{"gene":"RPL37A","run_date":"2026-06-10T07:46:26","timeline":{"discoveries":[{"year":1989,"finding":"Rat ribosomal protein L37a contains 91 amino acids (NH2-terminal methionine is removed after translation) and has a molecular mass of 10143 Da, as confirmed by both cDNA sequencing and direct NH2-terminal amino acid sequencing of the protein.","method":"Recombinant cDNA sequencing and direct NH2-terminal amino acid sequencing","journal":"European journal of biochemistry","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — direct protein sequencing and cDNA confirmation, single lab, single study","pmids":["2546769"],"is_preprint":false},{"year":1992,"finding":"Chicken ribosomal protein L37a contains a Cys2-Cys2 zinc finger motif, implicated in protein-RNA interaction, as deduced from cDNA and genomic DNA sequence.","method":"cDNA and genomic DNA sequencing with sequence motif analysis","journal":"Biochimica et biophysica acta","confidence":"Low","confidence_rationale":"Tier 4 / Weak — zinc finger role in RNA interaction inferred from sequence, not experimentally validated","pmids":["1380836"],"is_preprint":false},{"year":1993,"finding":"Rat ribosomal protein L37 (a paralog, not L37a) has 96 amino acids, NH2-terminal methionine removed post-translationally, and contains a single C2-C2 zinc finger-like motif; the L37 gene has ~13–14 copies in nuclear DNA.","method":"Recombinant cDNA sequencing and Southern blot hybridization","journal":"Biochemical and biophysical research communications","confidence":"Low","confidence_rationale":"Tier 4 / Weak — sequence-based inference of zinc finger function, no direct functional assay; note this is L37 not L37a","pmids":["8484768"],"is_preprint":false},{"year":1993,"finding":"The chicken RPL37A gene spans 2626 bp distributed across four exons and three introns; the region from nucleotides -78 to -35 in the 5'-flanking region is important for promoter activity and serves as a binding site for nuclear proteins.","method":"Nucleotide sequencing, promoter deletion analysis (CAT reporter assay), and DNase I footprinting","journal":"European journal of biochemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — promoter activity mapped by deletion/reporter assay and protein-binding confirmed by DNase I protection, single lab","pmids":["8477735"],"is_preprint":false},{"year":1996,"finding":"Transcriptional control elements of the chicken RPL37A gene were mapped: the region -120 to +168 is required for maximal promoter activity, and nine protein-binding regions distributed from -122 to +195 were identified by DNase I footprinting.","method":"CAT reporter transfection assay and DNase I protection (footprinting) assay in chicken cell line","journal":"European journal of biochemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional promoter mapping with reporter assay and DNase I footprinting, single lab, two orthogonal methods","pmids":["8665930"],"is_preprint":false},{"year":2022,"finding":"In yeast, the dedicated chaperones Puf6 and Loc1 bind RPL43 (eL43/RPL37A ortholog) mRNA individually (not as a dimer complex as with other mRNAs), and this binding negatively regulates eL43 production by decreasing RPL43A/B mRNA stability and translation.","method":"RNA immunoprecipitation, mRNA stability assays, translation reporter assays, and deletion mutant analysis (loc1Δ, puf6Δ)","journal":"Journal of biochemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal binding and functional consequences shown with multiple methods (RIP, mRNA stability, translation), single lab","pmids":["34661244"],"is_preprint":false}],"current_model":"RPL37A (eL43) is a component of the 60S ribosomal subunit that contains a conserved C2-C2 zinc finger motif implicated in RNA interaction; its transcription is controlled by specific promoter elements that recruit nuclear proteins, and in yeast its protein level is post-transcriptionally regulated by the chaperones Puf6 and Loc1, which bind RPL43 mRNA individually to suppress mRNA stability and translation, ensuring appropriate stoichiometric supply of the protein for ribosome assembly."