac and muscle gene programs in vivo.","evidence":"BAF Co-IP, methylated/acetylated histone peptide pull-downs, zebrafish morpholino knockdown with cardiac/muscle phenotypes, Mef2a promoter analysis","pmids":["18765789"],"confidence":"High","gaps":["Does not resolve which BAF target genes are directly bound versus indirectly deregulated","Structural basis of dual methyl/acetyl recognition not defined"]},{"year":2013,"claim":"Placed DPF3 downstream of cytokine signaling by showing it is a direct STAT5 transcriptional target induced by IL-3, indicating its expression is signal-responsive.","evidence":"STAT5 ChIP at the DPF3 promoter and Stat5a/Stat5b shRNA knockdown in Ba/F3 cells","pmids":["24155890"],"confidence":"Medium","gaps":["Functional consequence of STAT5-driven DPF3 in hematopoietic cells not tested","No link to DPF3's chromatin-remodeling role in this context"]},{"year":2017,"claim":"Identified DPF3 as a brown-fat-selective BAF subunit acting downstream of EBF2 to maintain enhancer accessibility, extending its chromatin role to adipose lineage programming and mitochondrial function.","evidence":"EBF2/BRG1 Co-IP, ChIP-seq, ATAC-seq and DPF3 siRNA knockdown in brown adipocytes","pmids":["28428261"],"confidence":"High","gaps":["Whether DPF3 histone-reading is required for EBF2 enhancer accessibility not directly tested","In vivo brown-fat phenotype of DPF3 loss not established"]},{"year":2019,"claim":"Proposed a tumor-suppressive role in breast cancer where DPF3 loss promotes proliferation/motility via JAK2/STAT3 activation, but the mechanistic connection is unresolved.","evidence":"siRNA/overexpression in breast cancer lines with proliferation, migration assays and JAK2/STAT3 phospho-Western blots","pmids":["31076105"],"confidence":"Low","gaps":["Pathway placement rests on Western blot only without mechanistic dissection of how DPF3 regulates JAK2/STAT3","Opposite (oncogenic) direction reported in renal cells, leaving tissue context unresolved"]},{"year":2022,"claim":"Resolved how a germline risk SNP drives DPF3 in renal cancer, showing the variant creates an active enhancer HIF-binding motif that supports allele-specific HIF-driven DPF3 overexpression and oncogenic growth.","evidence":"Reporter/luciferase assays, eQTL analysis, allele-specific HIF ChIP in primary renal cells, ATAC-seq and CRISPR/siRNA DPF3 deletion with proliferation assays","pmids":["34390653","35148991"],"confidence":"Medium","gaps":["Direct chromatin targets mediating DPF3's pro-growth effect not fully defined","Single-lab functional system"]},{"year":2022,"claim":"Defined an isoform-specific cytoplasmic-to-chromatin mechanism: DPF3a binds SNIP1 in a SMAD4–p300 complex to relieve repression of p300 HAT, activating TGF-β migration genes and driving metastasis.","evidence":"Co-IP of DPF3a with SNIP1/SMAD4/p300, HAT activity assay, histone-acetylation ChIP, ccRCC migration assays and in vivo metastasis model","pmids":["35945219"],"confidence":"High","gaps":["Whether DPF3a's PHD-reading versus protein-protein interaction drives SNIP1 binding not separated","Generality beyond renal cancer not tested"]},{"year":2024,"claim":"Revealed a non-canonical extranuclear function, placing DPF3 at centriolar satellites, centrosomes, spindle midzone and midbodies where it is required for kinetochore-microtubule stability, mitotic fidelity, and ciliogenesis.","evidence":"Immunofluorescence/live-cell imaging localization and siRNA/CRISPR loss-of-function with mitotic and axoneme-length phenotypes","pmids":["38661008"],"confidence":"High","gaps":["Molecular partners at centrosome/midbody not identified","How a chromatin-remodeling subunit is targeted to centriolar satellites is unknown","Relationship between chromatin and mitotic/ciliary functions unresolved"]},{"year":null,"claim":"How DPF3 switches between its nuclear BAF chromatin role and its centrosomal/ciliary role, and what determines its opposing tumor-suppressive versus oncogenic outputs across tissues, remains open.