{"gene":"RPL36AL","run_date":"2026-06-10T07:46:26","timeline":{"discoveries":[{"year":2002,"finding":"RPL36AL is a functional autosomal retrotransposed copy of the X-linked ribosomal protein gene RPL36A, lacking introns in its coding region, and is ubiquitously expressed (unlike the testis-specific paralogs RPL10L and RPL39L). It encodes a protein with 92-99% amino acid identity to the X-linked progenitor.","method":"Northern blot, PCR, sequence analysis of gene structure","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Northern blot and PCR with sequence analysis in single study; ubiquitous expression and retrotransposition origin established by direct experiment","pmids":["12490704"],"is_preprint":false},{"year":2009,"finding":"RPL36AL (ribosomal protein L36a-like) contacts the CCA end of P-site bound tRNA on human 80S ribosomes, as demonstrated by periodate-oxidized tRNA (tRNAox) zero-length affinity crosslinking followed by mass spectrometry identification. Intact tRNA competed with tRNAox to prevent crosslinking, confirming specificity. RPL36AL belongs to the L44e family of ribosomal proteins.","method":"Periodate-oxidized tRNA (zero-length affinity labeling/crosslinking), mass spectrometry, competition assay with intact tRNA","journal":"Biochimie","confidence":"High","confidence_rationale":"Tier 1 / Strong — zero-length crosslinking with competition control and MS identification; replicated and extended in subsequent studies","pmids":["19647033"],"is_preprint":false},{"year":2012,"finding":"RPL36AL crosslinks specifically to the CCA end (C74, C75, and A76) of tRNA positioned at the P/E hybrid site of mammalian ribosomes; tRNA in all other ribosomal positions could not be crosslinked to a ribosomal protein. Lys53 of RPL36AL is in close proximity to the ultimate A76 of P/E-tRNA. RPL36AL contains seven monomethylated residues (three lysyl, three arginyl, and one glutaminyl at Q51). Q51 is part of a conserved GGQ motif in L44e proteins (identical to the universally conserved motif of release factors implicated in peptidyl-tRNA hydrolysis).","method":"Periodate-oxidized tRNA crosslinking, mass spectrometry, site-specific mutagenesis/identification of modification sites","journal":"Chembiochem : a European journal of chemical biology","confidence":"High","confidence_rationale":"Tier 1 / Strong — zero-length crosslinking with positional specificity controls, MS-based identification of modified residues, replication of prior crosslinking result with extension","pmids":["22865768"],"is_preprint":false},{"year":2014,"finding":"RPL36AL is an E-site specific protein that forms a ternary complex with the CCA end of P-site tRNA and the translation termination factor eRF1 at the peptidyl transferase center of human 80S ribosomes. The isolated recombinant RPL36AL binds deacylated tRNA with nanomolar affinity, and this interaction extends beyond the CCA end to include the tRNA elbow region. Upon eRF1 binding to the A-site (stop codon UAA), an alternative ribosome/tRNA conformation is induced, causing the crosslink to shift from RPL36AL to RPL37 in a mutually exclusive fashion. RPL36AL was modeled based on the archaeal ortholog RPL44E from Haloarcula marismortui.","method":"Periodate-oxidized tRNA crosslinking, recombinant protein binding assay (tRNA affinity), programmed 80S ribosome complex reconstitution with eRF1, structural modeling","journal":"The open biochemistry journal","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro reconstitution with recombinant protein, zero-length crosslinking in programmed ribosomes, multiple orthogonal approaches (binding assay + crosslinking + structural modeling)","pmids":["25191528"],"is_preprint":false}],"current_model":"RPL36AL is a ubiquitously expressed large-subunit ribosomal protein (L44e/L36a family) that occupies the E-site of human 80S ribosomes and contacts the CCA end of P/E hybrid-site tRNA via Lys53; it contains a conserved GGQ motif and multiple methylated residues, binds deacylated tRNA with nanomolar affinity, and forms a ternary complex with eRF1 at the peptidyl transferase center during translation termination, with its crosslinking site switching to RPL37 upon eRF1-induced ribosome conformational change."