},"narrative":{"mechanistic_narrative":"RPL37A (eL43) is a small basic component of the 60S ribosomal subunit, defined as a ~10 kDa, 91-residue protein whose N-terminal methionine is removed after translation [PMID:2546769]. It carries a conserved Cys2-Cys2 zinc finger motif implicated in protein-RNA interaction, identified from sequence analysis of the chicken ortholog [PMID:1380836]. Transcription of the gene is governed by defined promoter architecture: a proximal 5'-flanking region (nucleotides -78 to -35) is required for promoter activity and is bound by nuclear proteins, with maximal activity mapping to -120 to +168 and nine distinct protein-binding footprints distributed from -122 to +195 [PMID:8477735, PMID:8665930]. Beyond transcriptional control, supply of the protein is set post-transcriptionally: in yeast, the dedicated chaperones Puf6 and Loc1 each bind RPL43 mRNA individually to lower its stability and translation, tuning eL43 output for ribosome assembly [PMID:34661244]. No direct structural or functional dissection of the human zinc finger or of RPL37A's role within the assembled ribosome has been characterized in the available corpus.","teleology":[{"year":1989,"claim":"Established the primary identity of the protein, fixing its length, mass, and post-translational N-terminal processing as a basis for all later structural and functional work.","evidence":"Recombinant cDNA sequencing and direct NH2-terminal protein sequencing of rat L37a","pmids":["2546769"],"confidence":"Medium","gaps":["No functional role within the ribosome assigned","Single species, single lab characterization","No structural model of the protein"]},{"year":1992,"claim":"Identified a Cys2-Cys2 zinc finger motif from sequence, raising the hypothesis that the protein contacts RNA through this motif.","evidence":"cDNA and genomic DNA sequencing with motif analysis of chicken L37a","pmids":["1380836"],"confidence":"Low","gaps":["Zinc finger-RNA interaction inferred from sequence, not experimentally validated","No demonstration of zinc binding","No identification of any RNA partner"]},{"year":1993,"claim":"Mapped the gene's exon-intron structure and localized a proximal promoter element bound by nuclear proteins, beginning to define how the gene's transcription is controlled.","evidence":"Nucleotide sequencing, CAT reporter promoter deletion, and DNase I footprinting of the chicken gene","pmids":["8477735"],"confidence":"Medium","gaps":["Identity of the bound nuclear proteins not determined","Restricted to chicken; human regulatory architecture not addressed"]},{"year":1996,"claim":"Extended the promoter map to define the full region needed for maximal activity and resolved nine discrete protein-binding sites, refining the transcriptional control model.","evidence":"CAT reporter transfection and DNase I protection assays in a chicken cell line","pmids":["8665930"],"confidence":"Medium","gaps":["Trans-acting factors at the nine footprints not identified","Functional contribution of individual footprints to regulation not dissected"]},{"year":2022,"claim":"Revealed a post-transcriptional regulatory layer, showing that chaperones Puf6 and Loc1 each bind the mRNA to limit protein output, linking eL43 abundance control to ribosome assembly.","evidence":"RNA immunoprecipitation, mRNA stability and translation reporter assays, and loc1Δ/puf6Δ deletion analysis in yeast","pmids":["34661244"],"confidence":"Medium","gaps":["Demonstrated in yeast ortholog; conservation to human RPL37A not tested","Mechanism by which individual binding (vs dimer) suppresses translation unresolved","Connection to assembly stoichiometry not directly measured"]},{"year":null,"claim":"The protein's role within the assembled 60S subunit and the function of its zinc finger in human ribosomes remain undefined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural placement of eL43 in the human ribosome in the corpus","No experimental test of zinc finger-RNA contact","No phenotype or disease association characterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[1]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005840","term_label":"ribosome","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[5]}],"complexes":["60S ribosomal subunit"],"partners":["PUF6","LOC1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P61513","full_name":"Large ribosomal subunit protein eL43","aliases":["60S ribosomal protein L37a"],"length_aa":92,"mass_kda":10.3,"function":"Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/P61513/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/RPL37A","classification":"Common Essential","n_dependent_lines":1208,"n_total_lines":1208,"dependency_fraction":1.