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of dual histone-mark recognition","Centrosomal recruitment mechanism and partners unidentified","Tissue-specific determinants of oncogenic versus suppressive DPF3 function undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0042393","term_label":"histone binding","supporting_discovery_ids":[0]},{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[0,2,7]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[7]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,2]},{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[8]},{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[8]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[8]}],"pathway":[{"term_id":"R-HSA-4839726","term_label":"Chromatin organization","supporting_discovery_ids":[0,2]},{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[0,2,7]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[0,2]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[8]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[7]}],"complexes":["BAF (SWI/SNF) chromatin remodeling complex"],"partners":["BRG1","EBF2","SNIP1","SMAD4","EP300"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q92784","full_name":"Zinc finger protein DPF3","aliases":["BRG1-associated factor 45C","BAF45C","Zinc finger protein cer-d4"],"length_aa":378,"mass_kda":43.1,"function":"Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development Acts as a regulator of myogenesis in cooperation with HDGFL2 (PubMed:32459350). Mediates the interaction of HDGFL2 with the BAF complex (PubMed:32459350). HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350)","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/Q92784/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/DPF3","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"ARID1A","stoichiometry":0.2},{"gene":"SMARCA4","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/DPF3","total_profiled":1310},"omim":[{"mim_id":"601672","title":"D4, ZINC, AND DOUBLE PHD FINGERS FAMILY, MEMBER 3; DPF3","url":"https://www.omim.org/entry/601672"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Nucleoplasm","reliability":"Enhanced"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in some","driving_tissues":[{"tissue":"brain","ntpm":16.4},{"tissue":"heart muscle","ntpm":3.9},{"tissue":"retina","ntpm":4.8}],"url":"https://www.proteinatlas.org/search/DPF3"},"hgnc":{"alias_symbol":["cer-d4","Cerd4","FLJ14079","BAF45c","SMARCG3"],"prev_symbol":[]},"alphafold":{"accession":"Q92784","domains":[{"cath_id":"3.30.40.10","chopping":"254-316","consensus_level":"medium","plddt":94.7144,"start":254,"end":316},{"cath_id":"3.30.40.10","chopping":"319-371","consensus_level":"medium","plddt":93.216,"start":319,"end":371}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q92784","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q92784-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q92784-F1-predicted_aligned_error_v6.png","plddt_mean":73.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=DPF3","jax_strain_url":"https://www.jax.org/strain/search?query=DPF3"},"sequence":{"accession":"Q92784","fasta_url":"https://rest.uniprot.org/uniprotkb/Q92784.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q92784/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q92784"}},"corpus_meta":[{"pmid":"30824325","id":"PMC_30824325","title":"CCR7 Chemokine Receptor-Inducible lnc-Dpf3 Restrains Dendritic Cell Migration by Inhibiting HIF-1α-Mediated Glycolysis.","date":"2019","source":"Immunity","url":"https://pubmed.ncbi.nlm.nih.gov/30824325","citation_count":302,"is_preprint":false},{"pmid":"18765789","id":"PMC_18765789","title":"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex.","date":"2008","source":"Genes & development","url":"https://pubmed.ncbi.nlm.nih.gov/18765789","citation_count":182,"is_preprint":false},{"pmid":"28428261","id":"PMC_28428261","title":"EBF2 transcriptionally regulates brown adipogenesis via the histone reader DPF3 and the BAF chromatin remodeling complex.","date":"2017","source":"Genes & development","url":"https://pubmed.ncbi.nlm.nih.gov/28428261","citation_count":69,"is_preprint":false},{"pmid":"35945219","id":"PMC_35945219","title":"The SWI/SNF chromatin remodeling factor DPF3 regulates metastasis of ccRCC by modulating TGF-β signaling.","date":"2022","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/35945219","citation_count":32,"is_preprint":false},{"pmid":"32173431","id":"PMC_32173431","title":"Novel Pheretima guillelmi-derived antithrombotic protein DPf3: Identification, characterization, in vitro evaluation and antithrombotic mechanisms investigation.","date":"2020","source":"International journal of biological macromolecules","url":"https://pubmed.ncbi.nlm.nih.gov/32173431","citation_count":25,"is_preprint":false},{"pmid":"27232852","id":"PMC_27232852","title":"Strong association of SLC1A1 and DPF3 gene variants with idiopathic male infertility in Han Chinese.","date":"2017","source":"Asian journal of andrology","url":"https://pubmed.ncbi.nlm.nih.gov/27232852","citation_count":23,"is_preprint":false},{"pmid":"31076105","id":"PMC_31076105","title":"Downregulation of DPF3 promotes the proliferation and motility