},"narrative":{"mechanistic_narrative":"RPL36AL is a ubiquitously expressed large-subunit ribosomal protein of the L44e/L36a family that functions at the E-site of human 80S ribosomes during translation termination [PMID:19647033, PMID:25191528]. It originated as an intronless, autosomally retrotransposed copy of the X-linked progenitor RPL36A and shares 92–99% amino acid identity with it [PMID:12490704]. Within the ribosome, RPL36AL makes direct zero-length contact with the CCA end (C74, C75, A76) of deacylated tRNA positioned at the P/E hybrid site, with its Lys53 lying adjacent to the terminal A76, and it binds deacylated tRNA with nanomolar affinity through an interface extending from the CCA end to the tRNA elbow [PMID:19647033, PMID:22865768, PMID:25191528]. The protein carries seven monomethylated residues and a conserved GGQ motif (at Q51) characteristic of L44e proteins and shared with the peptidyl-tRNA hydrolysis motif of release factors [PMID:22865768]. During termination, RPL36AL forms a ternary complex with P-site tRNA and the release factor eRF1 at the peptidyl transferase center; eRF1 binding to a stop codon at the A-site induces an alternative ribosome/tRNA conformation that switches the tRNA crosslink from RPL36AL to RPL37 in a mutually exclusive manner [PMID:25191528].","teleology":[{"year":2002,"claim":"Established that RPL36AL is a bona fide functional ribosomal protein gene rather than a processed pseudogene, distinguishing it from tissue-restricted paralogs and setting it as the ubiquitous L36a-type product.","evidence":"Northern blot, PCR, and gene-structure sequence analysis defining its intronless retrotransposed origin and ubiquitous expression","pmids":["12490704"],"confidence":"Medium","gaps":["Functional role within the ribosome not addressed","Whether it is differentially incorporated relative to the X-linked progenitor RPL36A not tested"]},{"year":2009,"claim":"Resolved where RPL36AL acts on the ribosome by showing it directly contacts the CCA end of P-site tRNA, placing it at the tRNA-binding core of the large subunit.","evidence":"Periodate-oxidized tRNA zero-length crosslinking with intact-tRNA competition control and mass spectrometry identification in human 80S ribosomes","pmids":["19647033"],"confidence":"High","gaps":["Exact tRNA-binding site (P vs P/E) not yet pinpointed","Functional consequence of the contact unknown"]},{"year":2012,"claim":"Refined the contact to the P/E hybrid site and identified the specific residues and modifications involved, revealing a conserved GGQ motif that links RPL36AL to release-factor-type hydrolysis chemistry.","evidence":"Positional crosslinking with site specificity controls and MS-based mapping of Lys53 contact and seven monomethylated residues including Q51 of the GGQ motif","pmids":["22865768"],"confidence":"High","gaps":["Catalytic significance of the GGQ motif in RPL36AL not functionally demonstrated","Roles of the individual methylations not tested"]},{"year":2014,"claim":"Connected RPL36AL to translation termination by demonstrating a ternary complex with eRF1 and P-site tRNA and an eRF1-induced conformational switch that hands the tRNA contact to RPL37.","evidence":"Recombinant tRNA-affinity binding assay, programmed 80S ribosome reconstitution with eRF1, zero-length crosslinking, and structural modeling on the archaeal RPL44E ortholog","pmids":["25191528"],"confidence":"High","gaps":["No high-resolution structure of the human RPL36AL–tRNA–eRF1 complex","Mechanistic contribution of RPL36AL to peptidyl-tRNA hydrolysis not directly measured"]},{"year":null,"claim":"Whether RPL36AL's GGQ motif and methylations actively contribute to termination catalysis, and how the RPL36AL-to-RPL37 conformational switch is coupled to peptide release, remain unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No functional assay of RPL36AL GGQ-motif mutants in termination","No cryo-EM structure of the eRF1-bound termination intermediate","Cellular phenotype of RPL36AL loss uncharacterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[1,2,3]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[1,3]}],"localization":[{"term_id":"GO:0005840","term_label":"ribosome","supporting_discovery_ids":[1,2,3]}],"pathway":[],"complexes":["80S ribosome","60S large ribosomal subunit"],"partners":["ERF1","RPL37"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q969Q0","full_name":"Ribosomal protein eL42-like","aliases":["60S ribosomal protein L36a-like","Large ribosomal subunit protein eL42-like"],"length_aa":106,"mass_kda":12.5,"function":"","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/Q969Q0/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/RPL36AL","classification":"Common Essential","n_dependent_lines":1144,"n_total_lines":1208,"dependency_fraction":0.9470198675496688},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/RPL36AL","total_profiled":1310},"omim":[{"mim_id":"617893","title":"RIBOSOMAL PROTEIN L36; RPL36","url":"https://www.omim.org/entry/617893"},{"mim_id":"604902","title":"BRF1 SUBUNIT OF RNA POLYMERASE III TRANSCRIPTION INITIATION FACTOR; BRF1","url":"https://www.omim.org/entry/604902"},{"mim_id":"180469","title":"RIBOSOMAL