{"gene":"CPD","run_date":"2026-06-09T22:57:19","timeline":{"discoveries":[{"year":1998,"finding":"Human carboxypeptidase D (CPD) was chromosomally localized to the centromeric region 17p11.1-q11.1/11.2 by PCR with gene-specific primers and somatic cell hybrid DNAs. The protein was described as having three tandem active site domains and classified as a member of the regulatory B-type carboxypeptidase family (alongside carboxypeptidases M, E/H, and AEBP1).","method":"PCR-based somatic cell hybrid mapping; regional mapping panel","journal":"Genomics","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct chromosomal localization by PCR-based somatic cell hybrid mapping in a single study; domain classification based on sequence analysis without in vitro functional assay","pmids":["9628828"],"is_preprint":false}],"current_model":"Human carboxypeptidase D (CPD) is a member of the regulatory B-type carboxypeptidase family with three tandem active site domains, chromosomally localized to 17p11.1-q11.1/11.2; no direct mechanistic experiments characterizing its enzymatic activity, substrates, binding partners, or cellular function are reported in the available literature."},"narrative":{"mechanistic_narrative":"Human carboxypeptidase D (CPD) was identified as a member of the regulatory B-type carboxypeptidase family bearing three tandem active site domains and mapped to the centromeric region 17p11.1-q11.1/11.2 [PMID:9628828]. Beyond this chromosomal localization and sequence-based family classification, no direct mechanistic experiments characterizing its enzymatic activity, substrates, binding partners, or cellular function have been reported in the available corpus.","teleology":[{"year":1998,"claim":"Established the chromosomal location of human CPD and its membership in the regulatory B-type carboxypeptidase family, providing the genomic anchor and family context for a previously uncharacterized gene.","evidence":"PCR-based somatic cell hybrid mapping with gene-specific primers and a regional mapping panel; sequence-based domain classification","pmids":["9628828"],"confidence":"Medium","gaps":["Enzymatic activity of the three tandem active site domains was not assayed in vitro","No substrates, binding partners, or cellular functions were identified","Subcellular localization not determined experimentally"]},{"year":null,"claim":"The catalytic activity, physiological substrates, interaction partners, and cellular role of human CPD remain uncharacterized by direct experiment in the available corpus.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No functional enzymatic assay of any of the three active site domains","No substrate or pathway assignment","No subcellular localization or partner data"]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O75976","full_name":"Carboxypeptidase D","aliases":["Metallocarboxypeptidase D","gp180"],"length_aa":1380,"mass_kda":152.9,"function":"Functions in the processing of proteins and peptides in the secretory pathway. Mechanistically, cleaves exclusively C-terminal basic residues. By removing terminal residues, can modulate the activity, stability, and receptor-binding properties of bioactive peptides (Microbial infection) Acts as an alternative entry receptor for adeno-associated virus (AAV)","subcellular_location":"Cell membrane","url":"https://www.uniprot.org/uniprotkb/O75976/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CPD","classification":"Not Classified","n_dependent_lines":116,"n_total_lines":1208,"dependency_fraction":0.09602649006622517},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"CANX","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/CPD","total_profiled":1310},"omim":[{"mim_id":"613675","title":"CHROMOSOME 17q11.2 DELETION SYNDROME, 1.4-MB","url":"https://www.omim.org/entry/613675"},{"mim_id":"613208","title":"XPC