of breast cancer cells through activating JAK2/STAT3 signaling.","date":"2019","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/31076105","citation_count":22,"is_preprint":false},{"pmid":"34390653","id":"PMC_34390653","title":"Altered regulation of DPF3, a member of the SWI/SNF complexes, underlies the 14q24 renal cancer susceptibility locus.","date":"2021","source":"American journal of human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/34390653","citation_count":22,"is_preprint":false},{"pmid":"24155890","id":"PMC_24155890","title":"Identification of a STAT5 target gene, Dpf3, provides novel insights in chronic lymphocytic leukemia.","date":"2013","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/24155890","citation_count":19,"is_preprint":false},{"pmid":"16109180","id":"PMC_16109180","title":"Genetic polymorphisms in DPF3 associated with risk of breast cancer and lymph node metastases.","date":"2005","source":"Journal of carcinogenesis","url":"https://pubmed.ncbi.nlm.nih.gov/16109180","citation_count":18,"is_preprint":false},{"pmid":"11845289","id":"PMC_11845289","title":"Cerd4, third member of the d4 gene family: expression and organization of genomic locus.","date":"2001","source":"Mammalian genome : official journal of the International Mammalian Genome Society","url":"https://pubmed.ncbi.nlm.nih.gov/11845289","citation_count":17,"is_preprint":false},{"pmid":"35148991","id":"PMC_35148991","title":"The renal cancer risk allele at 14q24.2 activates a novel hypoxia-inducible transcription factor-binding enhancer of DPF3 expression.","date":"2022","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/35148991","citation_count":13,"is_preprint":false},{"pmid":"35325570","id":"PMC_35325570","title":"LINC00982 Inhibits the Proliferation, Migration, and Invasion of Breast Cancer Cells Through the miR-765/DPF3 Axis.","date":"2022","source":"DNA and cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/35325570","citation_count":12,"is_preprint":false},{"pmid":"28975488","id":"PMC_28975488","title":"Association of TUSC1 and DPF3 gene polymorphisms with male infertility.","date":"2017","source":"Journal of assisted reproduction and genetics","url":"https://pubmed.ncbi.nlm.nih.gov/28975488","citation_count":11,"is_preprint":false},{"pmid":"34801788","id":"PMC_34801788","title":"DPF3, A Putative Candidate Gene For Melanoma Etiopathogenesis in Gray Horses.","date":"2021","source":"Journal of equine veterinary science","url":"https://pubmed.ncbi.nlm.nih.gov/34801788","citation_count":9,"is_preprint":false},{"pmid":"40108168","id":"PMC_40108168","title":"Dipeptidyl peptidase DPF-3 is a gatekeeper of microRNA Argonaute compensation in animals.","date":"2025","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/40108168","citation_count":6,"is_preprint":false},{"pmid":"38661008","id":"PMC_38661008","title":"Non-canonical role for the BAF complex subunit DPF3 in mitosis and ciliogenesis.","date":"2024","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/38661008","citation_count":5,"is_preprint":false},{"pmid":"38159828","id":"PMC_38159828","title":"Alleviation of endothelial dysfunction of Pheretima guillemi (Michaelsen)-derived protein DPf3 in ponatinib-induced thrombotic zebrafish and mechanisms explored through ox-LDL-induced HUVECs and TMT-based proteomics.","date":"2023","source":"Journal of ethnopharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/38159828","citation_count":5,"is_preprint":false},{"pmid":"38795855","id":"PMC_38795855","title":"DPF3 polymorphisms increased the risk of pulmonary tuberculosis in the Northwest Chinese Han population.","date":"2024","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/38795855","citation_count":0,"is_preprint":false},{"pmid":"41889506","id":"PMC_41889506","title":"Validation of ITPR2, DPF3, EPAS1, and PVT1-associated SNPs as biomarkers for RCC in an independent case-control cohort.","date":"2026","source":"Frontiers in medicine","url":"https://pubmed.ncbi.nlm.nih.gov/41889506","citation_count":0,"is_preprint":false},{"pmid":"41988656","id":"PMC_41988656","title":"Identification of Amyloid Regions and Mechanisms from Sequence-Based Modeling and Molecular Dynamics Simulation: A Case Study of the Intrinsically Disordered Protein DPF3.","date":"2026","source":"Journal of chemical information and modeling","url":"https://pubmed.ncbi.nlm.nih.gov/41988656","citation_count":0,"is_preprint":false},{"pmid":"41239757","id":"PMC_41239757","title":"The Caenorhabditis elegans DPF-3 and human DPP4 have tripeptidyl peptidase