{"gene":"SSPN","run_date":"2026-06-10T07:46:41","timeline":{"discoveries":[{"year":1996,"finding":"The human KRAG gene (SSPN) encodes a protein with hydrophobicity plots suggesting a structure closely resembling transmembrane 4 superfamily members; it is co-amplified with KRAS2 in tumors and maps to chromosome 12p11.2. Northern analysis confirmed high-level expression in muscle and evidence of alternate splicing.","method":"RT-PCR, hydrophobicity analysis, Northern blot, YAC mapping, multiplex PCR","journal":"Genomics","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — structural prediction plus expression analysis in a single study; no functional reconstitution or mutagenesis","pmids":["8661122"],"is_preprint":false},{"year":2004,"finding":"SSPN is expressed at the mRNA and protein level in smooth muscle and endothelial cells of human umbilical cord vessels, where it co-localizes with sarcoglycans and with dystrophin or utrophin, indicating it forms part of the sarcoglycan-sarcospan complex associated with both dystrophin and utrophin scaffolds in vascular cells.","method":"RT-PCR, immunofluorescence, co-localization microscopy","journal":"Journal of vascular research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, co-localization only (no co-IP or functional perturbation), no mechanistic follow-up","pmids":["15583476"],"is_preprint":false},{"year":2018,"finding":"Complete DNA methylation of the SSPN promoter suppresses SSPN gene expression, as demonstrated by a luciferase reporter assay in MCF7 cells, linking epigenetic silencing of SSPN to changes in adipose tissue distribution and glucose metabolism traits.","method":"Luciferase reporter assay with methylated SSPN promoter construct, pyrosequencing, genome-wide methylation/expression data","journal":"FASEB journal","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single reporter assay for the mechanistic claim; broader associations are correlative","pmids":["29932866"],"is_preprint":false}],"current_model":"SSPN (Sarcospan/KRAG) is a tetraspanin-like transmembrane protein that forms part of the sarcoglycan-sarcospan complex associated with dystrophin or utrophin scaffolds in muscle, vascular smooth muscle, and endothelial cells; its promoter is subject to DNA methylation-dependent silencing, and it was originally identified as co-amplified with KRAS2 at chromosome 12p11.2, but detailed mechanistic understanding of its molecular function remains limited."},"narrative":{"mechanistic_narrative":"SSPN (Sarcospan/KRAG) encodes a transmembrane protein whose hydrophobicity profile resembles tetraspanin (transmembrane 4 superfamily) members and is highly expressed in muscle; it was originally identified through co-amplification with KRAS2 at chromosome 12p11.2 [PMID:8661122]. In vascular cells, SSPN co-localizes with sarcoglycans and with dystrophin or utrophin, placing it within the sarcoglycan-sarcospan complex on both dystrophin and utrophin scaffolds [PMID:15583476]. SSPN expression is controlled epigenetically, with complete DNA methylation of its promoter suppressing transcription in a reporter assay [PMID:29932866]. Beyond these observations, the molecular function of SSPN has not been characterized in the available corpus.","teleology":[{"year":1996,"claim":"Established SSPN/KRAG as a candidate tetraspanin-like transmembrane protein and defined its genomic context and tissue expression, framing what kind of molecule it might be.","evidence":"RT-PCR, hydrophobicity analysis, Northern blot, and YAC/multiplex PCR mapping of the human KRAG locus","pmids":["8661122"],"confidence":"Medium","gaps":["Structure inferred from hydrophobicity prediction only, with no experimental membrane topology","No functional reconstitution or mutagenesis","Significance of co-amplification with KRAS2 not mechanistically resolved"]},{"year":2004,"claim":"Placed SSPN within the sarcoglycan-sarcospan complex in vascular cells by showing co-localization with sarcoglycans and dystrophin/utrophin, extending its complex membership beyond skeletal muscle.","evidence":"RT-PCR, immunofluorescence, and co-localization microscopy in human umbilical cord vessel smooth muscle and endothelial cells","pmids":["15583476"],"confidence":"Low","gaps":["Co-localization only, without co-IP or reciprocal physical validation","No functional perturbation establishing a role in the complex","Stoichiometry and direct binding partners undefined"]},{"year":2018,"claim":"Demonstrated epigenetic control of SSPN, showing that promoter DNA methylation silences