{"gene":"SSR2","run_date":"2026-06-10T07:46:41","timeline":{"discoveries":[{"year":1995,"finding":"Human SSR2 (beta-signal sequence receptor) encodes an endoplasmic reticulum membrane protein associated with protein translocation across the ER membrane, and is ubiquitously expressed across organs; the gene was mapped to chromosome bands 1q21→q23.","method":"cDNA cloning, Northern blot analysis, fluorescence in situ hybridization (FISH)","journal":"Cytogenetics and cell genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — cDNA isolation with chromosomal mapping and expression analysis; functional annotation derived from homology to canine beta-SSR, single lab","pmids":["7789174"],"is_preprint":false},{"year":2020,"finding":"SSR2 knockdown in HCC cells suppresses epithelial-mesenchymal transition (EMT), reducing migration and invasion, as demonstrated by downregulation of EMT-related proteins detected by Western blot.","method":"siRNA knockdown, Western blot for EMT markers, transwell migration/invasion assay","journal":"Journal of Cancer","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — loss-of-function with defined cellular phenotype (EMT suppression) and protein-level readout, single lab with two orthogonal assay types","pmids":["32913453"],"is_preprint":false},{"year":2024,"finding":"SSR2 inhibits Yes-associated protein (YAP) phosphorylation and promotes transcription of downstream Hippo signaling genes, thereby conferring cisplatin resistance in HCC cells; a Hippo pathway inhibitor can suppress the colony formation and tumorigenesis driven by SSR2 upregulation.","method":"Western blot, luciferase reporter assay, colony formation assay, in vivo xenograft model, pharmacological inhibition","journal":"Frontiers in bioscience (Landmark edition)","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — pathway placement via reporter assay and pharmacological rescue, single lab, multiple orthogonal methods","pmids":["39206890"],"is_preprint":false},{"year":2026,"finding":"SSR2 physically interacts with glutathione peroxidase 4 (GPX4) and increases GPX4 catalytic activity, thereby suppressing ferroptosis and promoting sorafenib resistance in HCC cells; induction of ferroptosis reverses the pro-resistance effect of SSR2 overexpression.","method":"Co-immunoprecipitation (CoIP), MTT assay, colony formation assay, ferroptosis induction rescue experiment","journal":"Current molecular medicine","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — reciprocal Co-IP establishing protein-protein interaction and functional rescue experiment, but single lab and no in vitro reconstitution of GPX4 activation","pmids":["41568502"],"is_preprint":false},{"year":2025,"finding":"SSR2 is a direct target of A-to-I RNA edited miR-3167 (but not wild-type miR-3167) in lung adenocarcinoma; SSR2 promotes tumor progression by inactivating Hippo signaling, and edited miR-3167 exerts antitumor activity by downregulating SSR2 and thereby activating Hippo signaling.","method":"Dual-luciferase reporter assay, RT-qPCR, Western blot, Transwell assay, CCK-8, flow cytometry","journal":"Molecular carcinogenesis","confidence":"Low","confidence_rationale":"Tier 3 / Weak — luciferase reporter confirms direct miRNA targeting and pathway-level readout, but single lab, single study, and Hippo link is inferred rather than directly reconstituted","pmids":["40632000"],"is_preprint":false}],"current_model":"SSR2 (signal sequence receptor subunit 2 / TRAPB) is an ER membrane protein involved in protein translocation; in cancer cells it promotes tumor progression by suppressing Hippo signaling (via inhibition of YAP phosphorylation), interacting with and enhancing the catalytic activity of the ferroptosis regulator GPX4 to suppress ferroptosis and confer sorafenib resistance, and facilitating epithelial-mesenchymal transition."