{"gene":"SCAND1","run_date":"2026-06-13T19:06:35","timeline":{"discoveries":[{"year":2000,"finding":"RAZ1 (SCAND1) was identified as a binding partner of the MZF1B SCAN box domain via yeast two-hybrid screen of a bone marrow cDNA library. Co-immunoprecipitation assays demonstrated that the SCAN box domain of MZF1B is necessary for association with RAZ1. The carboxyl terminus of RAZ1 is sufficient for interaction with the MZF1B SCAN box. Additionally, both MZF1B and RAZ1 self-associate in vitro via a SCAN box-dependent mechanism, establishing the SCAN box as a protein interaction domain mediating both hetero- and homoprotein associations.","method":"Yeast two-hybrid screen, co-immunoprecipitation, in vitro self-association assay","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP combined with yeast two-hybrid and domain-deletion mapping, replicated with multiple orthogonal methods in a single rigorous study","pmids":["10777584"],"is_preprint":false},{"year":2002,"finding":"RAZ1 (SCAND1) protein localizes to the nucleus in a diffuse pattern when fused to GFP, and the carboxyl terminus containing the SCAN-related domain is sufficient for nuclear localization. The gene produces two transcripts with variant 5'-UTRs but identical ORFs encoding a 28 kDa protein.","method":"GFP fusion live-cell imaging, in vitro transcription/translation, Northern blot, primer extension","journal":"Gene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct subcellular localization by GFP imaging with domain-deletion evidence, single lab, two orthogonal methods","pmids":["12383503"],"is_preprint":false},{"year":2006,"finding":"SCAND1 forms a heterodimer with the SCAN domain protein NY-REN-21, identified by yeast two-hybrid and confirmed with recombinant proteins. The NY-REN-21/SCAND1 heterodimer is asymmetric with respect to the DNA binding region, since SCAND1 lacks zinc finger motifs, indicating SCAND1 can modulate the DNA-binding activity of partner SCAN-zinc finger proteins.","method":"Yeast two-hybrid, recombinant protein interaction assay, spectroscopic characterization","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — yeast two-hybrid confirmed by recombinant protein assay, two orthogonal methods, single lab","pmids":["16540086"],"is_preprint":false},{"year":2022,"finding":"SCAND1 hetero-oligomerizes with MZF1 and together they co-occupy chromatin with heterochromatin protein HP1γ. Overexpression of SCAND1 in DU-145 prostate cancer cells reversed hybrid epithelial/mesenchymal status to an epithelial phenotype (restoring E-cadherin and β-catenin localization), suppressed cell proliferation by reducing MAP3K-MEK-ERK signaling, and inhibited migration and lymph node metastasis in a mouse xenograft model. SCAND1 and MZF1 were mutually inducible.","method":"Overexpression in cell lines, chromatin co-occupancy assay with HP1γ, western blot for EMT markers, mouse tumor xenograft with Ki-67/Vimentin IHC, migration assay","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo xenograft plus multiple cellular assays and chromatin data, single lab, several orthogonal methods","pmids":["36552758"],"is_preprint":false}],"current_model":"SCAND1 (RAZ1) is a nuclear SCAN domain-containing protein that lacks zinc finger motifs and functions primarily as a protein interaction module: its SCAN/SCAN-related domain mediates both homodimerization and heterodimerization with SCAN-zinc finger transcription factors (including MZF1B and NY-REN-21), enabling it to act as a transcriptional co-repressor by tethering partners such as MZF1 to heterochromatin (via HP1γ) and thereby repressing EMT-driver gene expression and the MAP3K-MEK-ERK proliferation pathway."},"narrative":{"mechanistic_narrative":"SCAND1 (RAZ1) is a nuclear SCAN domain-containing protein that functions as a protein-interaction module governing the activity of SCAN-zinc finger transcription factors [PMID:10777584, PMID:16540086]. Identified as a binding partner of the MZF1B SCAN box, SCAND1 uses its carboxyl-terminal SCAN-related domain to mediate both self-association and heterodimerization with SCAN-domain partners, and the same C-terminal region is sufficient for nuclear localization [PMID:10777584, PMID:12383503]. Because SCAND1 lacks zinc finger motifs, its heterodimer with the SCAN-zinc finger protein NY-REN-21 is asymmetric with respect to DNA binding, positioning SCAND1 to modulate the DNA-binding activity of partner transcription factors rather than to bind DNA directly [PMID:16540086]. In prostate cancer cells SCAND1 hetero-oligomerizes with MZF1 and co-occupies chromatin together with heterochromatin protein HP1γ; its overexpression reverses a hybrid epithelial/mesenchymal phenotype toward an epithelial state, suppresses MAP3K-MEK-ERK signaling and proliferation, and inhibits migration and lymph node metastasis in vivo, consistent with a