{"gene":"SCAND1","run_date":"2026-04-28T20:42:07","timeline":{"discoveries":[{"year":2006,"finding":"SCAND1 (RAZ1) forms a heterodimer with NY-REN-21 (a SCAN domain-containing zinc finger protein) through their SCAN domains, as identified by yeast two-hybrid and confirmed with recombinant proteins. The NY-REN-21/SCAND1 heterodimer is asymmetric regarding the DNA binding region, since SCAND1 lacks the zinc finger region.","method":"Yeast two-hybrid system and recombinant protein interaction assay","journal":"Biochemical and Biophysical Research Communications","confidence":"Medium","confidence_rationale":"Tier 2 — reciprocal confirmation with recombinant proteins, single lab, two orthogonal methods","pmids":["16540086"],"is_preprint":false},{"year":2003,"finding":"SCAND1 (SDP1) acts as a co-activator of PPARγ2-dependent gene transcription by interacting with PPARγ2 through its SCAN domain, even though PPARγ2 does not itself contain a SCAN domain. The SCAN domain was necessary but not sufficient for co-activation, indicating additional regions of SCAND1 contribute to transcriptional co-activation.","method":"Yeast two-hybrid, co-immunoprecipitation, transient transfection reporter assay, domain deletion analysis","journal":"The Biochemical Journal","confidence":"Medium","confidence_rationale":"Tier 2 — multiple methods (Y2H, reporter assay, domain mutants) in a single lab","pmids":["12444922"],"is_preprint":false},{"year":2002,"finding":"SCAND1 (RAZ1) protein localizes to the nucleus in a diffuse pattern, and the C-terminal SCAN-related domain is sufficient for nuclear localization, as shown by GFP fusion imaging.","method":"GFP fusion protein and fluorescence microscopy; deletion constructs","journal":"Gene","confidence":"Medium","confidence_rationale":"Tier 2 — direct localization experiment with deletion constructs defining the sufficient domain, single lab","pmids":["12383503"],"is_preprint":false},{"year":2022,"finding":"SCAND1 hetero-oligomerizes with the SCAN-zinc finger transcription factor MZF1, and both proteins are co-recruited to chromatin together with the heterochromatin protein HP1γ. SCAND1 overexpression reversed hybrid epithelial/mesenchymal status to an epithelial phenotype, suppressed tumor cell proliferation via reduction of the MAP3K-MEK-ERK signaling pathway, and inhibited migration and lymph node metastasis of prostate cancer cells in a mouse xenograft model.","method":"Co-immunoprecipitation (SCAND1/MZF1/HP1γ chromatin association), overexpression in DU-145 cells with phenotypic readouts (E-cadherin/β-catenin relocalization, Ki-67 staining, western blot for ERK pathway), mouse tumor xenograft model","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 — multiple orthogonal methods (Co-IP, functional overexpression, in vivo xenograft), single lab","pmids":["36552758"],"is_preprint":false}],"current_model":"SCAND1 is a nuclear SCAN domain-only protein (lacking zinc fingers) that functions as a transcriptional co-regulator: its SCAN domain mediates heterodimerization with SCAN-zinc finger proteins (including MZF1 and NY-REN-21) and with PPARγ2, enabling co-activation of PPARγ2-dependent transcription and co-repression of EMT driver genes in complex with MZF1 and HP1γ, thereby suppressing the MAP3K-MEK-ERK pathway, inhibiting prostate cancer cell proliferation, migration, and metastasis."},"narrative":{"teleology":[{"year":2002,"claim":"Establishing that SCAND1 is a nuclear protein and that its C-terminal SCAN-related domain is sufficient for nuclear targeting resolved the basic subcellular context in which this zinc-finger-less SCAN protein operates.","evidence":"GFP fusion imaging with deletion constructs in cultured cells","pmids":["12383503"],"confidence":"Medium","gaps":["Endogenous protein localization not confirmed by immunofluorescence with validated antibody","Whether SCAND1 associates with specific subnuclear compartments (e.g., heterochromatin foci) was not addressed"]},{"year":2003,"claim":"Demonstrating that SCAND1 physically interacts with PPARγ2 and co-activates PPARγ2-dependent transcription established SCAND1 as a transcriptional co-activator capable of engaging non-SCAN-domain partners, with the SCAN domain necessary but not sufficient for this function.","evidence":"Yeast two-hybrid, co-immunoprecipitation, transient transfection reporter assay, and domain deletion analysis","pmids":["12444922"],"confidence":"Medium","gaps":["The