{"gene":"MTPAP","run_date":"2026-06-10T05:19:51","timeline":{"discoveries":[{"year":2011,"finding":"Crystal structure of human PAPD1 (MTPAP) reveals palm and fingers domains forming an active site at their interface, with a large substrate-binding pocket. An N-terminal domain with RNP-type RNA-binding fold (named the RL domain) and a β-arm insertion in the palm domain mediate homodimerization. Mutagenesis and biochemical studies demonstrated that dimerization is required for catalytic activity.","method":"X-ray crystallography, active-site mutagenesis, biochemical activity assays","journal":"Molecular cell","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structure combined with mutagenesis and in vitro biochemical assays, multiple orthogonal methods in one rigorous study","pmids":["21292163"],"is_preprint":false},{"year":2015,"finding":"Crystal structures of mitochondrial PAP (mtPAP/MTPAP) reveal the structural basis for ATP selectivity over other nucleotides, and show an intricate dimerization interface featuring an RNA-recognition module formed through strand complementation. The N478D mutation (causing SPAX4) is structurally explained as drastically reducing poly(A) tail length on mitochondrial mRNAs.","method":"X-ray crystallography, structural analysis of disease-associated mutant","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 1 / Strong — high-resolution crystal structures with functional interpretation of disease mutation, rigorous structural analysis","pmids":["26319014"],"is_preprint":false},{"year":2019,"finding":"Pathogenic missense mutations in MTPAP (compound heterozygous p.Ile428Thr/p.Arg523Trp and homozygous p.Ile385Phe) cause shorter poly(A) tails on mitochondrial transcripts and altered mitochondrial protein expression in patient fibroblasts, establishing that MTPAP activity is required for normal polyadenylation of mitochondrially encoded mRNAs and mitochondrial protein synthesis.","method":"Mitochondrial poly(A) tail length analysis, de novo mitochondrial protein synthesis assay in patient fibroblasts","journal":"Neuropediatrics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct functional assays in patient-derived fibroblasts with two orthogonal methods (poly(A) analysis + protein synthesis), single lab","pmids":["31779033"],"is_preprint":false},{"year":2014,"finding":"Homozygous missense mutation in MTPAP causes cellular radiosensitivity characterized by delayed DNA double-strand break repair, increased reactive oxygen species (ROS), and increased apoptosis after ionizing radiation; wild-type MTPAP cDNA rescue abrogated radiosensitivity, and antioxidant pre-treatment (α-lipoic acid, N-acetylcysteine) rescued DNA repair and clonogenic survival defects, implicating ROS dysregulation as the pathogenic mechanism.","method":"Complementation with wild-type cDNA in MTPAP-deficient cell lines, clonogenic survival assay, γH2AX foci for DSB quantification, ROS measurement, antioxidant rescue experiment","journal":"Cell death & disease","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (rescue, clonogenic survival, DSB foci, ROS, pharmacological rescue), single lab","pmids":["24651433"],"is_preprint":false}],"current_model":"MTPAP (PAPD1/mtPAP) is a nuclear-encoded, noncanonical poly(A) polymerase that localizes to mitochondria and polyadenylates mitochondrial mRNAs to regulate their stability and expression; it functions as an obligate homodimer—with dimerization mediated by an N-terminal RL domain and a β-arm insertion forming an RNA-recognition module at the dimer interface—and selectively incorporates ATP via a structurally defined active-site pocket, while loss-of-function mutations truncate mitochondrial poly(A) tails, impair mitochondrial protein synthesis, disrupt ROS homeostasis, and cause neurodegenerative disease (SPAX4)."