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"uniprot_canonical_ac": "Q53GQ0-1", "protein_name": "Very-long-chain 3-oxoacyl-CoA reductase", "gene_name": "HSD17B12", "tax_name": "Human" }, { "uniprot_canonical_ac": "P18405-1", "protein_name": "3-oxo-5-alpha-steroid 4-dehydrogenase 1", "gene_name": "SRD5A1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P01189-1", "protein_name": "Pro-opiomelanocortin", "gene_name": "POMC", "tax_name": "Human" }, { "uniprot_canonical_ac": "P05093-1", "protein_name": "Steroid 17-alpha-hydroxylase/17,20 lyase", "gene_name": "CYP17A1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P01229-1", "protein_name": "Lutropin subunit beta", "gene_name": "LHB", "tax_name": "Human" }, { "uniprot_canonical_ac": "P14060-1", "protein_name": "3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1", "gene_name": "HSD3B1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P26439-1", "protein_name": "3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2", "gene_name": "HSD3B2", "tax_name": 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mtHsp70-escort protein 1: an essential mortalin co-chaperone.", "journal": "International journal of biological macromolecules", "date": "2013", "authors": "Dores-Silva PR, Minari K, Ramos CH, Barbosa LR, Borges JC", "reference": { "type": "PubMed", "id": "23462535", "url": "https://pubmed.ncbi.nlm.nih.gov/23462535" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q5SXM8-1", "protein_name": "DNL-type zinc finger protein", "gene_name": "DNLZ", "tax_name": "Human" }, { "uniprot_canonical_ac": "P38646-1", "protein_name": "Stress-70 protein, mitochondrial", "gene_name": "HSPA9", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q5SXM8", "url": "https://www.uniprot.org/uniprotkb/Q5SXM8" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.23462535", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], 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"count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Human dehydrogenase/reductase (SDR family) member 11 is a novel type of 17beta-hydroxysteroid dehydrogenase.", "journal": "Biochemical and biophysical research communications", "date": "2016", "authors": "Endo S, Miyagi N, Matsunaga T, Hara A, Ikari A", "reference": { "type": "PubMed", "id": "26920053", "url": "https://pubmed.ncbi.nlm.nih.gov/26920053" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q6UWP2-1", "protein_name": "Dehydrogenase/reductase SDR family member 11", "gene_name": "DHRS11", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q6UWP2", "url": "https://www.uniprot.org/uniprotkb/Q6UWP2" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.26920053", 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"tax_name": "Human" }, { "uniprot_canonical_ac": "Q9H2P9-1", "protein_name": "Diphthine methyl ester synthase", "gene_name": "DPH5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q3E840-1", "protein_name": "Diphthamide biosynthesis protein 3", "gene_name": "KTI11", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P32461-1", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 2", "gene_name": "DPH2", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P40487-1", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 1", "gene_name": "DPH1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "Q9BZG8-4", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 1", "gene_name": "DPH1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96FX2-1", "protein_name": "Diphthamide biosynthesis protein 3", "gene_name": "DPH3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9BQC3-1", "protein_name": 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"protein_name": "Diphthine methyl ester synthase", "gene_name": "Dph5", "tax_name": "Mouse" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q7L8W6", "url": "https://www.uniprot.org/uniprotkb/Q7L8W6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.15485916", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 15 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", 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"o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3.", "journal": "Molecular microbiology", "date": "2008", "authors": "Bar C, Zabel R, Liu S, Stark MJ, Schaffrath R", "reference": { "type": "PubMed", "id": "18627462", "url": "https://pubmed.ncbi.nlm.nih.gov/18627462" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q7L8W6-1", "protein_name": "Diphthine--ammonia ligase", "gene_name": "DPH6", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9H2P9-1", "protein_name": "Diphthine methyl ester synthase", "gene_name": "DPH5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q3E840-1", "protein_name": "Diphthamide biosynthesis protein 3", "gene_name": "KTI11", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P32461-1", "protein_name": 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Results in a functional protein that is resistant to diphtheria toxin and sordarin.", "evidence": [ { "database": "UniProtKB", "id": "P32324", "url": "https://www.uniprot.org/uniprotkb/P32324" }, { "database": "PubMed", "id": "18627462", "url": "https://pubmed.ncbi.nlm.nih.gov/18627462" }, { "database": "PubMed", "id": "8473309", "url": "https://pubmed.ncbi.nlm.nih.gov/8473309" } ], "uniprot_canonical_ac": "P32324-1" }, { "start_pos": 699, "end_pos": 699, "sequence_org": "H", "sequence_mut": "E", "comment": "Prevents post-translational modification of this residue to diphthamide. 