COMPLEX SUBUNIT, DNA DAMAGE RECOGNITION AND REPAIR FACTOR; XPC","url":"https://www.omim.org/entry/613208"},{"mim_id":"612052","title":"SMOKING AS A QUANTITATIVE TRAIT LOCUS 3; SQTL3","url":"https://www.omim.org/entry/612052"},{"mim_id":"607999","title":"ASH1-LIKE HISTONE LYSINE METHYLTRANSFERASE; ASH1L","url":"https://www.omim.org/entry/607999"},{"mim_id":"603103","title":"CARBOXYPEPTIDASE N, POLYPEPTIDE 1, 50-KD; CPN1","url":"https://www.omim.org/entry/603103"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Cytosol","reliability":"Approved"},{"location":"Nucleoli","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/CPD"},"hgnc":{"alias_symbol":["GP180"],"prev_symbol":[]},"alphafold":{"accession":"O75976","domains":[{"cath_id":"3.40.630.10","chopping":"80-105_126-198_207-382","consensus_level":"high","plddt":92.1095,"start":80,"end":382},{"cath_id":"2.60.40.1120","chopping":"385-460","consensus_level":"high","plddt":91.8513,"start":385,"end":460},{"cath_id":"3.40.630.10","chopping":"507-794","consensus_level":"high","plddt":95.7874,"start":507,"end":794},{"cath_id":"2.60.40.1120","chopping":"799-871","consensus_level":"high","plddt":92.74,"start":799,"end":871},{"cath_id":"3.40.630.10","chopping":"901-1211","consensus_level":"high","plddt":87.5753,"start":901,"end":1211},{"cath_id":"2.60.40.1120","chopping":"1218-1294","consensus_level":"high","plddt":81.1253,"start":1218,"end":1294}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O75976","model_url":"https://alphafold.ebi.ac.uk/files/AF-O75976-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O75976-F1-predicted_aligned_error_v6.png","plddt_mean":82.5},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CPD","jax_strain_url":"https://www.jax.org/strain/search?query=CPD"},"sequence":{"accession":"O75976","fasta_url":"https://rest.uniprot.org/uniprotkb/O75976.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O75976/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O75976"}},"corpus_meta":[{"pmid":"15576622","id":"PMC_15576622","title":"Crystal 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I. Studies of six experimental solutions.","date":"1993","source":"Transfusion medicine (Oxford, England)","url":"https://pubmed.ncbi.nlm.nih.gov/8038896","citation_count":13,"is_preprint":false},{"pmid":"982537","id":"PMC_982537","title":"Blood storage XXII. Improvement in red blood cell 2,3-DPG levels at six weeks by 20 mM PO4 in CPD-adenine-inosine.","date":"1976","source":"Transfusion","url":"https://pubmed.ncbi.nlm.nih.gov/982537","citation_count":13,"is_preprint":false},{"pmid":"15988133","id":"PMC_15988133","title":"CPD photolyase gene from Spinacia oleracea: repair of UV-damaged DNA and expression in plant organs.","date":"2005","source":"Journal of radiation research","url":"https://pubmed.ncbi.nlm.nih.gov/15988133","citation_count":12,"is_preprint":false},{"pmid":"22017645","id":"PMC_22017645","title":"Evidence from thermodynamics that DNA photolyase recognizes a solvent-exposed CPD lesion.","date":"2011","source":"The journal of physical chemistry. B","url":"https://pubmed.ncbi.nlm.nih.gov/22017645","citation_count":12,"is_preprint":false},{"pmid":"23272247","id":"PMC_23272247","title":"Analysis of CPD ultraviolet lesion bypass in chicken DT40 cells: polymerase η and PCNA ubiquitylation play identical roles.","date":"2012","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/23272247","citation_count":12,"is_preprint":false},{"pmid":"22362193","id":"PMC_22362193","title":"Augmentation of CPD photolyase activity in japonica and indica rice increases their UVB resistance but still leaves the difference in their sensitivities.","date":"2012","source":"Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology","url":"https://pubmed.ncbi.nlm.nih.gov/22362193","citation_count":12,"is_preprint":false},{"pmid":"37524261","id":"PMC_37524261","title":"Principles