{"gene":"NAA50","run_date":"2026-06-10T05:19:52","timeline":{"discoveries":[{"year":2019,"finding":"X-ray crystal structure of yeast NatA/Naa50 ternary complex shows Naa50 makes evolutionarily conserved contacts to both the Naa10 and Naa15 subunits of NatA; these interactions promote catalytic crosstalk within the human NatA/Naa50 complex but to a lesser extent in the yeast complex where Naa50 activity is compromised.","method":"X-ray crystallography of yeast NatA/Naa50 complex; in vitro enzymatic activity assays comparing yeast and human complexes","journal":"Structure","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structure with functional validation comparing yeast and human complexes, multiple orthogonal methods in a single rigorous study","pmids":["31155310"],"is_preprint":false},{"year":2015,"finding":"Human Naa50 preferentially Nt-acetylates N-terminal Met (iMet)-starting N-termini including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr; a kinetic competition exists between Naa50 and Met-aminopeptidases (MetAPs), such that Naa50-mediated Nt-acetylation of iMet followed by a small residue blocks subsequent MetAP cleavage.","method":"Quantitative N-terminal acetylome profiling in yeast expressing human Naa50 versus wild-type or Naa50-knockout yeast; in vitro MetAP cleavage assays","journal":"Proteomics","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — quantitative proteomics with genetic manipulation combined with in vitro biochemical validation, multiple orthogonal methods","pmids":["25886145"],"is_preprint":false},{"year":2016,"finding":"Crystal structure of human Naa50 revealed co-purified CoA and an acetylated tetrapeptide (AcMMXX); biochemical analysis of a tetrapeptide library showed that Met-Met in positions 1–2 is the optimal substrate, and Naa50 acetylates all MXAA peptides except MPAA.","method":"X-ray crystallography; biochemical peptide library screen and thermal stability assays","journal":"Journal of Biological Chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure combined with systematic biochemical substrate profiling, single lab but two orthogonal methods","pmids":["27484799"],"is_preprint":false},{"year":2021,"finding":"High-resolution X-ray crystal structures of Arabidopsis Naa50 (AtNaa50) in complex with AcCoA and a bisubstrate analog defined its active site and substrate specificity; functionally important catalytic residues were identified by mutagenesis; yeast Naa50 is catalytically inactive yet retains CoA conjugate binding.","method":"X-ray crystallography (AtNaa50-AcCoA and bisubstrate analog complexes); enzymatic kinetics; active-site mutagenesis","journal":"Structure","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structures with bisubstrate analog, enzymatic kinetics, and mutagenesis in a single rigorous study","pmids":["33400917"],"is_preprint":false},{"year":2020,"finding":"Purified Arabidopsis NAA50 (AtNAA50) displays both Nα-terminal acetyltransferase activity and lysine-ε-autoacetyltransferase activity in vitro; global N-acetylome profiling in E. coli expressing AtNAA50 confirmed conservation of NatE substrate specificity between plants and humans; the catalytically inactive yeast Naa50 failed to complement naa50 mutant plants, demonstrating enzymatic activity is required for NAA50 function in planta.","method":"In vitro acetyltransferase assay with purified recombinant AtNAA50; N-acetylome profiling in E. coli; genetic complementation in Arabidopsis naa50 mutant lines","journal":"Plant Physiology","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — in vitro enzymatic assay plus in vivo acetylome profiling plus genetic rescue experiment, multiple orthogonal methods","pmids":["32461302"],"is_preprint":false},{"year":2016,"finding":"Depletion of Naa50 in HeLa cells weakens the interaction between cohesin and its positive regulator sororin, causing sister-chromatid cohesion defects in S phase; co-depletion of NatA rescues the cohesion defects and mitotic arrest caused by Naa50 depletion, demonstrating that NatA and Naa50 play antagonistic roles in cohesion; purified NatA and Naa50 do not affect each other's NAT activity in vitro.","method":"siRNA knockdown in HeLa cells; co-immunoprecipitation; mitotic arrest assays; in vitro NAT activity assays with purified proteins","journal":"Journal of Biological Chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — epistasis by co-depletion with defined cellular phenotype rescue, Co-IP, and in vitro enzymatic assay, single lab","pmids":["27422821"],"is_preprint":false},{"year":2016,"finding":"Genetic and biochemical evidence in Drosophila indicates that Naa50/San N-terminally acetylates the nascent Scc1 (cohesin subunit) polypeptide co-translationally, and that this modification is required for the correct interaction between cohesin subunits Scc1 and Smc3 and for sister-chromatid cohesion during tissue proliferation.","method":"Genetic epistasis in Drosophila; biochemical co-immunoprecipitation of cohesin subunits in Naa50/San-depleted cells","journal":"Scientific Reports","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — genetic and biochemical approaches in model organism, single lab, two complementary methods","pmids":["27996020"],"is_preprint":false},{"year":2020,"finding":"Two novel small-molecule inhibitors of Naa50 were identified; co-crystal structures with Naa50 and biochemical assays defined their mechanism of action and selectivity over related enzymes Naa10 and Naa60; cellular target engagement was confirmed for compound 4a.","method":"DNA-encoded