expression and linking this to metabolic traits.","evidence":"Luciferase reporter assay with methylated SSPN promoter construct, pyrosequencing, and genome-wide methylation/expression data in MCF7 cells","pmids":["29932866"],"confidence":"Low","gaps":["Mechanistic claim rests on a single reporter assay; metabolic associations are correlative","Methylation-sensitive transcription factors at the promoter not identified","Causal link between SSPN silencing and adipose/glucose phenotypes not established"]},{"year":null,"claim":"The molecular activity of SSPN within the sarcoglycan-sarcospan complex remains undefined: how it contributes to complex assembly, scaffold stability, or signaling has not been determined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct binding assays defining SSPN interaction interfaces","No loss-of-function phenotype reported in the corpus","No structural model of the protein"]}],"mechanism_profile":{"molecular_activity":[],"localization":[{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[0,1]}],"pathway":[],"complexes":["sarcoglycan-sarcospan complex"],"partners":[],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q14714","full_name":"Sarcospan","aliases":["K-ras oncogene-associated protein","Kirsten-ras-associated protein"],"length_aa":243,"mass_kda":26.6,"function":"Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC","subcellular_location":"Cell membrane; Cell membrane, sarcolemma; Postsynaptic cell membrane","url":"https://www.uniprot.org/uniprotkb/Q14714/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SSPN","classification":"Not Classified","n_dependent_lines":10,"n_total_lines":1208,"dependency_fraction":0.008278145695364239},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/SSPN","total_profiled":1310},"omim":[{"mim_id":"608896","title":"SARCOGLYCAN, GAMMA; SGCG","url":"https://www.omim.org/entry/608896"},{"mim_id":"604149","title":"SARCOGLYCAN, EPSILON; SGCE","url":"https://www.omim.org/entry/604149"},{"mim_id":"601599","title":"SARCOSPAN; SSPN","url":"https://www.omim.org/entry/601599"},{"mim_id":"601411","title":"SARCOGLYCAN, DELTA; SGCD","url":"https://www.omim.org/entry/601411"},{"mim_id":"600119","title":"SARCOGLYCAN, ALPHA; SGCA","url":"https://www.omim.org/entry/600119"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nuclear membrane","reliability":"Approved"},{"location":"Nucleoplasm","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"tongue","ntpm":73.7}],"url":"https://www.proteinatlas.org/search/SSPN"},"hgnc":{"alias_symbol":["SPN1","SPN2"],"prev_symbol":["KRAG"]},"alphafold":{"accession":"Q14714","domains":[{"cath_id":"1.20.120","chopping":"49-153_183-221","consensus_level":"high","plddt":89.3634,"start":49,"end":221}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q14714","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q14714-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q14714-F1-predicted_aligned_error_v6.png","plddt_mean":74.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SSPN","jax_strain_url":"https://www.jax.org/strain/search?query=SSPN"},"sequence":{"accession":"Q14714","fasta_url":"https://rest.uniprot.org/uniprotkb/Q14714.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q14714/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q14714"}},"corpus_meta":[{"pmid":"21094070","id":"PMC_21094070","title":"Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.","date":"2010","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/21094070","citation_count":69,"is_preprint":false},{"pmid":"30448193","id":"PMC_30448193","title":"Supplemental parenteral nutrition improves immunity with unchanged carbohydrate and protein metabolism in critically ill patients: The SPN2 randomized tracer study.","date":"2018","source":"Clinical nutrition (Edinburgh, Scotland)","url":"https://pubmed.ncbi.nlm.nih.gov/30448193","citation_count":68,"is_preprint":false},{"pmid":"18086892","id":"PMC_18086892","title":"Spn1 regulates the recruitment of Spt6 and the Swi/Snf complex during transcriptional activation by RNA polymerase II.","date":"2007","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/18086892","citation_count":63,"is_preprint":false},{"pmid":"12524336","id":"PMC_12524336","title":"SPN1, a conserved gene identified by suppression of a postrecruitment-defective yeast TATA-binding protein mutant.","date":"2002","source":"Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/12524336","citation_count":40,"is_preprint":false},{"pmid":"21576362","id":"PMC_21576362","title":"Spn1 regulates