region(s) outside the SCAN domain required for co-activation were not mapped","Endogenous target genes co-regulated by SCAND1 and PPARγ2 were not identified","No structural or biophysical data on the SCAND1–PPARγ2 interface"]},{"year":2006,"claim":"Showing that SCAND1 heterodimerizes with the SCAN-zinc finger protein NY-REN-21 through their respective SCAN domains established the principle that SCAND1 forms asymmetric complexes (lacking its own DNA-binding module) that could modulate the transcriptional output of zinc finger partners.","evidence":"Yeast two-hybrid screen confirmed with recombinant protein interaction assay","pmids":["16540086"],"confidence":"Medium","gaps":["Functional consequence of the SCAND1–NY-REN-21 heterodimer on transcription was not tested","Genomic targets of NY-REN-21 that might be modulated by SCAND1 were not identified"]},{"year":2022,"claim":"Revealing that SCAND1 co-associates with MZF1 and HP1γ on chromatin to repress EMT genes and suppress the MAP3K–MEK–ERK pathway provided the first in vivo functional context—tumor suppression in prostate cancer—and linked SCAND1's heterodimer-mediated co-repression to a defined signaling outcome.","evidence":"Co-immunoprecipitation of SCAND1/MZF1/HP1γ, overexpression phenotypic assays in DU-145 cells, and mouse xenograft metastasis model","pmids":["36552758"],"confidence":"Medium","gaps":["Direct genomic binding sites (e.g., ChIP-seq) of the SCAND1–MZF1–HP1γ complex were not mapped","Loss-of-function (knockout/knockdown) validation of SCAND1's tumor-suppressive role was not reported","Whether the co-repressive function extends beyond prostate cancer contexts is unknown"]},{"year":null,"claim":"The direct genomic targets of SCAND1-containing complexes, the structural basis of SCAN-domain-mediated heterodimerization selectivity, and whether SCAND1 functions as a co-activator versus co-repressor in a partner-dependent manner remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No genome-wide binding data (ChIP-seq) for SCAND1","No structural model of any SCAND1 heterodimer","Whether co-activation (PPARγ2) and co-repression (MZF1/HP1γ) reflect distinct complexes or context-dependent mechanisms is unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[1,3]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1,3]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[3]}],"complexes":[],"partners":["MZF1","HP1Γ","NY-REN-21","PPARΓ2"],"other_free_text":[]},"mechanistic_narrative":"SCAND1 is a nuclear SCAN domain-only protein that lacks zinc finger regions and functions as a transcriptional co-regulator by heterodimerizing with SCAN domain-containing zinc finger transcription factors, including NY-REN-21 and MZF1, through its SCAN domain, thereby forming asymmetric complexes in which SCAND1 modulates the DNA-binding partner's transcriptional activity [PMID:16540086, PMID:36552758]. SCAND1 also interacts with PPARγ2 via its SCAN domain and co-activates PPARγ2-dependent transcription, with regions outside the SCAN domain additionally required for full co-activation [PMID:12444922]. In prostate cancer cells, SCAND1 associates with MZF1 and HP1γ on chromatin to co-repress epithelial–mesenchymal transition driver genes, suppress the MAP3K–MEK–ERK signaling axis, and inhibit proliferation, migration, and lymph node metastasis in xenograft models [PMID:36552758]."},"prefetch_data":{"uniprot":{"accession":"P57086","full_name":"SCAN domain-containing protein 1","aliases":[],"length_aa":179,"mass_kda":19.1,"function":"May regulate transcriptional activity","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/P57086/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SCAND1","classification":"Not Classified","n_dependent_lines":41,"n_total_lines":1208,"dependency_fraction":0.03394039735099338},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"SNRPA","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/SCAND1","total_profiled":1310},"omim":[{"mim_id":"610416","title":"SCAN DOMAIN-CONTAINING 1; SCAND1","url":"https://www.omim.org/entry/610416"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nuclear speckles","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/SCAND1"},"hgnc":{"alias_symbol":["SDP1","RAZ1"],"prev_symbol":[]},"alphafold":{"accession":"P57086","domains":[{"cath_id":"1.10.4020.10","chopping":"103-140","consensus_level":"medium","plddt":94.7089,"start":103,"end":140},{"cath_id":"-","chopping":"142-173","consensus_level":"medium","plddt":85.8984,"start":142,"end":173}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P57086","model_url":"https://alphafold.ebi.ac.uk/files/AF-P57086-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P57086-F1-predicted_aligned_error_v6.png","plddt_mean":70.0},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SCAND1","jax_strain_url":"https://www.jax.org/strain/search?query=SCAND1"},"sequence":{"accession":"P57086","fasta_url":"https://rest.uniprot.org/uniprotkb/P57086.