library screening; co-crystal structures; biochemical inhibition assays; cellular target engagement experiments","journal":"ACS Medicinal Chemistry Letters","confidence":"High","confidence_rationale":"Tier 1 / Moderate — co-crystal structures with mechanistic biochemistry and cellular confirmation, single lab but multiple orthogonal methods","pmids":["32550998"],"is_preprint":false},{"year":2023,"finding":"Purified recombinant human Naa50 displays serotonin N-acetyltransferase (SNAT) activity in vitro (Km = 986 μM, Vmax = 1800 pmol/min/mg), in addition to its Nα-terminal acetyltransferase activity, indicating enzymatic bifunctionality.","method":"In vitro SNAT enzyme assay with purified recombinant hNaa50 expressed in E. coli","journal":"Antioxidants","confidence":"Low","confidence_rationale":"Tier 1 / Weak — single in vitro biochemical assay, single lab, no independent replication, functional relevance in human cells not established","pmids":["36829878"],"is_preprint":false},{"year":2022,"finding":"In filamentous fungi (Chaetomium thermophilum), Naa50 contains significant N- and C-terminal extensions beyond the conserved GNAT domain; the elongated N-terminus increases thermostability and binds to dynein light chain protein 1 (DLC1); conserved positive patches in the C-terminus allow ribosome binding independent of NatA; CtNaa50 does not form a NatE complex with NatA.","method":"X-ray crystallography of CtNaa50; biochemical binding assays for DLC1 interaction and ribosome binding; structural comparison with other Naa50 homologs","journal":"International Journal of Molecular Sciences","confidence":"Medium","confidence_rationale":"Tier 1–2 / Moderate — crystal structure combined with biochemical binding assays, single lab, multiple methods","pmids":["36142717"],"is_preprint":false},{"year":2024,"finding":"In Arabidopsis, AtNAA50 associates with NatA at ribosomes (demonstrated by split-luciferase proximity assay in planta and interactome analysis), yet AtNAA50 and AtNatA/HYPK exert distinct in vivo functions: AtNAA50 negatively regulates plant immunity independently of salicylic acid accumulation and independently of NatA activity, and does not modulate drought tolerance or protein stability like NatA/HYPK.","method":"Split-luciferase proximity assay in planta; interactome analysis (AtNAA50 pull-down); transcriptome and proteome profiling of amiNAA50 plants; pathogen resistance assays","journal":"Plant Physiology","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — split-luciferase interaction, interactome, and functional genetic evidence, single lab with multiple complementary approaches","pmids":["38588051"],"is_preprint":false},{"year":2026,"finding":"NAA50 catalyzes N-terminal acetylation of the splicing factor SLU7, preventing its ubiquitin-proteasomal degradation and stabilizing SLU7 protein in bladder cancer cells; NAA50-stabilized SLU7 promotes MAP3K3 mRNA nuclear export and p38 MAPK activation to drive cisplatin resistance; pharmacological inhibition of NAA50 destabilizes SLU7 and reverses cisplatin resistance in vitro and in vivo.","method":"Co-immunoprecipitation; mass spectrometry; ubiquitination assays; RNA immunoprecipitation (RIP-qPCR); nucleocytoplasmic fractionation; xenograft models; pharmacological NAA50 inhibition","journal":"Cellular Oncology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP and MS identification of interaction plus multiple functional assays, single lab with orthogonal methods","pmids":["42151695"],"is_preprint":false}],"current_model":"NAA50 (Naa50/NatE) is an enzymatically active Nα-terminal acetyltransferase that co-translationally acetylates iMet-starting protein N-termini with broad but defined substrate specificity; it associates with the NatA complex (Naa10/Naa15) through conserved contacts with both subunits to form NatE, promotes catalytic crosstalk in the human complex, competes kinetically with methionine aminopeptidases to determine iMet retention, is required for sister-chromatid cohesion by facilitating cohesin-sororin interaction (antagonizing NatA in this role), and stabilizes specific substrates (e.g., SLU7) via N-terminal acetylation to protect them from proteasomal degradation."},"narrative":{"mechanistic_narrative":"NAA50 (Naa50/NatE) is a co-translationally acting Nα-terminal acetyltransferase that modifies the N-termini of nascent proteins retaining their initiator methionine, with a defined substrate preference for iMet followed by small or hydrophobic residues (iMet-Lys/Val/Ala/Tyr/Phe/Leu/Ser/Thr; optimal Met-Met) [PMID:25886145, PMID:27484799]. Crystallographic and kinetic analyses across yeast, plant, and human orthologs establish its GNAT active site and catalytic residues, and show that NAA50 acetyltransferase activity is required for its in vivo function [PMID:33400917, PMID:32461302]. NAA50 docks onto the NatA complex via conserved contacts to both the Naa10 and Naa15 subunits to form NatE, an association that promotes catalytic crosstalk in the human complex [PMID:31155310]. By acetylating iMet-starting termini, NAA50 kinetically competes with methionine aminopeptidases to determine iMet retention versus cleavage [PMID:25886145]. Beyond protein-N-terminal acetylation, NAA50 controls sister-chromatid cohesion: it is required for the cohesin-sororin interaction in human cells and antagonizes NatA in this role, and in Drosophila it N-terminally acetylates nascent Scc1 to support proper Scc1-Smc3 cohesin assembly [PMID:27422821, PMID:27996020]. NAA50 also stabilizes specific substrates by N-terminal