},"narrative":{"mechanistic_narrative":"MTPAP (PAPD1/mtPAP) is a noncanonical poly(A) polymerase that polyadenylates mitochondrially encoded mRNAs to support their stability and translation [PMID:31779033]. Structural and biochemical work established that it is catalytically active only as a homodimer: an N-terminal RNP-type RNA-binding fold (the RL domain) together with a β-arm insertion in the palm domain mediates dimerization, and dimerization is obligatory for activity [PMID:21292163]. High-resolution structures further defined the basis for selective ATP incorporation and revealed an RNA-recognition module assembled by strand complementation across the dimer interface, while structurally explaining how the SPAX4-causing N478D substitution shortens mitochondrial poly(A) tails [PMID:26319014]. Loss-of-function mutations truncate poly(A) tails on mitochondrial transcripts and impair de novo mitochondrial protein synthesis in patient fibroblasts [PMID:31779033], and a homozygous pathogenic mutation produces cellular radiosensitivity with delayed double-strand break repair, elevated ROS, and increased apoptosis that is rescued by wild-type cDNA and by antioxidant treatment, linking MTPAP dysfunction to ROS dysregulation [PMID:24651433]. Pathogenic MTPAP mutations cause the neurodegenerative disorder SPAX4 [PMID:26319014].","teleology":[{"year":2011,"claim":"The unknown question of how MTPAP achieves catalysis was answered by showing it is an obligate homodimer with a defined active site formed at the palm-fingers interface.","evidence":"X-ray crystallography of human PAPD1 with active-site mutagenesis and in vitro activity assays","pmids":["21292163"],"confidence":"High","gaps":["Does not establish RNA substrate specificity in vivo","Mechanism of substrate selection within the binding pocket not resolved"]},{"year":2015,"claim":"It was unclear how MTPAP discriminates ATP and how disease mutations impair function; structures revealed the basis for ATP selectivity and a dimer-interface RNA-recognition module, and explained the N478D SPAX4 mutation as shortening poly(A) tails.","evidence":"High-resolution crystal structures including structural analysis of the disease-associated mutant","pmids":["26319014"],"confidence":"High","gaps":["Structural snapshot does not capture catalytic cycle dynamics","Does not directly measure tail-length effects in patient tissue"]},{"year":2014,"claim":"The pathogenic mechanism downstream of MTPAP loss was addressed by linking deficiency to ROS-driven radiosensitivity and impaired DNA double-strand break repair, with antioxidant rescue identifying ROS dysregulation as causal.","evidence":"Wild-type cDNA complementation, clonogenic survival, γH2AX foci, ROS measurement, and antioxidant rescue in MTPAP-deficient cells","pmids":["24651433"],"confidence":"Medium","gaps":["Single lab","Mechanistic link between mitochondrial polyadenylation defect and nuclear DSB repair not fully resolved"]},{"year":2019,"claim":"Whether multiple distinct missense mutations converge on the same molecular defect was answered by showing diverse pathogenic alleles shorten mitochondrial poly(A) tails and alter mitochondrial protein synthesis.","evidence":"Mitochondrial poly(A) tail length analysis and de novo mitochondrial protein synthesis assays in patient fibroblasts","pmids":["31779033"],"confidence":"Medium","gaps":["Single lab","Transcript-specific consequences of tail shortening not delineated"]},{"year":null,"claim":"How shortened mitochondrial poly(A) tails mechanistically produce ROS dysregulation and neurodegeneration in SPAX4 remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No causal chain established from poly(A) defect to neuronal pathology","Transcript-level selectivity of MTPAP in vivo unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140098","term_label":"catalytic activity, acting on RNA","supporting_discovery_ids":[0,1,2]},{"term_id":"GO:0016740","term_label":"transferase activity","supporting_discovery_ids":[0,1]},{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[0,1]}],"localization":[{"term_id":"GO:0005739","term_label":"mitochondrion","supporting_discovery_ids":[1,2]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[2]}],"complexes":["MTPAP homodimer"],"partners":[],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9NVV4","full_name":"Poly(A) RNA polymerase, mitochondrial","aliases":["PAP-associated domain-containing protein 1","Polynucleotide adenylyltransferase","Terminal uridylyltransferase 1","TUTase 1","mtPAP"],"length_aa":582,"mass_kda":66.2,"function":"Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA","subcellular_location":"Cytoplasm; Mitochondrion","url":"https://www.uniprot.org/uniprotkb/Q9NVV4/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/MTPAP","classification":"Common