activity.","date":"2025","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/41239757","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":13163,"output_tokens":3051,"usd":0.042627,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":9956,"output_tokens":3561,"usd":0.069403,"stage2_stop_reason":"end_turn"},"total_usd":0.11203,"stage1_batch_id":"msgbatch_01AsR7g8dGTEiEw9U83bJeWn","stage2_batch_id":"msgbatch_01YV5ZyxtFNUZEjxRcpd9jzb","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking at the papers, I need to carefully classify each:\n\n- Papers [1] = about lnc-Dpf3 (long non-coding RNA), NOT the DPF3 protein → EXCLUDE\n- Papers [5], [18] = about DPf3 from earthworm Pheretima guillelmi (antithrombotic protein) → EXCLUDE (symbol collision, completely different organism/protein)\n- Papers [16], [22] = about C. elegans DPF-3 (dipeptidyl peptidase) → EXCLUDE (symbol collision - this is a peptidase, not the BAF complex histone reader)\n- Papers [6], [10], [14], [19], [20] = GWAS/SNP association studies with no mechanistic experiments → EXCLUDE\n- Papers [13] = about LINC00982/miR-765 pathway using DPF3 as downstream target, but the mechanistic experiment focuses on DPF3 as a functional target of miR-765 via luciferase assay → borderline, include for the DPF3 mechanistic aspect\n- Papers [15] = candidate gene study, no direct mechanistic experiment → EXCLUDE\n- Papers [21] = computational/MD simulation study, no wet-lab experimental validation → EXCLUDE\n\nRemaining relevant papers: [2], [3], [4], [7], [8], [9], [11], [12], [17]\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2008,\n      \"finding\": \"DPF3 is a component of the BAF chromatin remodeling complex and its double PHD finger domain binds methylated and acetylated lysine residues on histone H3 and H4, representing the first plant homeodomain shown to bind acetylated lysines. Morpholino knockdown of dpf3 in zebrafish caused incomplete cardiac looping, reduced ventricular contractility, and disassembled muscular fibers due to transcriptional deregulation of structural and regulatory proteins. Promoter analysis identified Dpf3 as a downstream transcriptional target of Mef2a.\",\n      \"method\": \"Co-immunoprecipitation with BAF complex, histone-binding assays (pull-down with methylated/acetylated histone peptides), zebrafish morpholino knockdown with phenotypic and transcriptional readouts, promoter luciferase analysis\",\n      \"journal\": \"Genes & development\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP with BAF complex, direct histone-binding assays, in vivo loss-of-function in zebrafish with defined cellular phenotype, replicated across multiple model organisms\",\n      \"pmids\": [\"18765789\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"DPF3 (Cerd4) encodes two major protein isoforms: a full-length isoform containing all d4 family domains and a truncated XZ isoform lacking the C-terminal tandem PHD fingers. Expression is restricted mainly to retina and cerebellum in chicken and mouse, with distinct developmental kinetics for each isoform.\",\n      \"method\": \"cDNA cloning from chicken and mouse libraries, Northern blot, RT-PCR for isoform expression analysis, genomic structure determination\",\n      \"journal\": \"Mammalian genome\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — molecular cloning and expression characterization across two species, single lab but multiple methods\",\n      \"pmids\": [\"11845289\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"DPF3 is a brown fat-selective component of the BAF chromatin remodeling complex required for brown fat gene programming and mitochondrial function. EBF2 physically interacts with BRG1/BAF complex, and DPF3 is a direct transcriptional target of EBF2. Loss of DPF3 in brown adipocytes reduced chromatin accessibility at EBF2-bound enhancers and decreased basal and catecholamine-stimulated expression of brown fat-selective genes.\",\n      \"method\": \"ChIP-seq, Co-immunoprecipitation (EBF2 with BRG1/BAF), siRNA knockdown of DPF3 in brown adipocytes, ATAC-seq for chromatin accessibility, gene expression analysis\",\n      \"journal\": \"Genes & development\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP, ChIP-seq, ATAC-seq, and loss-of-function with defined molecular and cellular phenotypes, multiple orthogonal methods in single rigorous study\",\n      \"pmids\": [\"28428261\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"DPF3 is a transcriptional target of STAT5: both STAT5a and STAT5b bind the DPF3 promoter upon IL-3 stimulation, and knockdown of Stat5a/Stat5b in Ba/F3 cells reduces Dpf3 expression.