acetylation, acetylating the splicing factor SLU7 to protect it from ubiquitin-proteasomal degradation and thereby driving cisplatin resistance in bladder cancer cells [PMID:42151695]. Small-molecule inhibitors selective for NAA50 over Naa10 and Naa60 have been defined structurally and shown to engage the enzyme in cells [PMID:32550998].","teleology":[{"year":2015,"claim":"Established that human Naa50 has a distinct substrate logic among NATs by defining its preference for iMet-retaining N-termini and showing it kinetically gates methionine excision.","evidence":"Quantitative N-terminal acetylome profiling in yeast expressing human Naa50 plus in vitro MetAP cleavage assays","pmids":["25886145"],"confidence":"High","gaps":["Did not resolve which physiological substrates depend on iMet retention","Cellular consequences of MetAP competition not measured"]},{"year":2016,"claim":"Connected NAA50 to a chromosome-segregation function distinct from generic Nt-acetylation, showing it is required for cohesin-sororin interaction and antagonizes NatA in cohesion.","evidence":"siRNA knockdown, Co-IP, mitotic arrest assays, and co-depletion epistasis in HeLa cells with in vitro NAT assays","pmids":["27422821"],"confidence":"Medium","gaps":["Direct acetylation substrate underlying cohesion defect not pinned down in human cells","Mechanism of NatA antagonism unresolved"]},{"year":2016,"claim":"Provided a candidate substrate for the cohesion role by showing Naa50/San co-translationally acetylates nascent Scc1 to enable Scc1-Smc3 cohesin assembly.","evidence":"Genetic epistasis and Co-IP of cohesin subunits in Naa50/San-depleted Drosophila","pmids":["27996020"],"confidence":"Medium","gaps":["Site of Scc1 acetylation not mapped","Whether the same mechanism operates in human cohesion not shown"]},{"year":2016,"claim":"Defined the structural basis of human Naa50 substrate selection, identifying Met-Met as optimal and capturing CoA and acetylated peptide products.","evidence":"X-ray crystallography of human Naa50 with a peptide library screen and thermal stability assays","pmids":["27484799"],"confidence":"High","gaps":["Did not address regulation within the NatE complex","Physiological substrate set not enumerated"]},{"year":2019,"claim":"Resolved how Naa50 integrates with NatA, showing conserved contacts to both Naa10 and Naa15 that drive catalytic crosstalk in the human complex.","evidence":"X-ray crystallography of the yeast NatA/Naa50 complex with comparative in vitro activity assays of yeast versus human complexes","pmids":["31155310"],"confidence":"High","gaps":["Functional consequence of crosstalk for substrate selection in cells not established","Why yeast Naa50 activity is compromised mechanistically incomplete"]},{"year":2020,"claim":"Demonstrated that catalytic activity, not merely complex association, is required for NAA50 function in vivo and that NatE substrate specificity is conserved across kingdoms.","evidence":"In vitro acetyltransferase assays with recombinant AtNAA50, E. coli acetylome profiling, and genetic complementation in Arabidopsis naa50 mutants","pmids":["32461302"],"confidence":"High","gaps":["Significance of the in vitro lysine-autoacetyltransferase activity unclear","Plant-specific substrates not defined"]},{"year":2020,"claim":"Delivered selective chemical tools for NAA50 by identifying inhibitors with defined binding modes and cellular target engagement, distinguishing it from related NATs.","evidence":"DNA-encoded library screening, co-crystal structures, biochemical inhibition assays, and cellular target engagement","pmids":["32550998"],"confidence":"High","gaps":["Phenotypic effects of inhibition on cohesion or substrate stability not characterized in this study"]},{"year":2021,"claim":"Defined the active-site architecture and catalytic residues of Naa50 using a bisubstrate analog, while confirming yeast Naa50 is inactive yet retains CoA binding.","evidence":"X-ray crystallography of AtNaa50-AcCoA and bisubstrate complexes with kinetics and active-site mutagenesis","pmids":["33400917"],"confidence":"High","gaps":["Structural basis of substrate scope variation between species not fully resolved"]},{"year":2022,"claim":"Revealed lineage-specific adaptations, with fungal Naa50 carrying terminal extensions that mediate DLC1 binding and NatA-independent ribosome association without forming NatE.","evidence":"X-ray crystallography of CtNaa50 with biochemical binding and ribosome-association assays","pmids":["36142717"],"confidence":"Medium","gaps":["Functional role of DLC1 interaction unknown","Whether human Naa50 has analogous NatA-independent ribosome recruitment not addressed"]},{"year":2023,"claim":"Reported a possible second enzymatic activity, showing recombinant human Naa50 acetylates serotonin in vitro.","evidence":"In vitro SNAT enzyme assay with purified recombinant hNaa50","pmids":["36829878"],"confidence":"Low","gaps":["Single in vitro assay without independent replication","Physiological relevance of SNAT activity in human cells not established","High Km raises questions of in vivo significance"]},{"year":2024,"claim":"Distinguished NAA50 function from NatA in vivo, showing that despite ribosomal NatA association, NAA50 negatively regulates plant immunity independently of NatA activity and salicylic acid.","evidence":"Split-luciferase proximity assay, interactome, transcriptome/proteome profiling, and pathogen resistance assays in Arabidopsis","pmids":["38588051"],"confidence":"Medium","gaps":["Immunity-relevant NAA50 substrates not identified","Whether the immune