Essential","n_dependent_lines":917,"n_total_lines":1208,"dependency_fraction":0.7591059602649006},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"DYNLL1","stoichiometry":0.2},{"gene":"DYNLL2","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/MTPAP","total_profiled":1310},"omim":[{"mim_id":"613672","title":"SPASTIC ATAXIA 4, AUTOSOMAL RECESSIVE; SPAX4","url":"https://www.omim.org/entry/613672"},{"mim_id":"613669","title":"MITOCHONDRIAL POLY(A) POLYMERASE; MTPAP","url":"https://www.omim.org/entry/613669"},{"mim_id":"609672","title":"EXOCYST COMPLEX COMPONENT 6; EXOC6","url":"https://www.omim.org/entry/609672"},{"mim_id":"108600","title":"SPASTIC ATAXIA 1, AUTOSOMAL DOMINANT; SPAX1","url":"https://www.omim.org/entry/108600"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Mitochondria","reliability":"Supported"},{"location":"Nucleoplasm","reliability":"Additional"},{"location":"Vesicles","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"bone marrow","ntpm":34.6}],"url":"https://www.proteinatlas.org/search/MTPAP"},"hgnc":{"alias_symbol":["FLJ10486","SPAX4","TENT6"],"prev_symbol":["PAPD1"]},"alphafold":{"accession":"Q9NVV4","domains":[{"cath_id":"1.10.1410.10","chopping":"349-397_432-532","consensus_level":"high","plddt":93.9392,"start":349,"end":532}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NVV4","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NVV4-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NVV4-F1-predicted_aligned_error_v6.png","plddt_mean":82.81},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=MTPAP","jax_strain_url":"https://www.jax.org/strain/search?query=MTPAP"},"sequence":{"accession":"Q9NVV4","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9NVV4.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9NVV4/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NVV4"}},"corpus_meta":[{"pmid":"21292163","id":"PMC_21292163","title":"Structural basis for dimerization and activity of human PAPD1, a noncanonical poly(A) polymerase.","date":"2011","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/21292163","citation_count":37,"is_preprint":false},{"pmid":"26319014","id":"PMC_26319014","title":"Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.","date":"2015","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/26319014","citation_count":21,"is_preprint":false},{"pmid":"24651433","id":"PMC_24651433","title":"Homozygous mutation of MTPAP causes cellular radiosensitivity and persistent DNA double-strand breaks.","date":"2014","source":"Cell death & disease","url":"https://pubmed.ncbi.nlm.nih.gov/24651433","citation_count":14,"is_preprint":false},{"pmid":"16810331","id":"PMC_16810331","title":"A novel nuclear-encoded mitochondrial poly(A) polymerase PAPD1 is a potential candidate gene for the extreme obesity related phenotypes in mammals.","date":"2006","source":"International journal of biological sciences","url":"https://pubmed.ncbi.nlm.nih.gov/16810331","citation_count":14,"is_preprint":false},{"pmid":"31779033","id":"PMC_31779033","title":"Biallelic Mutations in MTPAP Associated with a Lethal Encephalopathy.","date":"2019","source":"Neuropediatrics","url":"https://pubmed.ncbi.nlm.nih.gov/31779033","citation_count":5,"is_preprint":false},{"pmid":"22297614","id":"PMC_22297614","title":"Molecular characterization of the porcine MTPAP gene associated with meat quality traits: chromosome localization, expression distribution, and transcriptional regulation.","date":"2012","source":"Molecular and cellular biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/22297614","citation_count":3,"is_preprint":false},{"pmid":"41226525","id":"PMC_41226525","title":"Long Noncoding RNA Lnc-MTPAP-1 Overexpressed by Particulate Matter Suppresses Apoptosis in Non-Small Cell Lung Cancer (NSCLC) Cells.","date":"2025","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/41226525","citation_count":0,"is_preprint":false},{"pmid":"40499712","id":"PMC_40499712","title":"A Case Report of Primary Ovarian Failure in an Adolescent Associated With a Homozygous Pathogenic Variant in the Mitochondrial Poly-A-Polymerase Gene (MTPAP).","date":"2025","source":"Journal of pediatric and adolescent gynecology","url":"https://pubmed.ncbi.nlm.nih.gov/40499712","citation_count":0,"is_preprint":false},{"pmid":"40174712","id":"PMC_40174712","title":"Clinical and molecular assessment of a spastic ataxia 4 (SPAX4) patient with