the GNBP3-dependent Toll signaling pathway in Drosophila melanogaster.","date":"2011","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/21576362","citation_count":39,"is_preprint":false},{"pmid":"22768363","id":"PMC_22768363","title":"Complete genome sequence of the termite hindgut bacterium Spirochaeta coccoides type strain (SPN1(T)), reclassification in the genus Sphaerochaeta as Sphaerochaeta coccoides comb. nov. and emendations of the family Spirochaetaceae and the genus Sphaerochaeta.","date":"2012","source":"Standards in genomic sciences","url":"https://pubmed.ncbi.nlm.nih.gov/22768363","citation_count":37,"is_preprint":false},{"pmid":"8661122","id":"PMC_8661122","title":"Coamplification in tumors of KRAS2, type 2 inositol 1,4,5 triphosphate receptor gene, and a novel human gene, KRAG.","date":"1996","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/8661122","citation_count":35,"is_preprint":false},{"pmid":"32941642","id":"PMC_32941642","title":"The conserved elongation factor Spn1 is required for normal transcription, histone modifications, and splicing in Saccharomyces cerevisiae.","date":"2020","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/32941642","citation_count":28,"is_preprint":false},{"pmid":"29300974","id":"PMC_29300974","title":"The elongation factor Spn1 is a multi-functional chromatin binding protein.","date":"2018","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/29300974","citation_count":22,"is_preprint":false},{"pmid":"30566871","id":"PMC_30566871","title":"Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction.","date":"2018","source":"Cell reports","url":"https://pubmed.ncbi.nlm.nih.gov/30566871","citation_count":20,"is_preprint":false},{"pmid":"35595162","id":"PMC_35595162","title":"Spn1 and Its Dynamic Interactions with Spt6, Histones and Nucleosomes.","date":"2022","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/35595162","citation_count":13,"is_preprint":false},{"pmid":"15583476","id":"PMC_15583476","title":"Expression analysis of the SG-SSPN complex in smooth muscle and endothelial cells of human umbilical cord vessels.","date":"2004","source":"Journal of vascular research","url":"https://pubmed.ncbi.nlm.nih.gov/15583476","citation_count":13,"is_preprint":false},{"pmid":"32940805","id":"PMC_32940805","title":"The SSPN Score, a Novel Scoring System Incorporating PBRM1 Expression, Predicts Postoperative Recurrence for Patients with Non-metastatic Clear Cell Renal Cell Carcinoma.","date":"2020","source":"Annals of surgical oncology","url":"https://pubmed.ncbi.nlm.nih.gov/32940805","citation_count":13,"is_preprint":false},{"pmid":"35977387","id":"PMC_35977387","title":"Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in Saccharomyces cerevisiae.","date":"2022","source":"Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/35977387","citation_count":10,"is_preprint":false},{"pmid":"29932866","id":"PMC_29932866","title":"DNA methylation of SSPN is linked to adipose tissue distribution and glucose metabolism.","date":"2018","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/29932866","citation_count":9,"is_preprint":false},{"pmid":"30301740","id":"PMC_30301740","title":"Genome Instability Is Promoted by the Chromatin-Binding Protein Spn1 in Saccharomyces cerevisiae.","date":"2018","source":"Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/30301740","citation_count":6,"is_preprint":false},{"pmid":"39960479","id":"PMC_39960479","title":"The histone chaperone Spn1 preserves chromatin protections at promoters and nucleosome positioning in open reading frames.","date":"2025","source":"G3 (Bethesda, Md.)","url":"https://pubmed.ncbi.nlm.nih.gov/39960479","citation_count":5,"is_preprint":false},{"pmid":"40127868","id":"PMC_40127868","title":"Spt6-Spn1 interaction is required for RNA polymerase II association and precise nucleosome positioning along transcribed genes.","date":"2025","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/40127868","citation_count":3,"is_preprint":false},{"pmid":"38559248","id":"PMC_38559248","title":"THE HISTONE CHAPERONE SPN1 PRESERVES CHROMATIN PROTECTIONS AT PROMOTERS AND NUCLEOSOME POSITIONING IN OPEN READING FRAMES.","date":"2025","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/38559248","citation_count":2,"is_preprint":false},{"pmid":"26625290","id":"PMC_26625290","title":"Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex.","date":"2015","source":"Acta crystallographica. Section F, Structural biology