},"narrative":{"mechanistic_narrative":"SSR2 (beta-signal sequence receptor / TRAPB) is a ubiquitously expressed endoplasmic reticulum membrane protein originally characterized as a component of the machinery for protein translocation across the ER membrane [PMID:7789174]. Beyond this constitutive role, the available corpus characterizes SSR2 predominantly as a driver of tumor progression. In hepatocellular carcinoma cells, SSR2 promotes epithelial-mesenchymal transition, enhancing migration and invasion [PMID:32913453], and inhibits YAP phosphorylation to activate transcription of downstream Hippo pathway genes, conferring cisplatin resistance that is reversed by pharmacological Hippo inhibition [PMID:39206890]. SSR2 also physically interacts with the ferroptosis regulator GPX4 and increases its catalytic activity, thereby suppressing ferroptosis and conferring sorafenib resistance [PMID:41568502]. The pro-tumor activity of SSR2 through Hippo inactivation is also observed in lung adenocarcinoma, where SSR2 is a direct target of A-to-I edited miR-3167 [PMID:40632000]. The structural basis by which SSR2 modulates YAP phosphorylation or activates GPX4 has not been reconstituted in the available corpus.","teleology":[{"year":1995,"claim":"Established the molecular identity of human SSR2 as an ER membrane protein linked to protein translocation, providing the baseline annotation against which later cancer roles are interpreted.","evidence":"cDNA cloning, Northern blot expression profiling, and FISH chromosomal mapping to 1q21→q23","pmids":["7789174"],"confidence":"Medium","gaps":["Translocation function inferred by homology to canine beta-SSR rather than direct biochemical assay","No defined interaction with translocon components in human cells","No connection to disease at this stage"]},{"year":2020,"claim":"Tied SSR2 to a cancer-relevant cellular phenotype by showing it is required for EMT, migration, and invasion in HCC.","evidence":"siRNA knockdown with EMT-marker Western blot and transwell migration/invasion assays in HCC cells","pmids":["32913453"],"confidence":"Medium","gaps":["Molecular mechanism linking SSR2 to EMT markers not defined","Single lab, single tumor type","No in vivo confirmation of invasion phenotype"]},{"year":2024,"claim":"Placed SSR2 upstream of the Hippo pathway by showing it suppresses YAP phosphorylation to drive downstream transcription and chemoresistance.","evidence":"Western blot, luciferase reporter, colony formation, xenograft model, and pharmacological Hippo inhibition in HCC","pmids":["39206890"],"confidence":"Medium","gaps":["Direct mechanism by which SSR2 affects the kinase cascade controlling YAP phosphorylation unknown","No physical interaction with Hippo components shown","Single lab"]},{"year":2026,"claim":"Identified a direct protein partner and a second resistance axis, showing SSR2 binds GPX4 and enhances its activity to suppress ferroptosis.","evidence":"Reciprocal Co-IP, MTT, colony formation, and ferroptosis-induction rescue in HCC cells","pmids":["41568502"],"confidence":"Medium","gaps":["No in vitro reconstitution demonstrating SSR2-dependent activation of GPX4 catalysis","Single lab","Structural basis of the SSR2–GPX4 interaction unknown"]},{"year":2025,"claim":"Extended the SSR2–Hippo axis to lung adenocarcinoma and identified A-to-I edited miR-3167 as an upstream regulator that downregulates SSR2.","evidence":"Dual-luciferase reporter, RT-qPCR, Western blot, transwell, CCK-8, and flow cytometry in lung adenocarcinoma","pmids":["40632000"],"confidence":"Low","gaps":["Hippo link inferred from pathway readouts rather than directly reconstituted","Single lab, single study","Mechanism of SSR2-mediated Hippo inactivation not resolved"]},{"year":null,"claim":"How SSR2's ER translocation role mechanistically connects to its cytoplasmic regulation of YAP phosphorylation and GPX4 activity remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural model of SSR2 in either translocation or signaling contexts","No reconstitution of SSR2-dependent GPX4 activation or YAP regulation","Whether the ER role and tumor signaling roles are mechanistically linked is unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[2,3]}],"localization":[{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[2,4]},{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[3]}],"complexes":[],"partners":["GPX4"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P43308","full_name":"Translocon-associated protein subunit beta","aliases":["Signal sequence receptor subunit beta","SSR-beta"],"length_aa":183,"mass_kda":20.1,"function":"TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins","subcellular_location":"Endoplasmic reticulum membrane","url":"https://www.uniprot.org/uniprotkb/P43308/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SSR2","classification":"Not Classified","n_dependent_lines":162,"n_total_lines":1208,"dependency_fraction":0.13410596026490065},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/SSR2","total_profiled":1310},"omim":[{"mim_id":"612374","title":"STIMULATOR OF INTERFERON RESPONSE cGAMP INTERACTOR 