co-repressor role exerted through SCAN-domain partners [PMID:36552758].","teleology":[{"year":2000,"claim":"Established that SCAND1 is a SCAN-box interaction partner, defining the SCAN domain as a module mediating both homo- and heterodimerization rather than a DNA-binding element.","evidence":"Yeast two-hybrid screen of bone marrow cDNA, reciprocal co-immunoprecipitation, and domain-deletion mapping with MZF1B; in vitro self-association","pmids":["10777584"],"confidence":"High","gaps":["Does not establish a transcriptional output of the SCAND1–MZF1B interaction","Functional consequence of self-association unresolved","No structural model of the dimerization interface"]},{"year":2002,"claim":"Localized SCAND1 to the nucleus and mapped nuclear targeting to the C-terminal SCAN-related domain, indicating where the protein exerts its interaction function.","evidence":"GFP-fusion live-cell imaging with domain deletions, in vitro transcription/translation, Northern blot and primer extension","pmids":["12383503"],"confidence":"Medium","gaps":["Diffuse nuclear pattern does not resolve chromatin versus nucleoplasmic distribution","No identified nuclear import mechanism","Single lab"]},{"year":2006,"claim":"Showed SCAND1 forms an asymmetric DNA-binding-deficient heterodimer with NY-REN-21, providing the biochemical basis for SCAND1 acting as a regulator of partner DNA-binding activity.","evidence":"Yeast two-hybrid, recombinant protein interaction assay, and spectroscopic characterization","pmids":["16540086"],"confidence":"Medium","gaps":["Effect on NY-REN-21 target gene occupancy not measured","Stoichiometry of the heterodimer in cells not determined","Single lab, in vitro"]},{"year":2022,"claim":"Connected SCAND1's interaction biochemistry to a cellular phenotype by showing it tethers MZF1 to HP1γ-marked chromatin and represses EMT and proliferation programs in prostate cancer.","evidence":"Overexpression in DU-145 cells, chromatin co-occupancy with HP1γ, EMT-marker western blots, migration assays, and mouse xenograft with IHC","pmids":["36552758"],"confidence":"Medium","gaps":["Relies on overexpression; endogenous loss-of-function effect not tested","Direct target genes of the SCAND1–MZF1–HP1γ complex not mapped","Mechanistic link between chromatin co-occupancy and MAP3K-MEK-ERK suppression not resolved"]},{"year":null,"claim":"Whether SCAND1's repressive activity at endogenous loci and its full set of SCAN-zinc finger partners and direct target genes generalize beyond the prostate cancer model remains unknown.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No genome-wide map of SCAND1-dependent target genes","No loss-of-function or knockout phenotype in the corpus","Complete partner repertoire of SCAN-zinc finger factors uncharacterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[3]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,2]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[1]},{"term_id":"GO:0005694","term_label":"chromosome","supporting_discovery_ids":[3]}],"pathway":[{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[3]}],"complexes":[],"partners":["MZF1","NY-REN-21","CBX3"],"other_free_text":[]}},"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":"23741625","id":"PMC_23741625","title":"Exposure to Maternal Diabetes in Utero and DNA Methylation Patterns in the Offspring.","date":"2013","source":"Immunometabolism","url":"https://pubmed.ncbi.nlm.nih.gov/23741625","citation_count":48,"is_preprint":false},{"pmid":"18660489","id":"PMC_18660489","title":"Multiple genetic variants along candidate pathways influence plasma high-density lipoprotein cholesterol concentrations.","date":"2008","source":"Journal of lipid research","url":"https://pubmed.ncbi.nlm.nih.gov/18660489","citation_count":47,"is_preprint":false},{"pmid":"10777584","id":"PMC_10777584","title":"Identification of a novel SCAN box-related protein that interacts with MZF1B. The leucine-rich SCAN box mediates hetero- and homoprotein associations.","date":"2000","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/10777584","citation_count":46,"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":"19643593","id":"PMC_19643593","title":"Quantum dot immunoassays in renewable surface column and 96-well plate formats for the fluorescence detection of botulinum neurotoxin using high-affinity antibodies.","date":"2009","source":"Biosensors & bioelectronics","url":"https://pubmed.ncbi.nlm.nih.gov/19643593","citation_count":32,"is_preprint":false},{"pmid":"19381395","id":"PMC_19381395","title":"Renewable surface fluorescence sandwich immunoassay biosensor for rapid sensitive botulinum toxin detection in an automated fluidic format.","date":"2009","source":"The Analyst","url":"https://pubmed.ncbi.nlm.nih.gov/19381395","citation_count":19,"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":16,"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":"38116315","id":"PMC_38116315","title":"Impact