communications","url":"https://pubmed.ncbi.nlm.nih.gov/26625290","citation_count":2,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.10.30.621040","title":"An integrative RNA spliceosomic landscape of pancreatic neuroendocrine tumors unveils novel clinicomolecular associations","date":"2024-11-03","source":"bioRxiv","url":"https://doi.org/10.1101/2024.10.30.621040","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2025.05.13.653749","title":"Localization and function of septins are susceptible to epitope tagging","date":"2025-05-14","source":"bioRxiv","url":"https://doi.org/10.1101/2025.05.13.653749","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.07.09.602728","title":"Septins function in exocytosis via physical interactions with the exocyst complex in fission yeast cytokinesis","date":"2024-07-12","source":"bioRxiv","url":"https://doi.org/10.1101/2024.07.09.602728","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":12974,"output_tokens":1486,"usd":0.030606,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7193,"output_tokens":1386,"usd":0.035307,"stage2_stop_reason":"end_turn"},"total_usd":0.065913,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"I need to carefully classify each paper before extracting discoveries.\n\n**Classification:**\n\nThe query gene SSPN (aliases: SPN1, SPN2, KRAG) could refer to multiple entities in this corpus:\n\n1. **SSPN = Sarcospan** (human muscle protein, tetraspanin-like) — papers 7, 12, 15 are about this\n2. **SPN1 = Spn1/Iws1** (yeast/eukaryotic transcription elongation factor/histone chaperone) — papers 1, 3, 4, 8, 9, 10, 11, 14, 16, 17, 18, 19 are about this\n3. **SPN1 = Drosophila serpin** — paper 5 (different protein, serpin superfamily — symbol collision with Drosophila Spn1 which is a serpin, NOT an ortholog of the transcription factor)\n4. **SPN2** = clinical nutrition trial — paper 2 (irrelevant)\n5. **SPN1(T)** = bacterial strain — paper 6 (irrelevant)\n6. **SSPN score** — paper 13 (irrelevant clinical scoring)\n7. **SPN1/SPN2/SPN3** = splicing groups in PanNETs — paper 21 (irrelevant)\n8. **Spn1/Spn4** = fission yeast septins — papers 22, 23 (symbol collision — fission yeast septins are structurally/functionally incompatible with the mammalian SSPN/Sarcospan or the budding yeast transcription factor Spn1)\n9. **CRM1-SPN1** in nuclear export — paper 20 (SPN1 here = Snurportin1, a nuclear import adapter for snRNPs — this is a different protein, SNUPN gene)\n\nThe HGNC aliases tell me SPN1, SPN2, KRAG all refer to the SAME gene as SSPN (Sarcospan). However, the bulk of papers about \"Spn1\" in yeast are about IWS1/Spn1, which is a different gene (human gene: IWS1). The yeast Spn1 transcription factor is the ortholog of human IWS1, NOT of human SSPN/Sarcospan.\n\nSo the canonical SSPN gene papers are: 7 (KRAG), 12 (SG-SSPN complex), 15 (SSPN methylation). Paper 20 is about Snurportin1 (SNUPN), not SSPN.\n\nPapers 1, 3, 4, 8, 9, 10, 11, 14, 16, 17, 18, 19 are about yeast Spn1/IWS1 — NOT the human SSPN/Sarcospan gene.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1996,\n      \"finding\": \"The human KRAG gene (SSPN) encodes a protein with hydrophobicity plots suggesting a structure closely resembling transmembrane 4 superfamily members; it is co-amplified with KRAS2 in tumors and maps to chromosome 12p11.2. Northern analysis confirmed high-level expression in muscle and evidence of alternate splicing.\",\n      \"method\": \"RT-PCR, hydrophobicity analysis, Northern blot, YAC mapping, multiplex PCR\",\n      \"journal\": \"Genomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — structural prediction plus expression analysis in a single study; no functional reconstitution or mutagenesis\",\n      \"pmids\": [\"8661122\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"SSPN is expressed at the mRNA and protein level in smooth muscle and endothelial cells of human umbilical cord vessels, where it co-localizes with sarcoglycans and with dystrophin or utrophin, indicating it forms part of the sarcoglycan-sarcospan complex associated with both dystrophin and utrophin scaffolds in vascular cells.\",\n      \"method\": \"RT-PCR, immunofluorescence, co-localization microscopy\",\n      \"journal\": \"Journal of vascular research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, co-localization only (no co-IP or functional perturbation), no mechanistic follow-up\",\n      \"pmids\": [\"15583476\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Complete DNA methylation of the SSPN promoter suppresses SSPN gene expression, as demonstrated by a luciferase reporter assay in MCF7 cells, linking epigenetic silencing of SSPN to changes in adipose tissue distribution and glucose metabolism traits.