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P57086/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P57086"}},"corpus_meta":[{"pmid":"25775518","id":"PMC_25775518","title":"Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies.","date":"2015","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/25775518","citation_count":133,"is_preprint":false},{"pmid":"25293755","id":"PMC_25293755","title":"Arabidopsis lipins, PDAT1 acyltransferase, and SDP1 triacylglycerol lipase synergistically direct fatty acids toward β-oxidation, thereby maintaining membrane lipid homeostasis.","date":"2014","source":"The Plant cell","url":"https://pubmed.ncbi.nlm.nih.gov/25293755","citation_count":129,"is_preprint":false},{"pmid":"11923319","id":"PMC_11923319","title":"Regulation of the Saccharomyces cerevisiae Slt2 kinase pathway by the stress-inducible Sdp1 dual specificity phosphatase.","date":"2002","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/11923319","citation_count":101,"is_preprint":false},{"pmid":"35401590","id":"PMC_35401590","title":"Suppression of SDP1 Improves Soybean Seed Composition by Increasing Oil and Reducing Undigestible Oligosaccharides.","date":"2022","source":"Frontiers in plant science","url":"https://pubmed.ncbi.nlm.nih.gov/35401590","citation_count":36,"is_preprint":false},{"pmid":"17495930","id":"PMC_17495930","title":"Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases.","date":"2007","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/17495930","citation_count":34,"is_preprint":false},{"pmid":"16540086","id":"PMC_16540086","title":"Spectroscopic characterization of the tumor antigen NY-REN-21 and identification of heterodimer formation with SCAND1.","date":"2006","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/16540086","citation_count":33,"is_preprint":false},{"pmid":"35720575","id":"PMC_35720575","title":"Suppression of Physaria fendleri SDP1 Increased Seed Oil and Hydroxy Fatty Acid Content While Maintaining Oil Biosynthesis Through Triacylglycerol Remodeling.","date":"2022","source":"Frontiers in plant science","url":"https://pubmed.ncbi.nlm.nih.gov/35720575","citation_count":21,"is_preprint":false},{"pmid":"31152796","id":"PMC_31152796","title":"A homolog of Arabidopsis SDP1 lipase in Nannochloropsis is involved in degradation of de novo-synthesized triacylglycerols in the endoplasmic reticulum.","date":"2019","source":"Biochimica et biophysica acta. Molecular and cell biology of lipids","url":"https://pubmed.ncbi.nlm.nih.gov/31152796","citation_count":18,"is_preprint":false},{"pmid":"36552758","id":"PMC_36552758","title":"SCAND1 Reverses Epithelial-to-Mesenchymal Transition (EMT) and Suppresses Prostate Cancer Growth and Migration.","date":"2022","source":"Cells","url":"https://pubmed.ncbi.nlm.nih.gov/36552758","citation_count":15,"is_preprint":false},{"pmid":"12444922","id":"PMC_12444922","title":"SDP1 is a peroxisome-proliferator-activated receptor gamma 2 co-activator that binds through its SCAN domain.","date":"2003","source":"The Biochemical journal","url":"https://pubmed.ncbi.nlm.nih.gov/12444922","citation_count":13,"is_preprint":false},{"pmid":"12383503","id":"PMC_12383503","title":"Characterization of the SCAN box encoding RAZ1 gene: analysis of cDNA transcripts, expression, and cellular localization.","date":"2002","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/12383503","citation_count":8,"is_preprint":false},{"pmid":"38642182","id":"PMC_38642182","title":"Developmental pleiotropy of SDP1 from seedling to mature stages in B. napus.","date":"2024","source":"Plant molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/38642182","citation_count":5,"is_preprint":false},{"pmid":"8904809","id":"PMC_8904809","title":"The raz1 mutant of Arabidopsis thaliana lacks the activity of a high-affinity amino acid