\",\n      \"method\": \"Chromatin immunoprecipitation (ChIP) for STAT5 at DPF3 promoter, IL-3 stimulation assays, shRNA knockdown of Stat5a/Stat5b with RT-PCR/Western blot readout\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — ChIP demonstrating direct STAT5 binding plus loss-of-function confirmation, single lab with two orthogonal methods\",\n      \"pmids\": [\"24155890\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Downregulation of DPF3 in breast cancer cells promotes proliferation and motility, and this is mechanistically linked to activation of the JAK2/STAT3 signaling pathway as measured by phosphorylation of JAK2 and STAT3.\",\n      \"method\": \"siRNA knockdown and overexpression of DPF3 in breast cancer cell lines, MTT proliferation assay, wound healing and transwell invasion assays, Western blot for JAK2/STAT3 phosphorylation\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single set of methods, pathway placement via Western blot only without mechanistic dissection of how DPF3 regulates JAK2/STAT3\",\n      \"pmids\": [\"31076105\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"A germline risk SNP (rs4903064) at 14q24 confers allele-specific increased expression of DPF3. Overexpression of DPF3 in renal cell lines increases cell growth rates and alters chromatin accessibility and gene expression, leading to inhibition of apoptosis and activation of oncogenic pathways including STAT3. siRNA knockdown of multiple DPF3-deregulated genes reduces growth.\",\n      \"method\": \"Massively parallel reporter assay, luciferase assays, eQTL analysis, DPF3 overexpression in renal cell lines with growth assays, ATAC-seq, gene expression profiling, siRNA knockdown of downstream targets\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal functional methods (reporter assay, ATAC-seq, overexpression/KD with cellular phenotype), single lab\",\n      \"pmids\": [\"34390653\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"The renal cancer risk SNP rs4903064 resides within an active enhancer region that creates a novel HIF-binding motif. Allele-specific HIF binding to this locus was confirmed by ChIP of HIF subunits in primary renal cells, and HIF-mediated DPF3 upregulation was dependent on the presence of the risk allele. DPF3 deletion in proximal tubular cells retarded cell growth.\",\n      \"method\": \"ChIP for HIF subunits in primary renal cells and tumor tissue, luciferase enhancer assays, eQTL analysis in patient cohort, CRISPR/siRNA-mediated DPF3 deletion with proliferation assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — ChIP demonstrating allele-specific HIF binding plus functional deletion phenotype, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"35148991\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"The short isoform DPF3a specifically interacts with SNIP1, forming a complex with SMAD4 and p300 histone acetyltransferase (HAT) to activate TGF-β target genes. Binding of DPF3a to SNIP1 releases SNIP1's repressive effect on p300 HAT activity, increasing local histone acetylation and activating cell movement-related genes, thereby promoting kidney cancer cell migration in vitro and in vivo.\",\n      \"method\": \"Co-immunoprecipitation of DPF3a with SNIP1, SMAD4, and p300; HAT activity assay; histone acetylation ChIP; DPF3a overexpression/knockdown in ccRCC cell lines with migration assays; in vivo metastasis mouse model\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP identifying protein complex, enzymatic HAT activity assay, ChIP for histone acetylation, in vitro and in vivo functional validation with defined molecular mechanism\",\n      \"pmids\": [\"35945219\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"DPF3 exhibits a non-canonical localization outside the nucleus: it dynamically localizes to centriolar satellites in interphase and to the centrosome, spindle midzone, bridging fiber area, and midbodies during mitosis. Loss of DPF3 causes kinetochore fiber instability, unstable kinetochore-microtubule attachment, defects in chromosome alignment, altered mitotic progression, cell death, and genomic instability. DPF3 also localizes to centriolar satellites at the base of primary cilia and is required for axoneme extension during ciliogenesis.