role is conserved in animals unknown"]},{"year":2026,"claim":"Identified a substrate-stabilization mechanism with disease relevance, showing NAA50 acetylates SLU7 to block its degradation and drive chemoresistance.","evidence":"Co-IP, MS, ubiquitination assays, RIP-qPCR, fractionation, xenografts, and pharmacological inhibition in bladder cancer cells","pmids":["42151695"],"confidence":"Medium","gaps":["Acetylation site on SLU7 not mapped","Generality of N-terminal acetylation as a stabilization mechanism for other substrates not established"]},{"year":null,"claim":"It remains unresolved which endogenous human substrates link NAA50's Nt-acetyltransferase activity to its cohesion, immunity, and substrate-stabilization phenotypes, and whether its candidate second activities (SNAT, lysine autoacetylation) are physiologically operative.","evidence":"No timeline discovery integrates the catalytic, cohesion, and stabilization roles around a defined human substrate set","pmids":[],"confidence":"Low","gaps":["No comprehensive human in-cell substrate map","Mechanistic link between cohesion role and specific acetylated substrate in humans missing","Physiological status of non-canonical activities unclear"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0016740","term_label":"transferase activity","supporting_discovery_ids":[1,2,3,4,11]},{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[1,2,11]}],"localization":[{"term_id":"GO:0005840","term_label":"ribosome","supporting_discovery_ids":[9,10]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[5]}],"pathway":[{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[1,2,4]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[5,6]}],"complexes":["NatE (NatA/Naa50)"],"partners":["NAA10","NAA15","SLU7","DLC1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9GZZ1","full_name":"N-alpha-acetyltransferase 50","aliases":["N-acetyltransferase 13","N-acetyltransferase 5","hNAT5","N-acetyltransferase san homolog","hSAN","N-epsilon-acetyltransferase 50","NatE catalytic subunit"],"length_aa":169,"mass_kda":19.4,"function":"N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:21900231, PubMed:22311970, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity (PubMed:16507339, PubMed:27484799, PubMed:29754825, PubMed:32042062). Does not influence the acetyltransferase activity of NAA10 (PubMed:16507339, PubMed:27484799). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (PubMed:32042062). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821)","subcellular_location":"Cytoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/Q9GZZ1/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/NAA50","classification":"Common Essential","n_dependent_lines":1204,"n_total_lines":1208,"dependency_fraction":0.9966887417218543},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/NAA50","total_profiled":1310},"omim":[{"mim_id":"610834","title":"N-ALPHA-ACETYLTRANSFERASE 50, NatE CATALYTIC SUBUNIT; NAA50","url":"https://www.omim.org/entry/610834"},{"mim_id":"300013","title":"N-ALPHA-ACETYLTRANSFERASE 10, NatA CATALYTIC SUBUNIT; NAA10","url":"https://www.omim.org/entry/300013"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoli","reliability":"Supported"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"skeletal muscle","ntpm":259.1}],"url":"https://www.proteinatlas.org/search/NAA50"},"hgnc":{"alias_symbol":["FLJ13194","NAT5","San"],"prev_symbol":["MAK3","NAT13"]},"alphafold":{"accession":"Q9GZZ1","domains":[{"cath_id":"3.40.630.30","chopping":"5-152","consensus_level":"medium","plddt":97.6794,"start":5,"end":152}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9GZZ1","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9GZZ1-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9GZZ1-F1-predicted_aligned_error_v6.png","plddt_mean":92.19},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=NAA50","jax_strain_url":"https://www.jax.org/strain/search?query=NAA50"},"sequence":{"accession":"Q9GZZ1","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9GZZ1.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9GZZ1/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9GZZ1"}},"corpus_meta":[{"pmid":"25886145","id":"PMC_25886145","title":"N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases.","date":"2015","source":"Proteomics","url":"https://pubmed.ncbi.nlm.nih.gov/25886145","citation_count":53,"is_preprint":false},{"pmid":"31155310","id":"PMC_31155310","title":"Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.","date":"2019","source":"Structure (London, England : 1993)","url":"https://pubmed.ncbi.nlm.nih.gov/31155310","citation_count":44,"is_preprint":false},{"pmid":"32461302","id":"PMC_32461302","title":"NAA50 Is an Enzymatically Active N α-Acetyltransferase That Is Crucial for Development and Regulation of Stress Responses.","date":"2020","source":"Plant physiology","url":"https://pubmed.ncbi.nlm.nih.gov/32461302","citation_count":28,"is_preprint":false},{"pmid":"32550998","id":"PMC_32550998","title":"Characterization of Specific N-α-Acetyltransferase 50 (Naa50) Inhibitors Identified Using a DNA Encoded Library.","date":"2020","source":"ACS medicinal chemistry letters","url":"https://pubmed.ncbi.nlm.nih.gov/32550998","citation_count":28,"is_preprint":false},{"pmid":"32457093","id":"PMC_32457093","title":"Loss of the Acetyltransferase NAA50 Induces Endoplasmic Reticulum Stress and Immune Responses and Suppresses Growth.","date":"2020","source":"Plant physiology","url":"https://pubmed.ncbi.nlm.nih.gov/32457093","citation_count":19,"is_preprint":false},{"pmid":"33400917","id":"PMC_33400917","title":"Structural