transporter.","date":"1996","source":"Planta","url":"https://pubmed.ncbi.nlm.nih.gov/8904809","citation_count":5,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8145,"output_tokens":1074,"usd":0.020272},"stage2":{"model":"claude-opus-4-6","input_tokens":4302,"output_tokens":1593,"usd":0.092003},"total_usd":0.112275,"stage1_batch_id":"msgbatch_011rkcQdVV1RaFq9XhcG6df6","stage2_batch_id":"msgbatch_01RzgrJafdF4EWHhj5mNi6dh","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2006,\n      \"finding\": \"SCAND1 (RAZ1) forms a heterodimer with NY-REN-21 (a SCAN domain-containing zinc finger protein) through their SCAN domains, as identified by yeast two-hybrid and confirmed with recombinant proteins. The NY-REN-21/SCAND1 heterodimer is asymmetric regarding the DNA binding region, since SCAND1 lacks the zinc finger region.\",\n      \"method\": \"Yeast two-hybrid system and recombinant protein interaction assay\",\n      \"journal\": \"Biochemical and Biophysical Research Communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal confirmation with recombinant proteins, single lab, two orthogonal methods\",\n      \"pmids\": [\"16540086\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"SCAND1 (SDP1) acts as a co-activator of PPARγ2-dependent gene transcription by interacting with PPARγ2 through its SCAN domain, even though PPARγ2 does not itself contain a SCAN domain. The SCAN domain was necessary but not sufficient for co-activation, indicating additional regions of SCAND1 contribute to transcriptional co-activation.\",\n      \"method\": \"Yeast two-hybrid, co-immunoprecipitation, transient transfection reporter assay, domain deletion analysis\",\n      \"journal\": \"The Biochemical Journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — multiple methods (Y2H, reporter assay, domain mutants) in a single lab\",\n      \"pmids\": [\"12444922\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2002,\n      \"finding\": \"SCAND1 (RAZ1) protein localizes to the nucleus in a diffuse pattern, and the C-terminal SCAN-related domain is sufficient for nuclear localization, as shown by GFP fusion imaging.\",\n      \"method\": \"GFP fusion protein and fluorescence microscopy; deletion constructs\",\n      \"journal\": \"Gene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct localization experiment with deletion constructs defining the sufficient domain, single lab\",\n      \"pmids\": [\"12383503\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"SCAND1 hetero-oligomerizes with the SCAN-zinc finger transcription factor MZF1, and both proteins are co-recruited to chromatin together with the heterochromatin protein HP1γ. SCAND1 overexpression reversed hybrid epithelial/mesenchymal status to an epithelial phenotype, suppressed tumor cell proliferation via reduction of the MAP3K-MEK-ERK signaling pathway, and inhibited migration and lymph node metastasis of prostate cancer cells in a mouse xenograft model.\",\n      \"method\": \"Co-immunoprecipitation (SCAND1/MZF1/HP1γ chromatin association), overexpression in DU-145 cells with phenotypic readouts (E-cadherin/β-catenin relocalization, Ki-67 staining, western blot for ERK pathway), mouse tumor xenograft model\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (Co-IP, functional overexpression, in vivo xenograft), single lab\",\n      \"pmids\": [\"36552758\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SCAND1 is a nuclear SCAN domain-only protein (lacking zinc fingers) that functions as a transcriptional co-regulator: its SCAN domain mediates heterodimerization with SCAN-zinc finger proteins (including MZF1 and NY-REN-21) and with PPARγ2, enabling co-activation of PPARγ2-dependent transcription and co-repression of EMT driver genes in complex with MZF1 and HP1γ, thereby suppressing the MAP3K-MEK-ERK pathway, inhibiting prostate cancer cell proliferation, migration, and metastasis.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"SCAND1 is a nuclear SCAN domain-only protein that lacks zinc finger regions and functions as a transcriptional co-regulator by heterodimerizing with SCAN domain-containing zinc finger transcription factors, including NY-REN-21 and MZF1, through its SCAN domain, thereby forming asymmetric complexes in which SCAND1 modulates the DNA-binding partner's transcriptional activity [PMID:16540086, PMID:36552758]. SCAND1 also interacts with PPARγ2 via its SCAN domain and co-activates PPARγ2-dependent transcription, with regions outside the SCAN domain additionally required for full co-activation [PMID:12444922]. In prostate cancer cells, SCAND1 associates with MZF1 and HP1γ on chromatin to co-repress epithelial–mesenchymal transition driver genes, suppress the MAP3K–MEK–ERK signaling axis, and inhibit proliferation, migration, and lymph node metastasis in xenograft models [PMID:36552758].