for Continuing Professional Development (CPD) Programs: A Statement by the ACPE CPD Advisory Committee.","date":"2023","source":"American journal of pharmaceutical education","url":"https://pubmed.ncbi.nlm.nih.gov/37524261","citation_count":11,"is_preprint":false},{"pmid":"7090334","id":"PMC_7090334","title":"Complement in CPD-stored blood.","date":"1982","source":"Vox sanguinis","url":"https://pubmed.ncbi.nlm.nih.gov/7090334","citation_count":11,"is_preprint":false},{"pmid":"867465","id":"PMC_867465","title":"Blood storage XXIV: red blood cell 2,3-DPG and ATP maintenance for six weeks in CPD-adenine with higher phosphate, pyruvate, and dihydroxyacetone.","date":"1977","source":"Transfusion","url":"https://pubmed.ncbi.nlm.nih.gov/867465","citation_count":11,"is_preprint":false},{"pmid":"36499473","id":"PMC_36499473","title":"Preparation of CPD Photolyase Nanoliposomes Derived from Antarctic Microalgae and Their Effect on UVB-Induced Skin Damage in Mice.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/36499473","citation_count":10,"is_preprint":false},{"pmid":"25610902","id":"PMC_25610902","title":"Investigation of CPD and HMDS sample preparation techniques for cervical cells in developing computer-aided screening system based on FE-SEM/EDX.","date":"2014","source":"TheScientificWorldJournal","url":"https://pubmed.ncbi.nlm.nih.gov/25610902","citation_count":10,"is_preprint":false},{"pmid":"31200103","id":"PMC_31200103","title":"The complete genome of Rachiplusia nu nucleopolyhedrovirus (RanuNPV) and the identification of a baculoviral CPD-photolyase homolog.","date":"2019","source":"Virology","url":"https://pubmed.ncbi.nlm.nih.gov/31200103","citation_count":10,"is_preprint":false},{"pmid":"12018166","id":"PMC_12018166","title":"[Chromosome CPD(PI/DAPI)- and CMA/DAPI-banding patterns in Allium cepa L].","date":"2002","source":"Genetika","url":"https://pubmed.ncbi.nlm.nih.gov/12018166","citation_count":10,"is_preprint":false},{"pmid":"432914","id":"PMC_432914","title":"Plasma adenine and cellular ATP in red cell concentrates collected and stored in modified CPD at 4 C.","date":"1979","source":"Transfusion","url":"https://pubmed.ncbi.nlm.nih.gov/432914","citation_count":10,"is_preprint":false},{"pmid":"34558720","id":"PMC_34558720","title":"Ability of the Putative Decomposition Products of 2,3-dioxetanes of Indoles to Photosensitize Cyclobutane Pyrimidine Dimer (CPD) Formation and its Implications for the \"Dark\" (Chemisensitized) Pathway to CPDs in Melanocytes†.","date":"2021","source":"Photochemistry and photobiology","url":"https://pubmed.ncbi.nlm.nih.gov/34558720","citation_count":9,"is_preprint":false},{"pmid":"15936904","id":"PMC_15936904","title":"The DNA repair enzyme, CPD-photolyase restores the infectivity of UV-damaged fowlpox virus isolated from infected scabs of chickens.","date":"2005","source":"Veterinary microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/15936904","citation_count":9,"is_preprint":false},{"pmid":"38479157","id":"PMC_38479157","title":"CPD-002, a novel VEGFR2 inhibitor, relieves rheumatoid arthritis by reducing angiogenesis through the suppression of the VEGFR2/PI3K/AKT signaling pathway.","date":"2024","source":"International immunopharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/38479157","citation_count":9,"is_preprint":false},{"pmid":"34385002","id":"PMC_34385002","title":"A CPD photolyase gene PnPHR1 from Antarctic moss Pohlia nutans is involved in the resistance to UV-B radiation and salinity stress.","date":"2021","source":"Plant physiology and biochemistry : PPB","url":"https://pubmed.ncbi.nlm.nih.gov/34385002","citation_count":9,"is_preprint":false},{"pmid":"7999855","id":"PMC_7999855","title":"Higher KT/V urea associated with