PROTEIN L36A-LIKE; RPL36AL","url":"https://www.omim.org/entry/180469"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Endoplasmic reticulum","reliability":"Approved"},{"location":"Cytosol","reliability":"Approved"},{"location":"Plasma membrane","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/RPL36AL"},"hgnc":{"alias_symbol":[],"prev_symbol":["RPL36A","RPL36AP42"]},"alphafold":{"accession":"Q969Q0","domains":[{"cath_id":"3.10.450.80","chopping":"1-28_62-101","consensus_level":"medium","plddt":95.5347,"start":1,"end":101}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q969Q0","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q969Q0-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q969Q0-F1-predicted_aligned_error_v6.png","plddt_mean":95.0},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=RPL36AL","jax_strain_url":"https://www.jax.org/strain/search?query=RPL36AL"},"sequence":{"accession":"Q969Q0","fasta_url":"https://rest.uniprot.org/uniprotkb/Q969Q0.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q969Q0/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q969Q0"}},"corpus_meta":[{"pmid":"20116044","id":"PMC_20116044","title":"Ribosomal protein genes RPS10 and RPS26 are commonly mutated in Diamond-Blackfan anemia.","date":"2010","source":"American journal of human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/20116044","citation_count":192,"is_preprint":false},{"pmid":"36405716","id":"PMC_36405716","title":"Identification of diagnostic genes for both Alzheimer's disease and Metabolic syndrome by the machine learning algorithm.","date":"2022","source":"Frontiers in immunology","url":"https://pubmed.ncbi.nlm.nih.gov/36405716","citation_count":62,"is_preprint":false},{"pmid":"30478411","id":"PMC_30478411","title":"Systematic Analysis and Biomarker Study for Alzheimer's Disease.","date":"2018","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/30478411","citation_count":60,"is_preprint":false},{"pmid":"34276768","id":"PMC_34276768","title":"Discovery and Validation of Key Biomarkers Based on Immune Infiltrates in Alzheimer's Disease.","date":"2021","source":"Frontiers in genetics","url":"https://pubmed.ncbi.nlm.nih.gov/34276768","citation_count":56,"is_preprint":false},{"pmid":"12490704","id":"PMC_12490704","title":"Functional second genes generated by retrotransposition of the X-linked ribosomal protein genes.","date":"2002","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/12490704","citation_count":44,"is_preprint":false},{"pmid":"19647033","id":"PMC_19647033","title":"The human large subunit ribosomal protein L36A-like contacts the CCA end of P-site bound tRNA.","date":"2009","source":"Biochimie","url":"https://pubmed.ncbi.nlm.nih.gov/19647033","citation_count":25,"is_preprint":false},{"pmid":"22865768","id":"PMC_22865768","title":"Lys53 of ribosomal protein L36AL and the CCA end of a tRNA at the P/E hybrid site are in close proximity on the human ribosome.","date":"2012","source":"Chembiochem : a European journal of chemical biology","url":"https://pubmed.ncbi.nlm.nih.gov/22865768","citation_count":19,"is_preprint":false},{"pmid":"25191528","id":"PMC_25191528","title":"The CCA-end of P-tRNA Contacts Both the Human RPL36AL and the A-site Bound Translation Termination Factor eRF1 at the Peptidyl Transferase Center of the Human 80S Ribosome.","date":"2014","source":"The open biochemistry journal","url":"https://pubmed.ncbi.nlm.nih.gov/25191528","citation_count":14,"is_preprint":false},{"pmid":"36171445","id":"PMC_36171445","title":"Identification of stable housekeeping genes for induced pluripotent stem cells and -derived endothelial cells for drug testing.","date":"2022","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/36171445","citation_count":9,"is_preprint":false},{"pmid":"36407771","id":"PMC_36407771","title":"Association of Predicted Expression and Multimodel Association Analysis of Substance Abuse Traits.","date":"2022","source":"Complex psychiatry","url":"https://pubmed.ncbi.nlm.nih.gov/36407771","citation_count":4,"is_preprint":false},{"pmid":"38092793","id":"PMC_38092793","title":"Identification of hub genes and their expression profiling for predicting buffalo (Bubalus bubalis) semen quality and fertility.","date":"2023","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/38092793","citation_count":2,"is_preprint":false},{"pmid":"40842654","id":"PMC_40842654","title":"Bioinformatics and experimental validation identify biomarkers for diagnosing Alzheimer's disease.","date":"2025","source":"Frontiers in aging neuroscience","url":"https://pubmed.ncbi.nlm.nih.gov/40842654","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8652,"output_tokens":1326,"usd":0.022923,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7944,"output_tokens":1986,"usd":0.044685,"stage2_stop_reason":"end_turn"},"total_usd":0.067608,"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\": 2002,\n      \"finding\": \"RPL36AL is a functional autosomal retrotransposed copy of the X-linked ribosomal protein gene RPL36A, lacking introns in its coding region, and is ubiquitously expressed (unlike the testis-specific paralogs RPL10L and RPL39L). It encodes a protein with 92-99% amino acid identity to the X-linked progenitor.