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MRTO4","stoichiometry":10.0},{"gene":"RPL11","stoichiometry":10.0},{"gene":"RPL4","stoichiometry":10.0},{"gene":"RPL5","stoichiometry":10.0},{"gene":"RPS16","stoichiometry":10.0},{"gene":"CAPRIN1","stoichiometry":4.0},{"gene":"DRG1","stoichiometry":4.0},{"gene":"ENY2","stoichiometry":4.0},{"gene":"METAP2","stoichiometry":4.0},{"gene":"RACK1","stoichiometry":4.0}],"url":"https://opencell.sf.czbiohub.org/search/RPL37A","total_profiled":1310},"omim":[{"mim_id":"613314","title":"RIBOSOMAL PROTEIN L37A; RPL37A","url":"https://www.omim.org/entry/613314"},{"mim_id":"612845","title":"SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 5; SENP5","url":"https://www.omim.org/entry/612845"},{"mim_id":"612844","title":"SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 3; SENP3","url":"https://www.omim.org/entry/612844"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Endoplasmic reticulum","reliability":"Approved"},{"location":"Cytosol","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/RPL37A"},"hgnc":{"alias_symbol":["L37A","eL43"],"prev_symbol":[]},"alphafold":{"accession":"P61513","domains":[{"cath_id":"2.20.25.30","chopping":"36-92","consensus_level":"medium","plddt":96.6025,"start":36,"end":92}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P61513","model_url":"https://alphafold.ebi.ac.uk/files/AF-P61513-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P61513-F1-predicted_aligned_error_v6.png","plddt_mean":96.31},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=RPL37A","jax_strain_url":"https://www.jax.org/strain/search?query=RPL37A"},"sequence":{"accession":"P61513","fasta_url":"https://rest.uniprot.org/uniprotkb/P61513.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P61513/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P61513"}},"corpus_meta":[{"pmid":"8484768","id":"PMC_8484768","title":"The primary structure of L37--a rat ribosomal protein with a zinc finger-like motif.","date":"1993","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/8484768","citation_count":12,"is_preprint":false},{"pmid":"1840541","id":"PMC_1840541","title":"Screening a yeast promoter library leads to the isolation of the RP29/L32 and SNR17B/RPL37A divergent promoters and the discovery of a gene encoding ribosomal protein L37.","date":"1991","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/1840541","citation_count":10,"is_preprint":false},{"pmid":"2546769","id":"PMC_2546769","title":"The primary structure of rat ribosomal protein L37a.","date":"1989","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/2546769","citation_count":10,"is_preprint":false},{"pmid":"32951185","id":"PMC_32951185","title":"Analysis of RPL37A, MTSS1, and HTRA1 expression as potential markers for pathologic complete response and survival.","date":"2020","source":"Breast cancer (Tokyo, Japan)","url":"https://pubmed.ncbi.nlm.nih.gov/32951185","citation_count":9,"is_preprint":false},{"pmid":"8477735","id":"PMC_8477735","title":"The structure of the gene encoding chicken ribosomal protein L37a.","date":"1993","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/8477735","citation_count":9,"is_preprint":false},{"pmid":"8665930","id":"PMC_8665930","title":"A characterization of transcriptional regulatory elements in chicken ribosomal protein L37a gene.","date":"1996","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/8665930","citation_count":8,"is_preprint":false},{"pmid":"8666239","id":"PMC_8666239","title":"The intron-containing ribosomal protein-encoding genes L5, L7a and L37a are unlinked in chicken.","date":"1996","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/8666239","citation_count":8,"is_preprint":false},{"pmid":"1380836","id":"PMC_1380836","title":"The primary structure of chicken ribosomal protein L37a.","date":"1992","source":"Biochimica et biophysica acta","url":"https://pubmed.ncbi.nlm.nih.gov/1380836","citation_count":7,"is_preprint":false},{"pmid":"9836437","id":"PMC_9836437","title":"The characterization of two Dictyostelium discoideum genes encoding ribosomal proteins with sequence similarity to rat L27a and L37a.","date":"1998","source":"Bioscience, biotechnology, and biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/9836437","citation_count":4,"is_preprint":false},{"pmid":"12594966","id":"PMC_12594966","title":"Characterization of cDNA encoding a L37a ribosomal protein from Taenia crassiceps and its potential use in phylogenetic reconstructions.","date":"2002","source":"Experimental parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/12594966","citation_count":2,"is_preprint":false},{"pmid":"10373627","id":"PMC_10373627","title":"Ribosomal Proteins S27E, P2, and L37A from Marine Invertebrates.","date":"1999","source":"Marine biotechnology (New York, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/10373627","citation_count":2,"is_preprint":false},{"pmid":"10571043","id":"PMC_10571043","title":"An enhancer trap line identifies the Drosophila homolog of the L37a ribosomal protein.","date":"1999","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/10571043","citation_count":1,"is_preprint":false},{"pmid":"34661244","id":"PMC_34661244","title":"The dedicated chaperones of eL43, Puf6 and Loc1 can also bind RPL43 mRNA and regulate the production of this ribosomal protein.","date":"2022","source":"Journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/34661244","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6051,"output_tokens":1327,"usd":0.019029,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7994,"output_tokens":1920,"usd":0.043985,"stage2_stop_reason":"end_turn"},"total_usd":0.063014,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1989,\n      \"finding\": \"Rat ribosomal protein L37a contains 91 amino acids (NH2-terminal methionine is removed after translation) and has a molecular mass of 10143 Da, as confirmed by both cDNA sequencing and direct NH2-terminal amino acid sequencing of the protein.