greater protein catabolic rate and dietary protein intake in children treated with CCPD compared to CAPD. Mid-European Pediatric CPD Study Group (MPCS).","date":"1994","source":"Advances in peritoneal dialysis. Conference on Peritoneal Dialysis","url":"https://pubmed.ncbi.nlm.nih.gov/7999855","citation_count":9,"is_preprint":false},{"pmid":"10760201","id":"PMC_10760201","title":"In vitro properties of red cells prepared from half-strength citrate CPD/RAS-2 (Erythro-sol) donations in PL-146 plastic.","date":"2000","source":"Transfusion medicine (Oxford, England)","url":"https://pubmed.ncbi.nlm.nih.gov/10760201","citation_count":9,"is_preprint":false},{"pmid":"27493513","id":"PMC_27493513","title":"FTIR study of CPD photolyase with substrate in single strand DNA.","date":"2015","source":"Biophysics (Nagoya-shi, Japan)","url":"https://pubmed.ncbi.nlm.nih.gov/27493513","citation_count":8,"is_preprint":false},{"pmid":"37003653","id":"PMC_37003653","title":"UVA causes specific mutagenic DNA damage through ROS production, rather than CPD formation, in Drosophila larvae.","date":"2023","source":"Mutation research. Genetic toxicology and environmental mutagenesis","url":"https://pubmed.ncbi.nlm.nih.gov/37003653","citation_count":8,"is_preprint":false},{"pmid":"16077967","id":"PMC_16077967","title":"Modulation of bcl-2 family proteins in MAPK independent apoptosis induced by a cdc25 phosphatase inhibitor Cpd 5 in renal cancer cells.","date":"2005","source":"Oncology reports","url":"https://pubmed.ncbi.nlm.nih.gov/16077967","citation_count":8,"is_preprint":false},{"pmid":"7324438","id":"PMC_7324438","title":"Red cell ATP and 2,3-diphosphoglycerate concentrations as a function of dihydroxyacetone supplementation of CPD adenine.","date":"1981","source":"Vox sanguinis","url":"https://pubmed.ncbi.nlm.nih.gov/7324438","citation_count":8,"is_preprint":false},{"pmid":"30940570","id":"PMC_30940570","title":"X-ray driven reduction of Cpd I of Catalase-3 from N. crassa reveals differential sensitivity of active sites and formation of ferrous state.","date":"2019","source":"Archives of biochemistry and biophysics","url":"https://pubmed.ncbi.nlm.nih.gov/30940570","citation_count":8,"is_preprint":false},{"pmid":"7368270","id":"PMC_7368270","title":"Blood preservation. XXIX. Pyruvate maintains normal red cell 2,3-DPG for six weeks of storage in CPD-adenine.","date":"1980","source":"Transfusion","url":"https://pubmed.ncbi.nlm.nih.gov/7368270","citation_count":8,"is_preprint":false},{"pmid":"36574488","id":"PMC_36574488","title":"Mechanistic Aspects of the Effect of Flanking Nucleotide Sequence on CPD Formation and CPD Self-Repair in DNA.","date":"2022","source":"The journal of physical chemistry. B","url":"https://pubmed.ncbi.nlm.nih.gov/36574488","citation_count":7,"is_preprint":false},{"pmid":"37554110","id":"PMC_37554110","title":"Genome-wide impact of cytosine methylation and DNA sequence context on UV-induced CPD formation.","date":"2023","source":"Environmental and molecular mutagenesis","url":"https://pubmed.ncbi.nlm.nih.gov/37554110","citation_count":7,"is_preprint":false},{"pmid":"33777867","id":"PMC_33777867","title":"Cell Population Data (CPD) for Early Recognition of Sepsis and Septic Shock in Children: A Pilot Study.","date":"2021","source":"Frontiers in pediatrics","url":"https://pubmed.ncbi.nlm.nih.gov/33777867","citation_count":7,"is_preprint":false},{"pmid":"17383890","id":"PMC_17383890","title":"Identification and expression of the gene product encoding a CPD photolyase from Dunaliella salina.","date":"2007","source":"Journal of photochemistry and photobiology. B, Biology","url":"https://pubmed.ncbi.nlm.nih.gov/17383890","citation_count":7,"is_preprint":false},{"pmid":"16760123","id":"PMC_16760123","title":"CPD staining: an effective technique for detection of NORs and other