1; STING1","url":"https://www.omim.org/entry/612374"},{"mim_id":"606213","title":"SIGNAL SEQUENCE RECEPTOR, GAMMA; SSR3","url":"https://www.omim.org/entry/606213"},{"mim_id":"600867","title":"SIGNAL SEQUENCE RECEPTOR, BETA; SSR2","url":"https://www.omim.org/entry/600867"},{"mim_id":"300090","title":"SIGNAL SEQUENCE RECEPTOR, DELTA; SSR4","url":"https://www.omim.org/entry/300090"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/SSR2"},"hgnc":{"alias_symbol":["TLAP","TRAPB"],"prev_symbol":[]},"alphafold":{"accession":"P43308","domains":[{"cath_id":"2.60.40.10","chopping":"17-134","consensus_level":"medium","plddt":94.3354,"start":17,"end":134},{"cath_id":"-","chopping":"145-172","consensus_level":"high","plddt":94.85,"start":145,"end":172}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P43308","model_url":"https://alphafold.ebi.ac.uk/files/AF-P43308-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P43308-F1-predicted_aligned_error_v6.png","plddt_mean":91.81},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SSR2","jax_strain_url":"https://www.jax.org/strain/search?query=SSR2"},"sequence":{"accession":"P43308","fasta_url":"https://rest.uniprot.org/uniprotkb/P43308.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P43308/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P43308"}},"corpus_meta":[{"pmid":"33485374","id":"PMC_33485374","title":"Long noncoding RNA SNHG14 promotes hepatocellular carcinoma progression by regulating miR-876-5p/SSR2 axis.","date":"2021","source":"Journal of experimental & clinical cancer research : CR","url":"https://pubmed.ncbi.nlm.nih.gov/33485374","citation_count":32,"is_preprint":false},{"pmid":"12675130","id":"PMC_12675130","title":"SSR2(a) receptor expression and adrenergic/cholinergic characteristics in differentiated SH-SY5Y cells.","date":"2003","source":"Neurochemical research","url":"https://pubmed.ncbi.nlm.nih.gov/12675130","citation_count":25,"is_preprint":false},{"pmid":"32913453","id":"PMC_32913453","title":"SSR2 overexpression associates with tumorigenesis and metastasis of Hepatocellular Carcinoma through modulating EMT.","date":"2020","source":"Journal of Cancer","url":"https://pubmed.ncbi.nlm.nih.gov/32913453","citation_count":18,"is_preprint":false},{"pmid":"34306333","id":"PMC_34306333","title":"RP11-874J12.4, a novel lncRNA, confers chemoresistance in human gastric cancer cells by sponging miR-3972 and upregulating SSR2 expression.","date":"2021","source":"American journal of translational research","url":"https://pubmed.ncbi.nlm.nih.gov/34306333","citation_count":12,"is_preprint":false},{"pmid":"7789174","id":"PMC_7789174","title":"Isolation and mapping of the human beta-signal sequence receptor gene (SSR2).","date":"1995","source":"Cytogenetics and cell genetics","url":"https://pubmed.ncbi.nlm.nih.gov/7789174","citation_count":8,"is_preprint":false},{"pmid":"39206890","id":"PMC_39206890","title":"Downregulation of SSR2 Enhances Hepatocellular Carcinoma Cisplatin Sensitivity via the Hippo Pathway.","date":"2024","source":"Frontiers in bioscience (Landmark edition)","url":"https://pubmed.ncbi.nlm.nih.gov/39206890","citation_count":5,"is_preprint":false},{"pmid":"38641575","id":"PMC_38641575","title":"F127-SE-tLAP thermosensitive hydrogel alleviates bleomycin-induced skin fibrosis via TGF-β/Smad pathway.","date":"2024","source":"Molecular medicine (Cambridge, Mass.)","url":"https://pubmed.ncbi.nlm.nih.gov/38641575","citation_count":2,"is_preprint":false},{"pmid":"40632000","id":"PMC_40632000","title":"A-to-I RNA Edited miR-3167 Restrains Malignant Behaviors of Lung Adenocarcinoma by Influencing SSR2-Meditated Hippo Signaling.","date":"2025","source":"Molecular carcinogenesis","url":"https://pubmed.ncbi.nlm.nih.gov/40632000","citation_count":0,"is_preprint":false},{"pmid":"41979818","id":"PMC_41979818","title":"Exploration of the roles of SSR2 in hepatocellular carcinogenesis based on single-cell transcriptomics and spatial transcriptomics.","date":"2026","source":"Discover oncology","url":"https://pubmed.ncbi.nlm.nih.gov/41979818","citation_count":0,"is_preprint":false},{"pmid":"41568502","id":"PMC_41568502","title":"SSR2 Promotes Sorafenib Resistance Via Interacting with GPX4 to Inhibit Ferroptosis.","date":"2026","source":"Current molecular medicine","url":"https://pubmed.ncbi.nlm.nih.gov/41568502","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7581,"output_tokens":1205,"usd":0.020409,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7864,"output_tokens":2073,"usd":0.045573,"stage2_stop_reason":"end_turn"},"total_usd":0.065982,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1995,\n      \"finding\": \"Human SSR2 (beta-signal sequence receptor) encodes an endoplasmic reticulum membrane protein associated with protein translocation across the ER membrane, and is ubiquitously expressed across organs; the gene was mapped to chromosome bands 1q21→q23.