of disulfidptosis-associated clusters on breast cancer survival rates and guiding personalized treatment.","date":"2023","source":"Frontiers in endocrinology","url":"https://pubmed.ncbi.nlm.nih.gov/38116315","citation_count":5,"is_preprint":false},{"pmid":"31819040","id":"PMC_31819040","title":"A computationally inspired in-vivo approach identifies a link between amygdalar transcriptional heterogeneity, socialization and anxiety.","date":"2019","source":"Translational psychiatry","url":"https://pubmed.ncbi.nlm.nih.gov/31819040","citation_count":5,"is_preprint":false},{"pmid":"41286944","id":"PMC_41286944","title":"Dynamic remodelling of epithelial plasticity in colorectal cancer from single-cell and spatially resolved perspectives.","date":"2025","source":"Journal of translational medicine","url":"https://pubmed.ncbi.nlm.nih.gov/41286944","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":16324,"output_tokens":2530,"usd":0.06479,"retried_sync":true},"stage2":{"model":"claude-opus-4-8","input_tokens":7861,"output_tokens":2017,"usd":0.044865,"stage2_stop_reason":"end_turn"},"total_usd":0.109655,"stage1_batch_id":"msgbatch_0147LFpL5iCPFZF66xp23BqC","stage2_batch_id":"msgbatch_01Crtwc6eCsZh1CrnfJhY7J7","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2000,\n      \"finding\": \"RAZ1 (SCAND1) was identified as a binding partner of the MZF1B SCAN box domain via yeast two-hybrid screen of a bone marrow cDNA library. Co-immunoprecipitation assays demonstrated that the SCAN box domain of MZF1B is necessary for association with RAZ1. The carboxyl terminus of RAZ1 is sufficient for interaction with the MZF1B SCAN box. Additionally, both MZF1B and RAZ1 self-associate in vitro via a SCAN box-dependent mechanism, establishing the SCAN box as a protein interaction domain mediating both hetero- and homoprotein associations.\",\n      \"method\": \"Yeast two-hybrid screen, co-immunoprecipitation, in vitro self-association assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP combined with yeast two-hybrid and domain-deletion mapping, replicated with multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"10777584\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2002,\n      \"finding\": \"RAZ1 (SCAND1) protein localizes to the nucleus in a diffuse pattern when fused to GFP, and the carboxyl terminus containing the SCAN-related domain is sufficient for nuclear localization. The gene produces two transcripts with variant 5'-UTRs but identical ORFs encoding a 28 kDa protein.\",\n      \"method\": \"GFP fusion live-cell imaging, in vitro transcription/translation, Northern blot, primer extension\",\n      \"journal\": \"Gene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct subcellular localization by GFP imaging with domain-deletion evidence, single lab, two orthogonal methods\",\n      \"pmids\": [\"12383503\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"SCAND1 forms a heterodimer with the SCAN domain protein NY-REN-21, identified by yeast two-hybrid and confirmed with recombinant proteins. The NY-REN-21/SCAND1 heterodimer is asymmetric with respect to the DNA binding region, since SCAND1 lacks zinc finger motifs, indicating SCAND1 can modulate the DNA-binding activity of partner SCAN-zinc finger proteins.\",\n      \"method\": \"Yeast two-hybrid, recombinant protein interaction assay, spectroscopic characterization\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — yeast two-hybrid confirmed by recombinant protein assay, two orthogonal methods, single lab\",\n      \"pmids\": [\"16540086\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"SCAND1 hetero-oligomerizes with MZF1 and together they co-occupy chromatin with heterochromatin protein HP1γ. Overexpression of SCAND1 in DU-145 prostate cancer cells reversed hybrid epithelial/mesenchymal status to an epithelial phenotype (restoring E-cadherin and β-catenin localization), suppressed cell proliferation by reducing MAP3K-MEK-ERK signaling, and inhibited migration and lymph node metastasis in a mouse xenograft model. SCAND1 and MZF1 were mutually inducible.\",\n      \"method\": \"Overexpression in cell lines, chromatin co-occupancy assay with HP1γ, western blot for EMT markers, mouse tumor xenograft with Ki-67/Vimentin IHC, migration assay\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo xenograft plus multiple cellular assays and chromatin data, single lab, several orthogonal methods\",\n      \"pmids\": [\"36552758\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SCAND1 (RAZ1) is a nuclear SCAN domain-containing protein that lacks zinc finger motifs and functions primarily as a protein interaction module: its SCAN/SCAN-related domain mediates both homodimerization and heterodimerization with SCAN-zinc finger transcription factors (including MZF1B and NY-REN-21), enabling it to act as a transcriptional co-repressor by tethering partners such as MZF1 to heterochromatin (via HP1γ) and thereby repressing EMT-driver gene expression and the MAP3K-MEK-ERK proliferation pathway.