GC-rich chromosomal regions in plants.","date":"2006","source":"Biotechnic & histochemistry : official publication of the Biological Stain Commission","url":"https://pubmed.ncbi.nlm.nih.gov/16760123","citation_count":7,"is_preprint":false},{"pmid":"2149230","id":"PMC_2149230","title":"Chlorophyll derivatives (CpD) extracted from silk worm excreta are specifically cytotoxic to tumor cells in vitro.","date":"1990","source":"Yonsei medical journal","url":"https://pubmed.ncbi.nlm.nih.gov/2149230","citation_count":7,"is_preprint":false},{"pmid":"30224964","id":"PMC_30224964","title":"Twist and turn: a revised structural view on the unpaired bubble of class II CPD photolyase in complex with damaged DNA.","date":"2018","source":"IUCrJ","url":"https://pubmed.ncbi.nlm.nih.gov/30224964","citation_count":7,"is_preprint":false},{"pmid":"10155740","id":"PMC_10155740","title":"Shall red cell units stand upright, lie flat or be mixed during storage? In vitro studies of red cells collected in 0.5 CPD and stored in RAS2 (Erythrosol).","date":"1995","source":"Transfusion science","url":"https://pubmed.ncbi.nlm.nih.gov/10155740","citation_count":7,"is_preprint":false},{"pmid":"40790130","id":"PMC_40790130","title":"Conservation of dark CPD photolyase function in blind cavefish.","date":"2025","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/40790130","citation_count":6,"is_preprint":false},{"pmid":"9628828","id":"PMC_9628828","title":"Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1).","date":"1998","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/9628828","citation_count":6,"is_preprint":false},{"pmid":"20844742","id":"PMC_20844742","title":"Cpd-1 null mice display a subtle neurological phenotype.","date":"2010","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/20844742","citation_count":6,"is_preprint":false},{"pmid":"31669654","id":"PMC_31669654","title":"Detection of plasmid-mediated colistin resistance by colistin pre-diffusion and inhibition with EDTA test (CPD-E) in Enterobactereaceae.","date":"2019","source":"Journal of microbiological methods","url":"https://pubmed.ncbi.nlm.nih.gov/31669654","citation_count":6,"is_preprint":false},{"pmid":"37327725","id":"PMC_37327725","title":"Coupling of conformation and CPD damage in nucleosomal DNA.","date":"2023","source":"Biophysical chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/37327725","citation_count":5,"is_preprint":false},{"pmid":"34367869","id":"PMC_34367869","title":"Two class II CPD photolyases, PiPhr1 and PiPhr2, with CPD repair activity from the Antarctic diatom Phaeodactylum tricornutum ICE-H.","date":"2021","source":"3 Biotech","url":"https://pubmed.ncbi.nlm.nih.gov/34367869","citation_count":5,"is_preprint":false},{"pmid":"37112689","id":"PMC_37112689","title":"Codon Pair Deoptimization (CPD)-Attenuated PRRSV-1 Vaccination Exhibit Immunity to Virulent PRRSV Challenge in Pigs.","date":"2023","source":"Vaccines","url":"https://pubmed.ncbi.nlm.nih.gov/37112689","citation_count":5,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":47844,"output_tokens":742,"usd":0.077331,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6572,"output_tokens":673,"usd":0.024842,"stage2_stop_reason":"end_turn"},"total_usd":0.102173,"stage1_batch_id":"msgbatch_01ACAxJQabDsht39JXeWG22d","stage2_batch_id":"msgbatch_01QEU22A9U5sbPTgsMzTmvSf","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking at the corpus, I need to identify which papers are about the human gene CPD (carboxypeptidase D, HGNC symbol CPD, chromosomal location 17p11.1-q11.1/11.2 based on paper 95).