a novel variant in the MTPAP gene, and a systematic review.","date":"2025","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/40174712","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6166,"output_tokens":1163,"usd":0.017972,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7823,"output_tokens":1826,"usd":0.042382,"stage2_stop_reason":"end_turn"},"total_usd":0.060354,"stage1_batch_id":"msgbatch_013a8chtv3AWyTqv4z4sEF4C","stage2_batch_id":"msgbatch_01AHsuW63vinsvuTgzmQ3n62","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2011,\n      \"finding\": \"Crystal structure of human PAPD1 (MTPAP) reveals palm and fingers domains forming an active site at their interface, with a large substrate-binding pocket. An N-terminal domain with RNP-type RNA-binding fold (named the RL domain) and a β-arm insertion in the palm domain mediate homodimerization. Mutagenesis and biochemical studies demonstrated that dimerization is required for catalytic activity.\",\n      \"method\": \"X-ray crystallography, active-site mutagenesis, biochemical activity assays\",\n      \"journal\": \"Molecular cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structure combined with mutagenesis and in vitro biochemical assays, multiple orthogonal methods in one rigorous study\",\n      \"pmids\": [\"21292163\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Crystal structures of mitochondrial PAP (mtPAP/MTPAP) reveal the structural basis for ATP selectivity over other nucleotides, and show an intricate dimerization interface featuring an RNA-recognition module formed through strand complementation. The N478D mutation (causing SPAX4) is structurally explained as drastically reducing poly(A) tail length on mitochondrial mRNAs.\",\n      \"method\": \"X-ray crystallography, structural analysis of disease-associated mutant\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — high-resolution crystal structures with functional interpretation of disease mutation, rigorous structural analysis\",\n      \"pmids\": [\"26319014\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Pathogenic missense mutations in MTPAP (compound heterozygous p.Ile428Thr/p.Arg523Trp and homozygous p.Ile385Phe) cause shorter poly(A) tails on mitochondrial transcripts and altered mitochondrial protein expression in patient fibroblasts, establishing that MTPAP activity is required for normal polyadenylation of mitochondrially encoded mRNAs and mitochondrial protein synthesis.\",\n      \"method\": \"Mitochondrial poly(A) tail length analysis, de novo mitochondrial protein synthesis assay in patient fibroblasts\",\n      \"journal\": \"Neuropediatrics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct functional assays in patient-derived fibroblasts with two orthogonal methods (poly(A) analysis + protein synthesis), single lab\",\n      \"pmids\": [\"31779033\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Homozygous missense mutation in MTPAP causes cellular radiosensitivity characterized by delayed DNA double-strand break repair, increased reactive oxygen species (ROS), and increased apoptosis after ionizing radiation; wild-type MTPAP cDNA rescue abrogated radiosensitivity, and antioxidant pre-treatment (α-lipoic acid, N-acetylcysteine) rescued DNA repair and clonogenic survival defects, implicating ROS dysregulation as the pathogenic mechanism.\",\n      \"method\": \"Complementation with wild-type cDNA in MTPAP-deficient cell lines, clonogenic survival assay, γH2AX foci for DSB quantification, ROS measurement, antioxidant rescue experiment\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (rescue, clonogenic survival, DSB foci, ROS, pharmacological rescue), single lab\",\n      \"pmids\": [\"24651433\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"MTPAP (PAPD1/mtPAP) is a nuclear-encoded, noncanonical poly(A) polymerase that localizes to mitochondria and polyadenylates mitochondrial mRNAs to regulate their stability and expression; it functions as an obligate homodimer—with dimerization mediated by an N-terminal RL domain and a β-arm insertion forming an RNA-recognition module at the dimer interface—and selectively incorporates ATP via a structurally defined active-site pocket, while loss-of-function mutations truncate mitochondrial poly(A) tails, impair mitochondrial protein synthesis, disrupt ROS homeostasis, and cause neurodegenerative disease (SPAX4).