\",\n  \"teleology\": [\n    {\n      \"year\": 2002,\n      \"claim\": \"Establishing that SCAND1 is a nuclear protein and that its C-terminal SCAN-related domain is sufficient for nuclear targeting resolved the basic subcellular context in which this zinc-finger-less SCAN protein operates.\",\n      \"evidence\": \"GFP fusion imaging with deletion constructs in cultured cells\",\n      \"pmids\": [\"12383503\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Endogenous protein localization not confirmed by immunofluorescence with validated antibody\",\n        \"Whether SCAND1 associates with specific subnuclear compartments (e.g., heterochromatin foci) was not addressed\"\n      ]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"Demonstrating that SCAND1 physically interacts with PPARγ2 and co-activates PPARγ2-dependent transcription established SCAND1 as a transcriptional co-activator capable of engaging non-SCAN-domain partners, with the SCAN domain necessary but not sufficient for this function.\",\n      \"evidence\": \"Yeast two-hybrid, co-immunoprecipitation, transient transfection reporter assay, and domain deletion analysis\",\n      \"pmids\": [\"12444922\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The region(s) outside the SCAN domain required for co-activation were not mapped\",\n        \"Endogenous target genes co-regulated by SCAND1 and PPARγ2 were not identified\",\n        \"No structural or biophysical data on the SCAND1–PPARγ2 interface\"\n      ]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"Showing that SCAND1 heterodimerizes with the SCAN-zinc finger protein NY-REN-21 through their respective SCAN domains established the principle that SCAND1 forms asymmetric complexes (lacking its own DNA-binding module) that could modulate the transcriptional output of zinc finger partners.\",\n      \"evidence\": \"Yeast two-hybrid screen confirmed with recombinant protein interaction assay\",\n      \"pmids\": [\"16540086\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional consequence of the SCAND1–NY-REN-21 heterodimer on transcription was not tested\",\n        \"Genomic targets of NY-REN-21 that might be modulated by SCAND1 were not identified\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Revealing that SCAND1 co-associates with MZF1 and HP1γ on chromatin to repress EMT genes and suppress the MAP3K–MEK–ERK pathway provided the first in vivo functional context—tumor suppression in prostate cancer—and linked SCAND1's heterodimer-mediated co-repression to a defined signaling outcome.\",\n      \"evidence\": \"Co-immunoprecipitation of SCAND1/MZF1/HP1γ, overexpression phenotypic assays in DU-145 cells, and mouse xenograft metastasis model\",\n      \"pmids\": [\"36552758\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct genomic binding sites (e.g., ChIP-seq) of the SCAND1–MZF1–HP1γ complex were not mapped\",\n        \"Loss-of-function (knockout/knockdown) validation of SCAND1's tumor-suppressive role was not reported\",\n        \"Whether the co-repressive function extends beyond prostate cancer contexts is unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The direct genomic targets of SCAND1-containing complexes, the structural basis of SCAN-domain-mediated heterodimerization selectivity, and whether SCAND1 functions as a co-activator versus co-repressor in a partner-dependent manner remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No genome-wide binding data (ChIP-seq) for SCAND1\",\n        \"No structural model of any SCAND1 heterodimer\",\n        \"Whether co-activation (PPARγ2) and co-repression (MZF1/HP1γ) reflect distinct complexes or context-dependent mechanisms is unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [1, 3]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0074160\", \"supporting_discovery_ids\": [1, 3]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"MZF1\", \"HP1γ\", \"NY-REN-21\", \"PPARγ2\"],\n    \"other_free_text\": []\n  }\n}\n```"}