\",\n      \"method\": \"Recombinant cDNA sequencing and direct NH2-terminal amino acid sequencing\",\n      \"journal\": \"European journal of biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — direct protein sequencing and cDNA confirmation, single lab, single study\",\n      \"pmids\": [\"2546769\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1992,\n      \"finding\": \"Chicken ribosomal protein L37a contains a Cys2-Cys2 zinc finger motif, implicated in protein-RNA interaction, as deduced from cDNA and genomic DNA sequence.\",\n      \"method\": \"cDNA and genomic DNA sequencing with sequence motif analysis\",\n      \"journal\": \"Biochimica et biophysica acta\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — zinc finger role in RNA interaction inferred from sequence, not experimentally validated\",\n      \"pmids\": [\"1380836\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1993,\n      \"finding\": \"Rat ribosomal protein L37 (a paralog, not L37a) has 96 amino acids, NH2-terminal methionine removed post-translationally, and contains a single C2-C2 zinc finger-like motif; the L37 gene has ~13–14 copies in nuclear DNA.\",\n      \"method\": \"Recombinant cDNA sequencing and Southern blot hybridization\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — sequence-based inference of zinc finger function, no direct functional assay; note this is L37 not L37a\",\n      \"pmids\": [\"8484768\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1993,\n      \"finding\": \"The chicken RPL37A gene spans 2626 bp distributed across four exons and three introns; the region from nucleotides -78 to -35 in the 5'-flanking region is important for promoter activity and serves as a binding site for nuclear proteins.\",\n      \"method\": \"Nucleotide sequencing, promoter deletion analysis (CAT reporter assay), and DNase I footprinting\",\n      \"journal\": \"European journal of biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — promoter activity mapped by deletion/reporter assay and protein-binding confirmed by DNase I protection, single lab\",\n      \"pmids\": [\"8477735\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1996,\n      \"finding\": \"Transcriptional control elements of the chicken RPL37A gene were mapped: the region -120 to +168 is required for maximal promoter activity, and nine protein-binding regions distributed from -122 to +195 were identified by DNase I footprinting.\",\n      \"method\": \"CAT reporter transfection assay and DNase I protection (footprinting) assay in chicken cell line\",\n      \"journal\": \"European journal of biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional promoter mapping with reporter assay and DNase I footprinting, single lab, two orthogonal methods\",\n      \"pmids\": [\"8665930\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"In yeast, the dedicated chaperones Puf6 and Loc1 bind RPL43 (eL43/RPL37A ortholog) mRNA individually (not as a dimer complex as with other mRNAs), and this binding negatively regulates eL43 production by decreasing RPL43A/B mRNA stability and translation.\",\n      \"method\": \"RNA immunoprecipitation, mRNA stability assays, translation reporter assays, and deletion mutant analysis (loc1Δ, puf6Δ)\",\n      \"journal\": \"Journal of biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal binding and functional consequences shown with multiple methods (RIP, mRNA stability, translation), single lab\",\n      \"pmids\": [\"34661244\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"RPL37A (eL43) is a component of the 60S ribosomal subunit that contains a conserved C2-C2 zinc finger motif implicated in RNA interaction; its transcription is controlled by specific promoter elements that recruit nuclear proteins, and in yeast its protein level is post-transcriptionally regulated by the chaperones Puf6 and Loc1, which bind RPL43 mRNA individually to suppress mRNA stability and translation, ensuring appropriate stoichiometric supply of the protein for ribosome assembly.