\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MTPAP (PAPD1/mtPAP) is a noncanonical poly(A) polymerase that polyadenylates mitochondrially encoded mRNAs to support their stability and translation [#2]. Structural and biochemical work established that it is catalytically active only as a homodimer: an N-terminal RNP-type RNA-binding fold (the RL domain) together with a \\u03b2-arm insertion in the palm domain mediates dimerization, and dimerization is obligatory for activity [#0]. High-resolution structures further defined the basis for selective ATP incorporation and revealed an RNA-recognition module assembled by strand complementation across the dimer interface, while structurally explaining how the SPAX4-causing N478D substitution shortens mitochondrial poly(A) tails [#1]. Loss-of-function mutations truncate poly(A) tails on mitochondrial transcripts and impair de novo mitochondrial protein synthesis in patient fibroblasts [#2], and a homozygous pathogenic mutation produces cellular radiosensitivity with delayed double-strand break repair, elevated ROS, and increased apoptosis that is rescued by wild-type cDNA and by antioxidant treatment, linking MTPAP dysfunction to ROS dysregulation [#3]. Pathogenic MTPAP mutations cause the neurodegenerative disorder SPAX4 [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"The unknown question of how MTPAP achieves catalysis was answered by showing it is an obligate homodimer with a defined active site formed at the palm-fingers interface.\",\n      \"evidence\": \"X-ray crystallography of human PAPD1 with active-site mutagenesis and in vitro activity assays\",\n      \"pmids\": [\"21292163\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not establish RNA substrate specificity in vivo\", \"Mechanism of substrate selection within the binding pocket not resolved\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"It was unclear how MTPAP discriminates ATP and how disease mutations impair function; structures revealed the basis for ATP selectivity and a dimer-interface RNA-recognition module, and explained the N478D SPAX4 mutation as shortening poly(A) tails.\",\n      \"evidence\": \"High-resolution crystal structures including structural analysis of the disease-associated mutant\",\n      \"pmids\": [\"26319014\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural snapshot does not capture catalytic cycle dynamics\", \"Does not directly measure tail-length effects in patient tissue\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"The pathogenic mechanism downstream of MTPAP loss was addressed by linking deficiency to ROS-driven radiosensitivity and impaired DNA double-strand break repair, with antioxidant rescue identifying ROS dysregulation as causal.\",\n      \"evidence\": \"Wild-type cDNA complementation, clonogenic survival, \\u03b3H2AX foci, ROS measurement, and antioxidant rescue in MTPAP-deficient cells\",\n      \"pmids\": [\"24651433\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab\", \"Mechanistic link between mitochondrial polyadenylation defect and nuclear DSB repair not fully resolved\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether multiple distinct missense mutations converge on the same molecular defect was answered by showing diverse pathogenic alleles shorten mitochondrial poly(A) tails and alter mitochondrial protein synthesis.\",\n      \"evidence\": \"Mitochondrial poly(A) tail length analysis and de novo mitochondrial protein synthesis assays in patient fibroblasts\",\n      \"pmids\": [\"31779033\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab\", \"Transcript-specific consequences of tail shortening not delineated\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How shortened mitochondrial poly(A) tails mechanistically produce ROS dysregulation and neurodegeneration in SPAX4 remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No causal chain established from poly(A) defect to neuronal pathology\", \"Transcript-level selectivity of MTPAP in vivo unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140098\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0016740\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\"MTPAP homodimer\"],\n    \"partners\": [],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}