and functional characterization of the N-terminal acetyltransferase Naa50.","date":"2021","source":"Structure (London, England : 1993)","url":"https://pubmed.ncbi.nlm.nih.gov/33400917","citation_count":15,"is_preprint":false},{"pmid":"27996020","id":"PMC_27996020","title":"Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion.","date":"2016","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/27996020","citation_count":14,"is_preprint":false},{"pmid":"27484799","id":"PMC_27484799","title":"Human Naa50 Protein Displays Broad Substrate Specificity for Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL ANALYSIS USING TETRAPEPTIDE LIBRARY.","date":"2016","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/27484799","citation_count":12,"is_preprint":false},{"pmid":"27422821","id":"PMC_27422821","title":"Opposing Functions of the N-terminal Acetyltransferases Naa50 and NatA in Sister-chromatid Cohesion.","date":"2016","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/27422821","citation_count":11,"is_preprint":false},{"pmid":"36829878","id":"PMC_36829878","title":"Human Naa50 Shows Serotonin N-Acetyltransferase Activity, and Its Overexpression Enhances Melatonin Biosynthesis, Resulting in Osmotic Stress Tolerance in Rice.","date":"2023","source":"Antioxidants (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/36829878","citation_count":4,"is_preprint":false},{"pmid":"36142717","id":"PMC_36142717","title":"Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/36142717","citation_count":3,"is_preprint":false},{"pmid":"38588051","id":"PMC_38588051","title":"Nα-acetyltransferase NAA50 mediates plant immunity independent of the Nα-acetyltransferase A complex.","date":"2024","source":"Plant physiology","url":"https://pubmed.ncbi.nlm.nih.gov/38588051","citation_count":3,"is_preprint":false},{"pmid":"42151695","id":"PMC_42151695","title":"NAA50-mediated SLU7 stabilization promotes cisplatin resistance in bladder cancer via regulating MAP3K3 mRNA nuclear export and p38 MAPK activation.","date":"2026","source":"Cellular oncology (Dordrecht, Netherlands)","url":"https://pubmed.ncbi.nlm.nih.gov/42151695","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8602,"output_tokens":3225,"usd":0.03709,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10629,"output_tokens":3757,"usd":0.073535,"stage2_stop_reason":"end_turn"},"total_usd":0.110625,"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\": 2019,\n      \"finding\": \"X-ray crystal structure of yeast NatA/Naa50 ternary complex shows Naa50 makes evolutionarily conserved contacts to both the Naa10 and Naa15 subunits of NatA; these interactions promote catalytic crosstalk within the human NatA/Naa50 complex but to a lesser extent in the yeast complex where Naa50 activity is compromised.\",\n      \"method\": \"X-ray crystallography of yeast NatA/Naa50 complex; in vitro enzymatic activity assays comparing yeast and human complexes\",\n      \"journal\": \"Structure\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structure with functional validation comparing yeast and human complexes, multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"31155310\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Human Naa50 preferentially Nt-acetylates N-terminal Met (iMet)-starting N-termini including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr; a kinetic competition exists between Naa50 and Met-aminopeptidases (MetAPs), such that Naa50-mediated Nt-acetylation of iMet followed by a small residue blocks subsequent MetAP cleavage.\",\n      \"method\": \"Quantitative N-terminal acetylome profiling in yeast expressing human Naa50 versus wild-type or Naa50-knockout yeast; in vitro MetAP cleavage assays\",\n      \"journal\": \"Proteomics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — quantitative proteomics with genetic manipulation combined with in vitro biochemical validation, multiple orthogonal methods\",\n      \"pmids\": [\"25886145\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Crystal structure of human Naa50 revealed co-purified CoA and an acetylated tetrapeptide (AcMMXX); biochemical analysis of a tetrapeptide library showed that Met-Met in positions 1–2 is the optimal substrate, and Naa50 acetylates all MXAA peptides except MPAA.\",\n      \"method\": \"X-ray crystallography; biochemical peptide library screen and thermal stability assays\",\n      \"journal\": \"Journal of Biological Chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure combined with systematic biochemical substrate profiling, single lab but two orthogonal methods\",\n      \"pmids\": [\"27484799\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"High-resolution X-ray crystal structures of Arabidopsis Naa50 (AtNaa50) in complex with AcCoA and a bisubstrate analog defined its active site and substrate specificity; functionally important catalytic residues were identified by mutagenesis; yeast Naa50 is catalytically inactive yet retains CoA conjugate binding.\",\n      \"method\": \"X-ray crystallography (AtNaa50-AcCoA and bisubstrate analog complexes); enzymatic kinetics; active-site mutagenesis\",\n      \"journal\": \"Structure\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structures with bisubstrate analog, enzymatic kinetics, and mutagenesis in a single rigorous study\",\n      \"pmids\": [\"33400917\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Purified Arabidopsis NAA50 (AtNAA50) displays both Nα-terminal acetyltransferase activity and lysine-ε-autoacetyltransferase activity in vitro; global N-acetylome profiling in E. coli expressing AtNAA50 confirmed conservation of NatE substrate specificity between plants and humans; the catalytically inactive yeast Naa50 failed to complement naa50 mutant plants, demonstrating enzymatic activity is required for NAA50 function in planta.