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SCAND1 (RAZ1) is a nuclear SCAN domain-containing protein that functions as a protein-interaction module governing the activity of SCAN-zinc finger transcription factors [#0, #2]. Identified as a binding partner of the MZF1B SCAN box, SCAND1 uses its carboxyl-terminal SCAN-related domain to mediate both self-association and heterodimerization with SCAN-domain partners, and the same C-terminal region is sufficient for nuclear localization [#0, #1]. Because SCAND1 lacks zinc finger motifs, its heterodimer with the SCAN-zinc finger protein NY-REN-21 is asymmetric with respect to DNA binding, positioning SCAND1 to modulate the DNA-binding activity of partner transcription factors rather than to bind DNA directly [#2]. In prostate cancer cells SCAND1 hetero-oligomerizes with MZF1 and co-occupies chromatin together with heterochromatin protein HP1\\u03b3; its overexpression reverses a hybrid epithelial/mesenchymal phenotype toward an epithelial state, suppresses MAP3K-MEK-ERK signaling and proliferation, and inhibits migration and lymph node metastasis in vivo, consistent with a co-repressor role exerted through SCAN-domain partners [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2000,\n      \"claim\": \"Established that SCAND1 is a SCAN-box interaction partner, defining the SCAN domain as a module mediating both homo- and heterodimerization rather than a DNA-binding element.\",\n      \"evidence\": \"Yeast two-hybrid screen of bone marrow cDNA, reciprocal co-immunoprecipitation, and domain-deletion mapping with MZF1B; in vitro self-association\",\n      \"pmids\": [\"10777584\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not establish a transcriptional output of the SCAND1\\u2013MZF1B interaction\",\n        \"Functional consequence of self-association unresolved\",\n        \"No structural model of the dimerization interface\"\n      ]\n    },\n    {\n      \"year\": 2002,\n      \"claim\": \"Localized SCAND1 to the nucleus and mapped nuclear targeting to the C-terminal SCAN-related domain, indicating where the protein exerts its interaction function.\",\n      \"evidence\": \"GFP-fusion live-cell imaging with domain deletions, in vitro transcription/translation, Northern blot and primer extension\",\n      \"pmids\": [\"12383503\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Diffuse nuclear pattern does not resolve chromatin versus nucleoplasmic distribution\",\n        \"No identified nuclear import mechanism\",\n        \"Single lab\"\n      ]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"Showed SCAND1 forms an asymmetric DNA-binding-deficient heterodimer with NY-REN-21, providing the biochemical basis for SCAND1 acting as a regulator of partner DNA-binding activity.\",\n      \"evidence\": \"Yeast two-hybrid, recombinant protein interaction assay, and spectroscopic characterization\",\n      \"pmids\": [\"16540086\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Effect on NY-REN-21 target gene occupancy not measured\",\n        \"Stoichiometry of the heterodimer in cells not determined\",\n        \"Single lab, in vitro\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Connected SCAND1's interaction biochemistry to a cellular phenotype by showing it tethers MZF1 to HP1\\u03b3-marked chromatin and represses EMT and proliferation programs in prostate cancer.\",\n      \"evidence\": \"Overexpression in DU-145 cells, chromatin co-occupancy with HP1\\u03b3, EMT-marker western blots, migration assays, and mouse xenograft with IHC\",\n      \"pmids\": [\"36552758\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Relies on overexpression; endogenous loss-of-function effect not tested\",\n        \"Direct target genes of the SCAND1\\u2013MZF1\\u2013HP1\\u03b3 complex not mapped\",\n        \"Mechanistic link between chromatin co-occupancy and MAP3K-MEK-ERK suppression not resolved\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether SCAND1's repressive activity at endogenous loci and its full set of SCAN-zinc finger partners and direct target genes generalize beyond the prostate cancer model remains unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No genome-wide map of SCAND1-dependent target genes\",\n        \"No loss-of-function or knockout phenotype in the corpus\",\n        \"Complete partner repertoire of SCAN-zinc finger factors uncharacterized\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005694\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"MZF1\", \"NY-REN-21\", \"CBX3\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":null}