\",\n      \"method\": \"Immunofluorescence microscopy and live-cell imaging for subcellular localization, siRNA/CRISPR loss-of-function with mitotic phenotype assays (kinetochore fiber stability, chromosome alignment), ciliogenesis assays measuring axoneme length\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — direct localization experiments with functional consequence via loss-of-function, multiple phenotypic readouts (mitosis, ciliogenesis), orthogonal methods in single rigorous study\",\n      \"pmids\": [\"38661008\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"DPF3 (BAF45c) is a tissue-specific subunit of the BAF/SWI/SNF chromatin remodeling complex whose double PHD finger domain reads both acetylated and methylated histone H3/H4 lysine residues, anchoring the complex to chromatin; it regulates heart/muscle development, brown adipogenesis (downstream of EBF2), and cancer cell migration (via a DPF3a–SNIP1–SMAD4–p300 complex that relieves repression of p300 HAT activity to activate TGF-β target genes); additionally, DPF3 has a non-canonical role at centriolar satellites, centrosomes, and midbodies where it is required for kinetochore-microtubule stability, proper mitotic progression, and ciliogenesis.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"DPF3 (BAF45c) is a tissue-restricted, histone-reading subunit of the BAF (SWI/SNF) chromatin remodeling complex that couples chromatin recognition to lineage-specific transcriptional programs in heart, muscle, and adipose tissue [#0, #2]. Its tandem (double) PHD finger domain directly binds both methylated and acetylated lysines on histones H3 and H4, anchoring the BAF complex to chromatin, and loss of dpf3 in vivo deregulates structural and regulatory genes to produce defective cardiac looping and disrupted muscle fibers [#0]. In brown adipocytes, DPF3 is a direct transcriptional target of EBF2 and is required for chromatin accessibility at EBF2-bound enhancers and for catecholamine-responsive brown fat gene expression and mitochondrial function [#2]. DPF3 expression is itself driven by upstream signaling inputs, being a transcriptional target of STAT5 downstream of IL-3 [#3], and in renal cancer a germline risk allele creates an enhancer HIF-binding motif that drives allele-specific DPF3 overexpression, promoting cell growth and oncogenic chromatin/transcriptional changes [#5, #6]. Through its short DPF3a isoform, DPF3 also acts in the cytoplasm-to-chromatin TGF-\\u03b2 axis: DPF3a binds SNIP1 within a SMAD4\\u2013p300 complex, relieving SNIP1-mediated repression of p300 HAT activity to increase local histone acetylation and activate cell-movement genes that drive kidney cancer migration and metastasis [#7]. Beyond its nuclear chromatin role, DPF3 has a non-canonical localization to centriolar satellites, the centrosome, spindle midzone, and midbodies, where it is required for kinetochore-microtubule attachment stability, faithful mitotic progression and genome stability, and for axoneme extension during ciliogenesis [#8]. The gene encodes a full-length and a truncated XZ isoform with restricted, developmentally distinct expression [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Established the gene's isoform structure and tissue restriction, defining a full-length form bearing all d4 domains and a truncated XZ form lacking the C-terminal tandem PHD fingers — the structural basis for later isoform-specific functions.\",\n      \"evidence\": \"cDNA cloning, Northern blot and RT-PCR isoform expression across chicken and mouse\",\n      \"pmids\": [\"11845289\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No molecular function assigned to either isoform at this stage\", \"Does not establish how the PHD-less XZ isoform differs functionally\"]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Defined DPF3's core molecular function as a BAF complex subunit whose double PHD finger reads both methylated and acetylated histone lysines, linking chromatin recognition to cardiac and muscle gene programs in vivo.\",\n      \"evidence\": \"BAF Co-IP, methylated/acetylated histone peptide pull-downs, zebrafish morpholino knockdown with cardiac/muscle phenotypes, Mef2a promoter analysis\",\n      \"pmids\": [\"18765789\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not resolve which BAF target genes are directly bound versus indirectly deregulated\", \"Structural basis of dual methyl/acetyl recognition not defined\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Placed DPF3 downstream of cytokine signaling by showing it is a direct STAT5 transcriptional target induced by IL-3, indicating its expression is signal-responsive.\",\n      \"evidence\": \"STAT5 ChIP at the DPF3 promoter and Stat5a/Stat5b shRNA knockdown in Ba/F3 cells\",\n      \"pmids\": [\"24155890\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional consequence of STAT5-driven DPF3 in hematopoietic cells not tested\", \"No link to DPF3's chromatin-remodeling role in this context\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Identified DPF3 as a brown-fat-selective BAF subunit acting downstream of EBF2 to maintain enhancer accessibility, extending its chromatin role to adipose lineage programming and mitochondrial function.