\",\n      \"method\": \"Northern blot, PCR, sequence analysis of gene structure\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Northern blot and PCR with sequence analysis in single study; ubiquitous expression and retrotransposition origin established by direct experiment\",\n      \"pmids\": [\"12490704\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"RPL36AL (ribosomal protein L36a-like) contacts the CCA end of P-site bound tRNA on human 80S ribosomes, as demonstrated by periodate-oxidized tRNA (tRNAox) zero-length affinity crosslinking followed by mass spectrometry identification. Intact tRNA competed with tRNAox to prevent crosslinking, confirming specificity. RPL36AL belongs to the L44e family of ribosomal proteins.\",\n      \"method\": \"Periodate-oxidized tRNA (zero-length affinity labeling/crosslinking), mass spectrometry, competition assay with intact tRNA\",\n      \"journal\": \"Biochimie\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — zero-length crosslinking with competition control and MS identification; replicated and extended in subsequent studies\",\n      \"pmids\": [\"19647033\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"RPL36AL crosslinks specifically to the CCA end (C74, C75, and A76) of tRNA positioned at the P/E hybrid site of mammalian ribosomes; tRNA in all other ribosomal positions could not be crosslinked to a ribosomal protein. Lys53 of RPL36AL is in close proximity to the ultimate A76 of P/E-tRNA. RPL36AL contains seven monomethylated residues (three lysyl, three arginyl, and one glutaminyl at Q51). Q51 is part of a conserved GGQ motif in L44e proteins (identical to the universally conserved motif of release factors implicated in peptidyl-tRNA hydrolysis).\",\n      \"method\": \"Periodate-oxidized tRNA crosslinking, mass spectrometry, site-specific mutagenesis/identification of modification sites\",\n      \"journal\": \"Chembiochem : a European journal of chemical biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — zero-length crosslinking with positional specificity controls, MS-based identification of modified residues, replication of prior crosslinking result with extension\",\n      \"pmids\": [\"22865768\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"RPL36AL is an E-site specific protein that forms a ternary complex with the CCA end of P-site tRNA and the translation termination factor eRF1 at the peptidyl transferase center of human 80S ribosomes. The isolated recombinant RPL36AL binds deacylated tRNA with nanomolar affinity, and this interaction extends beyond the CCA end to include the tRNA elbow region. Upon eRF1 binding to the A-site (stop codon UAA), an alternative ribosome/tRNA conformation is induced, causing the crosslink to shift from RPL36AL to RPL37 in a mutually exclusive fashion. RPL36AL was modeled based on the archaeal ortholog RPL44E from Haloarcula marismortui.\",\n      \"method\": \"Periodate-oxidized tRNA crosslinking, recombinant protein binding assay (tRNA affinity), programmed 80S ribosome complex reconstitution with eRF1, structural modeling\",\n      \"journal\": \"The open biochemistry journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro reconstitution with recombinant protein, zero-length crosslinking in programmed ribosomes, multiple orthogonal approaches (binding assay + crosslinking + structural modeling)\",\n      \"pmids\": [\"25191528\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"RPL36AL is a ubiquitously expressed large-subunit ribosomal protein (L44e/L36a family) that occupies the E-site of human 80S ribosomes and contacts the CCA end of P/E hybrid-site tRNA via Lys53; it contains a conserved GGQ motif and multiple methylated residues, binds deacylated tRNA with nanomolar affinity, and forms a ternary complex with eRF1 at the peptidyl transferase center during translation termination, with its crosslinking site switching to RPL37 upon eRF1-induced ribosome conformational change.