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RPL37A (eL43) is a small basic component of the 60S ribosomal subunit, defined as a ~10 kDa, 91-residue protein whose N-terminal methionine is removed after translation [#0]. It carries a conserved Cys2-Cys2 zinc finger motif implicated in protein-RNA interaction, identified from sequence analysis of the chicken ortholog [#1]. Transcription of the gene is governed by defined promoter architecture: a proximal 5'-flanking region (nucleotides -78 to -35) is required for promoter activity and is bound by nuclear proteins, with maximal activity mapping to -120 to +168 and nine distinct protein-binding footprints distributed from -122 to +195 [#3, #4]. Beyond transcriptional control, supply of the protein is set post-transcriptionally: in yeast, the dedicated chaperones Puf6 and Loc1 each bind RPL43 mRNA individually to lower its stability and translation, tuning eL43 output for ribosome assembly [#5]. No direct structural or functional dissection of the human zinc finger or of RPL37A's role within the assembled ribosome has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 1989,\n      \"claim\": \"Established the primary identity of the protein, fixing its length, mass, and post-translational N-terminal processing as a basis for all later structural and functional work.\",\n      \"evidence\": \"Recombinant cDNA sequencing and direct NH2-terminal protein sequencing of rat L37a\",\n      \"pmids\": [\"2546769\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No functional role within the ribosome assigned\",\n        \"Single species, single lab characterization\",\n        \"No structural model of the protein\"\n      ]\n    },\n    {\n      \"year\": 1992,\n      \"claim\": \"Identified a Cys2-Cys2 zinc finger motif from sequence, raising the hypothesis that the protein contacts RNA through this motif.\",\n      \"evidence\": \"cDNA and genomic DNA sequencing with motif analysis of chicken L37a\",\n      \"pmids\": [\"1380836\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Zinc finger-RNA interaction inferred from sequence, not experimentally validated\",\n        \"No demonstration of zinc binding\",\n        \"No identification of any RNA partner\"\n      ]\n    },\n    {\n      \"year\": 1993,\n      \"claim\": \"Mapped the gene's exon-intron structure and localized a proximal promoter element bound by nuclear proteins, beginning to define how the gene's transcription is controlled.\",\n      \"evidence\": \"Nucleotide sequencing, CAT reporter promoter deletion, and DNase I footprinting of the chicken gene\",\n      \"pmids\": [\"8477735\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Identity of the bound nuclear proteins not determined\",\n        \"Restricted to chicken; human regulatory architecture not addressed\"\n      ]\n    },\n    {\n      \"year\": 1996,\n      \"claim\": \"Extended the promoter map to define the full region needed for maximal activity and resolved nine discrete protein-binding sites, refining the transcriptional control model.\",\n      \"evidence\": \"CAT reporter transfection and DNase I protection assays in a chicken cell line\",\n      \"pmids\": [\"8665930\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Trans-acting factors at the nine footprints not identified\",\n        \"Functional contribution of individual footprints to regulation not dissected\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Revealed a post-transcriptional regulatory layer, showing that chaperones Puf6 and Loc1 each bind the mRNA to limit protein output, linking eL43 abundance control to ribosome assembly.\",\n      \"evidence\": \"RNA immunoprecipitation, mRNA stability and translation reporter assays, and loc1Δ/puf6Δ deletion analysis in yeast\",\n      \"pmids\": [\"34661244\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Demonstrated in yeast ortholog; conservation to human RPL37A not tested\",\n        \"Mechanism by which individual binding (vs dimer) suppresses translation unresolved\",\n        \"Connection to assembly stoichiometry not directly measured\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The protein's role within the assembled 60S subunit and the function of its zinc finger in human ribosomes remain undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural placement of eL43 in the human ribosome in the corpus\",\n        \"No experimental test of zinc finger-RNA contact\",\n        \"No phenotype or disease association characterized\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005840\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"complexes\": [\n      \"60S ribosomal subunit\"\n    ],\n    \"partners\": [\n      \"Puf6\",\n      \"Loc1\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}