\",\n      \"method\": \"In vitro acetyltransferase assay with purified recombinant AtNAA50; N-acetylome profiling in E. coli; genetic complementation in Arabidopsis naa50 mutant lines\",\n      \"journal\": \"Plant Physiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — in vitro enzymatic assay plus in vivo acetylome profiling plus genetic rescue experiment, multiple orthogonal methods\",\n      \"pmids\": [\"32461302\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Depletion of Naa50 in HeLa cells weakens the interaction between cohesin and its positive regulator sororin, causing sister-chromatid cohesion defects in S phase; co-depletion of NatA rescues the cohesion defects and mitotic arrest caused by Naa50 depletion, demonstrating that NatA and Naa50 play antagonistic roles in cohesion; purified NatA and Naa50 do not affect each other's NAT activity in vitro.\",\n      \"method\": \"siRNA knockdown in HeLa cells; co-immunoprecipitation; mitotic arrest assays; in vitro NAT activity assays with purified proteins\",\n      \"journal\": \"Journal of Biological Chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — epistasis by co-depletion with defined cellular phenotype rescue, Co-IP, and in vitro enzymatic assay, single lab\",\n      \"pmids\": [\"27422821\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Genetic and biochemical evidence in Drosophila indicates that Naa50/San N-terminally acetylates the nascent Scc1 (cohesin subunit) polypeptide co-translationally, and that this modification is required for the correct interaction between cohesin subunits Scc1 and Smc3 and for sister-chromatid cohesion during tissue proliferation.\",\n      \"method\": \"Genetic epistasis in Drosophila; biochemical co-immunoprecipitation of cohesin subunits in Naa50/San-depleted cells\",\n      \"journal\": \"Scientific Reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — genetic and biochemical approaches in model organism, single lab, two complementary methods\",\n      \"pmids\": [\"27996020\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Two novel small-molecule inhibitors of Naa50 were identified; co-crystal structures with Naa50 and biochemical assays defined their mechanism of action and selectivity over related enzymes Naa10 and Naa60; cellular target engagement was confirmed for compound 4a.\",\n      \"method\": \"DNA-encoded library screening; co-crystal structures; biochemical inhibition assays; cellular target engagement experiments\",\n      \"journal\": \"ACS Medicinal Chemistry Letters\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — co-crystal structures with mechanistic biochemistry and cellular confirmation, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"32550998\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Purified recombinant human Naa50 displays serotonin N-acetyltransferase (SNAT) activity in vitro (Km = 986 μM, Vmax = 1800 pmol/min/mg), in addition to its Nα-terminal acetyltransferase activity, indicating enzymatic bifunctionality.\",\n      \"method\": \"In vitro SNAT enzyme assay with purified recombinant hNaa50 expressed in E. coli\",\n      \"journal\": \"Antioxidants\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 1 / Weak — single in vitro biochemical assay, single lab, no independent replication, functional relevance in human cells not established\",\n      \"pmids\": [\"36829878\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"In filamentous fungi (Chaetomium thermophilum), Naa50 contains significant N- and C-terminal extensions beyond the conserved GNAT domain; the elongated N-terminus increases thermostability and binds to dynein light chain protein 1 (DLC1); conserved positive patches in the C-terminus allow ribosome binding independent of NatA; CtNaa50 does not form a NatE complex with NatA.\",\n      \"method\": \"X-ray crystallography of CtNaa50; biochemical binding assays for DLC1 interaction and ribosome binding; structural comparison with other Naa50 homologs\",\n      \"journal\": \"International Journal of Molecular Sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — crystal structure combined with biochemical binding assays, single lab, multiple methods\",\n      \"pmids\": [\"36142717\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"In Arabidopsis, AtNAA50 associates with NatA at ribosomes (demonstrated by split-luciferase proximity assay in planta and interactome analysis), yet AtNAA50 and AtNatA/HYPK exert distinct in vivo functions: AtNAA50 negatively regulates plant immunity independently of salicylic acid accumulation and independently of NatA activity, and does not modulate drought tolerance or protein stability like NatA/HYPK.\",\n      \"method\": \"Split-luciferase proximity assay in planta; interactome analysis (AtNAA50 pull-down); transcriptome and proteome profiling of amiNAA50 plants; pathogen resistance assays\",\n      \"journal\": \"Plant Physiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — split-luciferase interaction, interactome, and functional genetic evidence, single lab with multiple complementary approaches\",\n      \"pmids\": [\"38588051\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"NAA50 catalyzes N-terminal acetylation of the splicing factor SLU7, preventing its ubiquitin-proteasomal degradation and stabilizing SLU7 protein in bladder cancer cells; NAA50-stabilized SLU7 promotes MAP3K3 mRNA nuclear export and p38 MAPK activation to drive cisplatin resistance; pharmacological inhibition of NAA50 destabilizes SLU7 and reverses cisplatin resistance in vitro and in vivo.