\",\n      \"evidence\": \"EBF2/BRG1 Co-IP, ChIP-seq, ATAC-seq and DPF3 siRNA knockdown in brown adipocytes\",\n      \"pmids\": [\"28428261\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether DPF3 histone-reading is required for EBF2 enhancer accessibility not directly tested\", \"In vivo brown-fat phenotype of DPF3 loss not established\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Proposed a tumor-suppressive role in breast cancer where DPF3 loss promotes proliferation/motility via JAK2/STAT3 activation, but the mechanistic connection is unresolved.\",\n      \"evidence\": \"siRNA/overexpression in breast cancer lines with proliferation, migration assays and JAK2/STAT3 phospho-Western blots\",\n      \"pmids\": [\"31076105\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Pathway placement rests on Western blot only without mechanistic dissection of how DPF3 regulates JAK2/STAT3\", \"Opposite (oncogenic) direction reported in renal cells, leaving tissue context unresolved\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Resolved how a germline risk SNP drives DPF3 in renal cancer, showing the variant creates an active enhancer HIF-binding motif that supports allele-specific HIF-driven DPF3 overexpression and oncogenic growth.\",\n      \"evidence\": \"Reporter/luciferase assays, eQTL analysis, allele-specific HIF ChIP in primary renal cells, ATAC-seq and CRISPR/siRNA DPF3 deletion with proliferation assays\",\n      \"pmids\": [\"34390653\", \"35148991\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct chromatin targets mediating DPF3's pro-growth effect not fully defined\", \"Single-lab functional system\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Defined an isoform-specific cytoplasmic-to-chromatin mechanism: DPF3a binds SNIP1 in a SMAD4–p300 complex to relieve repression of p300 HAT, activating TGF-β migration genes and driving metastasis.\",\n      \"evidence\": \"Co-IP of DPF3a with SNIP1/SMAD4/p300, HAT activity assay, histone-acetylation ChIP, ccRCC migration assays and in vivo metastasis model\",\n      \"pmids\": [\"35945219\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether DPF3a's PHD-reading versus protein-protein interaction drives SNIP1 binding not separated\", \"Generality beyond renal cancer not tested\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Revealed a non-canonical extranuclear function, placing DPF3 at centriolar satellites, centrosomes, spindle midzone and midbodies where it is required for kinetochore-microtubule stability, mitotic fidelity, and ciliogenesis.\",\n      \"evidence\": \"Immunofluorescence/live-cell imaging localization and siRNA/CRISPR loss-of-function with mitotic and axoneme-length phenotypes\",\n      \"pmids\": [\"38661008\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular partners at centrosome/midbody not identified\", \"How a chromatin-remodeling subunit is targeted to centriolar satellites is unknown\", \"Relationship between chromatin and mitotic/ciliary functions unresolved\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How DPF3 switches between its nuclear BAF chromatin role and its centrosomal/ciliary role, and what determines its opposing tumor-suppressive versus oncogenic outputs across tissues, remains open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of dual histone-mark recognition\", \"Centrosomal recruitment mechanism and partners unidentified\", \"Tissue-specific determinants of oncogenic versus suppressive DPF3 function undefined\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0042393\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [0, 2, 7]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [7]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [8]},\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [8]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [8]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-4839726\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [0, 2, 7]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [8]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [7]}\n    ],\n    \"complexes\": [\"BAF (SWI/SNF) chromatin remodeling complex\"],\n    \"partners\": [\"BRG1\", \"EBF2\", \"SNIP1\", \"SMAD4\", \"EP300\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":7,"faith_total":7,"faith_pct":100.0}}