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RPL36AL is a ubiquitously expressed large-subunit ribosomal protein of the L44e/L36a family that functions at the E-site of human 80S ribosomes during translation termination [#1, #3]. It originated as an intronless, autosomally retrotransposed copy of the X-linked progenitor RPL36A and shares 92–99% amino acid identity with it [#0]. Within the ribosome, RPL36AL makes direct zero-length contact with the CCA end (C74, C75, A76) of deacylated tRNA positioned at the P/E hybrid site, with its Lys53 lying adjacent to the terminal A76, and it binds deacylated tRNA with nanomolar affinity through an interface extending from the CCA end to the tRNA elbow [#1, #2, #3]. The protein carries seven monomethylated residues and a conserved GGQ motif (at Q51) characteristic of L44e proteins and shared with the peptidyl-tRNA hydrolysis motif of release factors [#2]. During termination, RPL36AL forms a ternary complex with P-site tRNA and the release factor eRF1 at the peptidyl transferase center; eRF1 binding to a stop codon at the A-site induces an alternative ribosome/tRNA conformation that switches the tRNA crosslink from RPL36AL to RPL37 in a mutually exclusive manner [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2002,\n      \"claim\": \"Established that RPL36AL is a bona fide functional ribosomal protein gene rather than a processed pseudogene, distinguishing it from tissue-restricted paralogs and setting it as the ubiquitous L36a-type product.\",\n      \"evidence\": \"Northern blot, PCR, and gene-structure sequence analysis defining its intronless retrotransposed origin and ubiquitous expression\",\n      \"pmids\": [\"12490704\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional role within the ribosome not addressed\",\n        \"Whether it is differentially incorporated relative to the X-linked progenitor RPL36A not tested\"\n      ]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Resolved where RPL36AL acts on the ribosome by showing it directly contacts the CCA end of P-site tRNA, placing it at the tRNA-binding core of the large subunit.\",\n      \"evidence\": \"Periodate-oxidized tRNA zero-length crosslinking with intact-tRNA competition control and mass spectrometry identification in human 80S ribosomes\",\n      \"pmids\": [\"19647033\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Exact tRNA-binding site (P vs P/E) not yet pinpointed\",\n        \"Functional consequence of the contact unknown\"\n      ]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Refined the contact to the P/E hybrid site and identified the specific residues and modifications involved, revealing a conserved GGQ motif that links RPL36AL to release-factor-type hydrolysis chemistry.\",\n      \"evidence\": \"Positional crosslinking with site specificity controls and MS-based mapping of Lys53 contact and seven monomethylated residues including Q51 of the GGQ motif\",\n      \"pmids\": [\"22865768\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Catalytic significance of the GGQ motif in RPL36AL not functionally demonstrated\",\n        \"Roles of the individual methylations not tested\"\n      ]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Connected RPL36AL to translation termination by demonstrating a ternary complex with eRF1 and P-site tRNA and an eRF1-induced conformational switch that hands the tRNA contact to RPL37.\",\n      \"evidence\": \"Recombinant tRNA-affinity binding assay, programmed 80S ribosome reconstitution with eRF1, zero-length crosslinking, and structural modeling on the archaeal RPL44E ortholog\",\n      \"pmids\": [\"25191528\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No high-resolution structure of the human RPL36AL–tRNA–eRF1 complex\",\n        \"Mechanistic contribution of RPL36AL to peptidyl-tRNA hydrolysis not directly measured\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether RPL36AL's GGQ motif and methylations actively contribute to termination catalysis, and how the RPL36AL-to-RPL37 conformational switch is coupled to peptide release, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No functional assay of RPL36AL GGQ-motif mutants in termination\",\n        \"No cryo-EM structure of the eRF1-bound termination intermediate\",\n        \"Cellular phenotype of RPL36AL loss uncharacterized\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [1, 2, 3]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005840\", \"supporting_discovery_ids\": [1, 2, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-72766\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [\n      \"80S ribosome\",\n      \"60S large ribosomal subunit\"\n    ],\n    \"partners\": [\n      \"eRF1\",\n      \"RPL37\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":5,"faith_total":5,"faith_pct":100.0}}