\",\n      \"method\": \"cDNA cloning, Northern blot analysis, fluorescence in situ hybridization (FISH)\",\n      \"journal\": \"Cytogenetics and cell genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — cDNA isolation with chromosomal mapping and expression analysis; functional annotation derived from homology to canine beta-SSR, single lab\",\n      \"pmids\": [\"7789174\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"SSR2 knockdown in HCC cells suppresses epithelial-mesenchymal transition (EMT), reducing migration and invasion, as demonstrated by downregulation of EMT-related proteins detected by Western blot.\",\n      \"method\": \"siRNA knockdown, Western blot for EMT markers, transwell migration/invasion assay\",\n      \"journal\": \"Journal of Cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — loss-of-function with defined cellular phenotype (EMT suppression) and protein-level readout, single lab with two orthogonal assay types\",\n      \"pmids\": [\"32913453\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"SSR2 inhibits Yes-associated protein (YAP) phosphorylation and promotes transcription of downstream Hippo signaling genes, thereby conferring cisplatin resistance in HCC cells; a Hippo pathway inhibitor can suppress the colony formation and tumorigenesis driven by SSR2 upregulation.\",\n      \"method\": \"Western blot, luciferase reporter assay, colony formation assay, in vivo xenograft model, pharmacological inhibition\",\n      \"journal\": \"Frontiers in bioscience (Landmark edition)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — pathway placement via reporter assay and pharmacological rescue, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"39206890\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"SSR2 physically interacts with glutathione peroxidase 4 (GPX4) and increases GPX4 catalytic activity, thereby suppressing ferroptosis and promoting sorafenib resistance in HCC cells; induction of ferroptosis reverses the pro-resistance effect of SSR2 overexpression.\",\n      \"method\": \"Co-immunoprecipitation (CoIP), MTT assay, colony formation assay, ferroptosis induction rescue experiment\",\n      \"journal\": \"Current molecular medicine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — reciprocal Co-IP establishing protein-protein interaction and functional rescue experiment, but single lab and no in vitro reconstitution of GPX4 activation\",\n      \"pmids\": [\"41568502\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"SSR2 is a direct target of A-to-I RNA edited miR-3167 (but not wild-type miR-3167) in lung adenocarcinoma; SSR2 promotes tumor progression by inactivating Hippo signaling, and edited miR-3167 exerts antitumor activity by downregulating SSR2 and thereby activating Hippo signaling.\",\n      \"method\": \"Dual-luciferase reporter assay, RT-qPCR, Western blot, Transwell assay, CCK-8, flow cytometry\",\n      \"journal\": \"Molecular carcinogenesis\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — luciferase reporter confirms direct miRNA targeting and pathway-level readout, but single lab, single study, and Hippo link is inferred rather than directly reconstituted\",\n      \"pmids\": [\"40632000\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SSR2 (signal sequence receptor subunit 2 / TRAPB) is an ER membrane protein involved in protein translocation; in cancer cells it promotes tumor progression by suppressing Hippo signaling (via inhibition of YAP phosphorylation), interacting with and enhancing the catalytic activity of the ferroptosis regulator GPX4 to suppress ferroptosis and confer sorafenib resistance, and facilitating epithelial-mesenchymal transition.