\",\n      \"method\": \"Co-immunoprecipitation; mass spectrometry; ubiquitination assays; RNA immunoprecipitation (RIP-qPCR); nucleocytoplasmic fractionation; xenograft models; pharmacological NAA50 inhibition\",\n      \"journal\": \"Cellular Oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP and MS identification of interaction plus multiple functional assays, single lab with orthogonal methods\",\n      \"pmids\": [\"42151695\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"NAA50 (Naa50/NatE) is an enzymatically active Nα-terminal acetyltransferase that co-translationally acetylates iMet-starting protein N-termini with broad but defined substrate specificity; it associates with the NatA complex (Naa10/Naa15) through conserved contacts with both subunits to form NatE, promotes catalytic crosstalk in the human complex, competes kinetically with methionine aminopeptidases to determine iMet retention, is required for sister-chromatid cohesion by facilitating cohesin-sororin interaction (antagonizing NatA in this role), and stabilizes specific substrates (e.g., SLU7) via N-terminal acetylation to protect them from proteasomal degradation.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"NAA50 (Naa50/NatE) is a co-translationally acting Nα-terminal acetyltransferase that modifies the N-termini of nascent proteins retaining their initiator methionine, with a defined substrate preference for iMet followed by small or hydrophobic residues (iMet-Lys/Val/Ala/Tyr/Phe/Leu/Ser/Thr; optimal Met-Met) [#1, #2]. Crystallographic and kinetic analyses across yeast, plant, and human orthologs establish its GNAT active site and catalytic residues, and show that NAA50 acetyltransferase activity is required for its in vivo function [#3, #4]. NAA50 docks onto the NatA complex via conserved contacts to both the Naa10 and Naa15 subunits to form NatE, an association that promotes catalytic crosstalk in the human complex [#0]. By acetylating iMet-starting termini, NAA50 kinetically competes with methionine aminopeptidases to determine iMet retention versus cleavage [#1]. Beyond protein-N-terminal acetylation, NAA50 controls sister-chromatid cohesion: it is required for the cohesin-sororin interaction in human cells and antagonizes NatA in this role, and in Drosophila it N-terminally acetylates nascent Scc1 to support proper Scc1-Smc3 cohesin assembly [#5, #6]. NAA50 also stabilizes specific substrates by N-terminal acetylation, acetylating the splicing factor SLU7 to protect it from ubiquitin-proteasomal degradation and thereby driving cisplatin resistance in bladder cancer cells [#11]. Small-molecule inhibitors selective for NAA50 over Naa10 and Naa60 have been defined structurally and shown to engage the enzyme in cells [#7].\",\n  \"teleology\": [\n    {\n      \"year\": 2015,\n      \"claim\": \"Established that human Naa50 has a distinct substrate logic among NATs by defining its preference for iMet-retaining N-termini and showing it kinetically gates methionine excision.\",\n      \"evidence\": \"Quantitative N-terminal acetylome profiling in yeast expressing human Naa50 plus in vitro MetAP cleavage assays\",\n      \"pmids\": [\"25886145\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not resolve which physiological substrates depend on iMet retention\", \"Cellular consequences of MetAP competition not measured\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Connected NAA50 to a chromosome-segregation function distinct from generic Nt-acetylation, showing it is required for cohesin-sororin interaction and antagonizes NatA in cohesion.\",\n      \"evidence\": \"siRNA knockdown, Co-IP, mitotic arrest assays, and co-depletion epistasis in HeLa cells with in vitro NAT assays\",\n      \"pmids\": [\"27422821\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct acetylation substrate underlying cohesion defect not pinned down in human cells\", \"Mechanism of NatA antagonism unresolved\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Provided a candidate substrate for the cohesion role by showing Naa50/San co-translationally acetylates nascent Scc1 to enable Scc1-Smc3 cohesin assembly.\",\n      \"evidence\": \"Genetic epistasis and Co-IP of cohesin subunits in Naa50/San-depleted Drosophila\",\n      \"pmids\": [\"27996020\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Site of Scc1 acetylation not mapped\", \"Whether the same mechanism operates in human cohesion not shown\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Defined the structural basis of human Naa50 substrate selection, identifying Met-Met as optimal and capturing CoA and acetylated peptide products.\",\n      \"evidence\": \"X-ray crystallography of human Naa50 with a peptide library screen and thermal stability assays\",\n      \"pmids\": [\"27484799\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not address regulation within the NatE complex\", \"Physiological substrate set not enumerated\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Resolved how Naa50 integrates with NatA, showing conserved contacts to both Naa10 and Naa15 that drive catalytic crosstalk in the human complex.