\",\n      \"method\": \"Luciferase reporter assay with methylated SSPN promoter construct, pyrosequencing, genome-wide methylation/expression data\",\n      \"journal\": \"FASEB journal\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single reporter assay for the mechanistic claim; broader associations are correlative\",\n      \"pmids\": [\"29932866\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SSPN (Sarcospan/KRAG) is a tetraspanin-like transmembrane protein that forms part of the sarcoglycan-sarcospan complex associated with dystrophin or utrophin scaffolds in muscle, vascular smooth muscle, and endothelial cells; its promoter is subject to DNA methylation-dependent silencing, and it was originally identified as co-amplified with KRAS2 at chromosome 12p11.2, but detailed mechanistic understanding of its molecular function remains limited.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SSPN (Sarcospan/KRAG) encodes a transmembrane protein whose hydrophobicity profile resembles tetraspanin (transmembrane 4 superfamily) members and is highly expressed in muscle; it was originally identified through co-amplification with KRAS2 at chromosome 12p11.2 [#0]. In vascular cells, SSPN co-localizes with sarcoglycans and with dystrophin or utrophin, placing it within the sarcoglycan-sarcospan complex on both dystrophin and utrophin scaffolds [#1]. SSPN expression is controlled epigenetically, with complete DNA methylation of its promoter suppressing transcription in a reporter assay [#2]. Beyond these observations, the molecular function of SSPN has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 1996,\n      \"claim\": \"Established SSPN/KRAG as a candidate tetraspanin-like transmembrane protein and defined its genomic context and tissue expression, framing what kind of molecule it might be.\",\n      \"evidence\": \"RT-PCR, hydrophobicity analysis, Northern blot, and YAC/multiplex PCR mapping of the human KRAG locus\",\n      \"pmids\": [\"8661122\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Structure inferred from hydrophobicity prediction only, with no experimental membrane topology\",\n        \"No functional reconstitution or mutagenesis\",\n        \"Significance of co-amplification with KRAS2 not mechanistically resolved\"\n      ]\n    },\n    {\n      \"year\": 2004,\n      \"claim\": \"Placed SSPN within the sarcoglycan-sarcospan complex in vascular cells by showing co-localization with sarcoglycans and dystrophin/utrophin, extending its complex membership beyond skeletal muscle.\",\n      \"evidence\": \"RT-PCR, immunofluorescence, and co-localization microscopy in human umbilical cord vessel smooth muscle and endothelial cells\",\n      \"pmids\": [\"15583476\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Co-localization only, without co-IP or reciprocal physical validation\",\n        \"No functional perturbation establishing a role in the complex\",\n        \"Stoichiometry and direct binding partners undefined\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Demonstrated epigenetic control of SSPN, showing that promoter DNA methylation silences expression and linking this to metabolic traits.\",\n      \"evidence\": \"Luciferase reporter assay with methylated SSPN promoter construct, pyrosequencing, and genome-wide methylation/expression data in MCF7 cells\",\n      \"pmids\": [\"29932866\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Mechanistic claim rests on a single reporter assay; metabolic associations are correlative\",\n        \"Methylation-sensitive transcription factors at the promoter not identified\",\n        \"Causal link between SSPN silencing and adipose/glucose phenotypes not established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The molecular activity of SSPN within the sarcoglycan-sarcospan complex remains undefined: how it contributes to complex assembly, scaffold stability, or signaling has not been determined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No direct binding assays defining SSPN interaction interfaces\",\n        \"No loss-of-function phenotype reported in the corpus\",\n        \"No structural model of the protein\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [\"sarcoglycan-sarcospan complex\"],\n    \"partners\": [],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"tie","faith_supported":3,"faith_total":3,"faith_pct":100.0}}