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SSR2 (beta-signal sequence receptor / TRAPB) is a ubiquitously expressed endoplasmic reticulum membrane protein originally characterized as a component of the machinery for protein translocation across the ER membrane [#0]. Beyond this constitutive role, the available corpus characterizes SSR2 predominantly as a driver of tumor progression. In hepatocellular carcinoma cells, SSR2 promotes epithelial-mesenchymal transition, enhancing migration and invasion [#1], and inhibits YAP phosphorylation to activate transcription of downstream Hippo pathway genes, conferring cisplatin resistance that is reversed by pharmacological Hippo inhibition [#2]. SSR2 also physically interacts with the ferroptosis regulator GPX4 and increases its catalytic activity, thereby suppressing ferroptosis and conferring sorafenib resistance [#3]. The pro-tumor activity of SSR2 through Hippo inactivation is also observed in lung adenocarcinoma, where SSR2 is a direct target of A-to-I edited miR-3167 [#4]. The structural basis by which SSR2 modulates YAP phosphorylation or activates GPX4 has not been reconstituted in the available corpus.\"\n,\n  \"teleology\": [\n    {\n      \"year\": 1995,\n      \"claim\": \"Established the molecular identity of human SSR2 as an ER membrane protein linked to protein translocation, providing the baseline annotation against which later cancer roles are interpreted.\",\n      \"evidence\": \"cDNA cloning, Northern blot expression profiling, and FISH chromosomal mapping to 1q21\\u2192q23\",\n      \"pmids\": [\"7789174\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Translocation function inferred by homology to canine beta-SSR rather than direct biochemical assay\",\n        \"No defined interaction with translocon components in human cells\",\n        \"No connection to disease at this stage\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Tied SSR2 to a cancer-relevant cellular phenotype by showing it is required for EMT, migration, and invasion in HCC.\",\n      \"evidence\": \"siRNA knockdown with EMT-marker Western blot and transwell migration/invasion assays in HCC cells\",\n      \"pmids\": [\"32913453\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular mechanism linking SSR2 to EMT markers not defined\",\n        \"Single lab, single tumor type\",\n        \"No in vivo confirmation of invasion phenotype\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Placed SSR2 upstream of the Hippo pathway by showing it suppresses YAP phosphorylation to drive downstream transcription and chemoresistance.\",\n      \"evidence\": \"Western blot, luciferase reporter, colony formation, xenograft model, and pharmacological Hippo inhibition in HCC\",\n      \"pmids\": [\"39206890\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct mechanism by which SSR2 affects the kinase cascade controlling YAP phosphorylation unknown\",\n        \"No physical interaction with Hippo components shown\",\n        \"Single lab\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Identified a direct protein partner and a second resistance axis, showing SSR2 binds GPX4 and enhances its activity to suppress ferroptosis.\",\n      \"evidence\": \"Reciprocal Co-IP, MTT, colony formation, and ferroptosis-induction rescue in HCC cells\",\n      \"pmids\": [\"41568502\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No in vitro reconstitution demonstrating SSR2-dependent activation of GPX4 catalysis\",\n        \"Single lab\",\n        \"Structural basis of the SSR2\\u2013GPX4 interaction unknown\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Extended the SSR2\\u2013Hippo axis to lung adenocarcinoma and identified A-to-I edited miR-3167 as an upstream regulator that downregulates SSR2.\",\n      \"evidence\": \"Dual-luciferase reporter, RT-qPCR, Western blot, transwell, CCK-8, and flow cytometry in lung adenocarcinoma\",\n      \"pmids\": [\"40632000\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Hippo link inferred from pathway readouts rather than directly reconstituted\",\n        \"Single lab, single study\",\n        \"Mechanism of SSR2-mediated Hippo inactivation not resolved\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How SSR2's ER translocation role mechanistically connects to its cytoplasmic regulation of YAP phosphorylation and GPX4 activity remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural model of SSR2 in either translocation or signaling contexts\",\n        \"No reconstitution of SSR2-dependent GPX4 activation or YAP regulation\",\n        \"Whether the ER role and tumor signaling roles are mechanistically linked is unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [2, 4]},\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"GPX4\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"tie","faith_supported":4,"faith_total":4,"faith_pct":100.0}}