\",\n      \"evidence\": \"X-ray crystallography of the yeast NatA/Naa50 complex with comparative in vitro activity assays of yeast versus human complexes\",\n      \"pmids\": [\"31155310\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Functional consequence of crosstalk for substrate selection in cells not established\", \"Why yeast Naa50 activity is compromised mechanistically incomplete\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Demonstrated that catalytic activity, not merely complex association, is required for NAA50 function in vivo and that NatE substrate specificity is conserved across kingdoms.\",\n      \"evidence\": \"In vitro acetyltransferase assays with recombinant AtNAA50, E. coli acetylome profiling, and genetic complementation in Arabidopsis naa50 mutants\",\n      \"pmids\": [\"32461302\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Significance of the in vitro lysine-autoacetyltransferase activity unclear\", \"Plant-specific substrates not defined\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Delivered selective chemical tools for NAA50 by identifying inhibitors with defined binding modes and cellular target engagement, distinguishing it from related NATs.\",\n      \"evidence\": \"DNA-encoded library screening, co-crystal structures, biochemical inhibition assays, and cellular target engagement\",\n      \"pmids\": [\"32550998\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Phenotypic effects of inhibition on cohesion or substrate stability not characterized in this study\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Defined the active-site architecture and catalytic residues of Naa50 using a bisubstrate analog, while confirming yeast Naa50 is inactive yet retains CoA binding.\",\n      \"evidence\": \"X-ray crystallography of AtNaa50-AcCoA and bisubstrate complexes with kinetics and active-site mutagenesis\",\n      \"pmids\": [\"33400917\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of substrate scope variation between species not fully resolved\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Revealed lineage-specific adaptations, with fungal Naa50 carrying terminal extensions that mediate DLC1 binding and NatA-independent ribosome association without forming NatE.\",\n      \"evidence\": \"X-ray crystallography of CtNaa50 with biochemical binding and ribosome-association assays\",\n      \"pmids\": [\"36142717\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional role of DLC1 interaction unknown\", \"Whether human Naa50 has analogous NatA-independent ribosome recruitment not addressed\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Reported a possible second enzymatic activity, showing recombinant human Naa50 acetylates serotonin in vitro.\",\n      \"evidence\": \"In vitro SNAT enzyme assay with purified recombinant hNaa50\",\n      \"pmids\": [\"36829878\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single in vitro assay without independent replication\", \"Physiological relevance of SNAT activity in human cells not established\", \"High Km raises questions of in vivo significance\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Distinguished NAA50 function from NatA in vivo, showing that despite ribosomal NatA association, NAA50 negatively regulates plant immunity independently of NatA activity and salicylic acid.\",\n      \"evidence\": \"Split-luciferase proximity assay, interactome, transcriptome/proteome profiling, and pathogen resistance assays in Arabidopsis\",\n      \"pmids\": [\"38588051\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Immunity-relevant NAA50 substrates not identified\", \"Whether the immune role is conserved in animals unknown\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Identified a substrate-stabilization mechanism with disease relevance, showing NAA50 acetylates SLU7 to block its degradation and drive chemoresistance.\",\n      \"evidence\": \"Co-IP, MS, ubiquitination assays, RIP-qPCR, fractionation, xenografts, and pharmacological inhibition in bladder cancer cells\",\n      \"pmids\": [\"42151695\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Acetylation site on SLU7 not mapped\", \"Generality of N-terminal acetylation as a stabilization mechanism for other substrates not established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unresolved which endogenous human substrates link NAA50's Nt-acetyltransferase activity to its cohesion, immunity, and substrate-stabilization phenotypes, and whether its candidate second activities (SNAT, lysine autoacetylation) are physiologically operative.\",\n      \"evidence\": \"No timeline discovery integrates the catalytic, cohesion, and stabilization roles around a defined human substrate set\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No comprehensive human in-cell substrate map\", \"Mechanistic link between cohesion role and specific acetylated substrate in humans missing\", \"Physiological status of non-canonical activities unclear\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0016740\", \"supporting_discovery_ids\": [1, 2, 3, 4, 11]},\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [1, 2, 11]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005840\", \"supporting_discovery_ids\": [9, 10]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [1, 2, 4]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [5, 6]}\n    ],\n    \"complexes\": [\"NatE (NatA/Naa50)\"],\n    \"partners\": [\"NAA10\", \"NAA15\", \"SLU7\", \"DLC1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":7,"faith_total":7,"faith_pct":100.0}}