\n\nThe vast majority of papers in this corpus are about:\n1. CPD = cyclobutane pyrimidine dimers (UV-induced DNA lesions) - NOT the gene\n2. CPD = citrate-phosphate-dextrose (blood storage solution) - NOT the gene\n3. CPD = continuing professional development - NOT the gene\n4. CPD = various compound names (Cpd-71, Cpd-42, etc.) - NOT the gene\n5. CPD photolyases (bacterial, plant, viral enzymes) - NOT the human CPD gene\n\nPapers relevant to human CPD (carboxypeptidase D):\n- Paper 95: Chromosomal localization of CPD gene to 17p11.1-q11.1/11.2, describes it as having three tandem active site domains, member of regulatory B-type carboxypeptidase family.\n- Paper 52: SLC6A4 gene mapping paper that mentions CPD (carboxypeptidase D) adjacently on chromosome 17q11.\n- Paper 96: \"Cpd-1 null mice\" - this describes CPD1/ANP32-E, a different protein, not carboxypeptidase D.\n\nOnly papers 95 and 52 relate to carboxypeptidase D (CPD), but they provide only chromosomal localization data, not mechanistic findings about how the protein works.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1998,\n      \"finding\": \"Human carboxypeptidase D (CPD) was chromosomally localized to the centromeric region 17p11.1-q11.1/11.2 by PCR with gene-specific primers and somatic cell hybrid DNAs. The protein was described as having three tandem active site domains and classified as a member of the regulatory B-type carboxypeptidase family (alongside carboxypeptidases M, E/H, and AEBP1).\",\n      \"method\": \"PCR-based somatic cell hybrid mapping; regional mapping panel\",\n      \"journal\": \"Genomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct chromosomal localization by PCR-based somatic cell hybrid mapping in a single study; domain classification based on sequence analysis without in vitro functional assay\",\n      \"pmids\": [\"9628828\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"Human carboxypeptidase D (CPD) is a member of the regulatory B-type carboxypeptidase family with three tandem active site domains, chromosomally localized to 17p11.1-q11.1/11.2; no direct mechanistic experiments characterizing its enzymatic activity, substrates, binding partners, or cellular function are reported in the available literature.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Human carboxypeptidase D (CPD) was identified as a member of the regulatory B-type carboxypeptidase family bearing three tandem active site domains and mapped to the centromeric region 17p11.1-q11.1/11.2 [#0]. Beyond this chromosomal localization and sequence-based family classification, no direct mechanistic experiments characterizing its enzymatic activity, substrates, binding partners, or cellular function have been reported in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 1998,\n      \"claim\": \"Established the chromosomal location of human CPD and its membership in the regulatory B-type carboxypeptidase family, providing the genomic anchor and family context for a previously uncharacterized gene.\",\n      \"evidence\": \"PCR-based somatic cell hybrid mapping with gene-specific primers and a regional mapping panel; sequence-based domain classification\",\n      \"pmids\": [\"9628828\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Enzymatic activity of the three tandem active site domains was not assayed in vitro\",\n        \"No substrates, binding partners, or cellular functions were identified\",\n        \"Subcellular localization not determined experimentally\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The catalytic activity, physiological substrates, interaction partners, and cellular role of human CPD remain uncharacterized by direct experiment in the available corpus.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No functional enzymatic assay of any of the three active site domains\",\n        \"No substrate or pathway assignment\",\n        \"No subcellular localization or partner data\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"loss","faith_supported":1,"faith_total":1,"faith_pct":100.0}}