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Results in a functional protein that is resistant to diphtheria toxin and sordarin.", "evidence": [ { "database": "UniProtKB", "id": "P32324", "url": "https://www.uniprot.org/uniprotkb/P32324" }, { "database": "PubMed", "id": "18627462", "url": "https://pubmed.ncbi.nlm.nih.gov/18627462" }, { "database": "PubMed", "id": "8473309", "url": "https://pubmed.ncbi.nlm.nih.gov/8473309" } ], "uniprot_canonical_ac": "P32324-1" } ], "record_id": "pubmed.18627462", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 18 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": 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"count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.", "journal": "Nature", "date": "2010", "authors": "Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H", "reference": { "type": "PubMed", "id": "20559380", "url": "https://pubmed.ncbi.nlm.nih.gov/20559380" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q7L8W6-1", "protein_name": "Diphthine--ammonia ligase", "gene_name": "DPH6", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9H2P9-1", "protein_name": "Diphthine methyl ester synthase", "gene_name": "DPH5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9BZG8-4", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 1", 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"total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Chemogenomic approach identified yeast YLR143W as diphthamide synthetase.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2012", "authors": "Su X, Lin 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], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network.", "journal": "PLoS genetics", "date": "2013", "authors": "Uthman S, Bar C, Scheidt V, Liu S, ten Have S, Giorgini F, Stark MJ, Schaffrath R", "reference": { "type": "PubMed", "id": "23468660", "url": "https://pubmed.ncbi.nlm.nih.gov/23468660" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q7L8W6-1", "protein_name": "Diphthine--ammonia 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"count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "A modified form of diphthamide causes immunotoxin resistance in a lymphoma cell line with a deletion of the WDR85 gene.", "journal": "The Journal of biological chemistry", "date": "2013", "authors": "Wei H, Bera TK, Wayne AS, Xiang L, Colantonio S, Chertov O, Pastan I", "reference": { "type": "PubMed", "id": "23486472", "url": "https://pubmed.ncbi.nlm.nih.gov/23486472" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q7L8W6-1", "protein_name": "Diphthine--ammonia ligase", "gene_name": "DPH6", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9H2P9-1", "protein_name": "Diphthine methyl ester synthase", "gene_name": "DPH5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9BZG8-4", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 1", "gene_name": "DPH1", "tax_name": "Human" }, { 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"The post-translational trimethylation of diphthamide studied in vitro.", "journal": "The Journal of biological chemistry", "date": "1988", "authors": "Moehring JM, Moehring TJ", "reference": { "type": "PubMed", "id": "3346227", "url": "https://pubmed.ncbi.nlm.nih.gov/3346227" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q7L8W6-1", "protein_name": "Diphthine--ammonia ligase", "gene_name": "DPH6", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9H2P9-1", "protein_name": "Diphthine methyl ester synthase", "gene_name": "DPH5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9BZG8-4", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 1", "gene_name": "DPH1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96FX2-1", "protein_name": "Diphthamide biosynthesis protein 3", "gene_name": "DPH3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9BQC3-1", "protein_name": "2-(3-amino-3-carboxypropyl)histidine synthase subunit 2", 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"table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Genes that Affect Brain Structure and Function Identified by Rare Variant Analyses of Mendelian Neurologic Disease.", "journal": "Neuron", 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Complementation of the yeast CEM1 knock-out strain.", "journal": "The Journal of biological chemistry", "date": "2005", "authors": "Zhang L, Joshi AK, Hofmann J, Schweizer E, Smith S", "reference": { "type": "PubMed", "id": "15668256", "url": "https://pubmed.ncbi.nlm.nih.gov/15668256" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92506-1", "protein_name": "(3R)-3-hydroxyacyl-CoA dehydrogenase", "gene_name": "HSD17B8", "tax_name": "Human" }, { "uniprot_canonical_ac": "P50897-1", "protein_name": "Palmitoyl-protein thioesterase 1", "gene_name": "PPT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NV23-1", "protein_name": "S-acyl fatty acid synthase thioesterase, medium chain", "gene_name": "OLAH", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q86SK9-1", "protein_name": "Stearoyl-CoA desaturase 5", "gene_name": "SCD5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8N4T8-1", "protein_name": "3-oxoacyl-[acyl-carrier-protein] reductase", 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Endocrinol.", "date": "2009", "authors": "Rotinen Mirja, Celay Jon, Alonso Marta M, Arrazola Aranzazu, Encio Ignacio, Villar Joaquin", "reference": { "type": "PubMed", "id": "18852215", "url": "https://pubmed.ncbi.nlm.nih.gov/18852215" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92506-1", "protein_name": "(3R)-3-hydroxyacyl-CoA dehydrogenase", "gene_name": "HSD17B8", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.18852215", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", 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"count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth.", "journal": "Molecular cell", "date": "2013", "authors": "Lin R, Tao R, Gao X, Li T, Zhou X, Guan KL, Xiong Y, Lei QY", "reference": { "type": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92506-1", "protein_name": "(3R)-3-hydroxyacyl-CoA dehydrogenase", "gene_name": "HSD17B8", "tax_name": "Human" }, { "uniprot_canonical_ac": "P50897-1", "protein_name": "Palmitoyl-protein thioesterase 1", "gene_name": "PPT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NV23-1", "protein_name": "S-acyl fatty acid synthase thioesterase, medium chain", "gene_name": "OLAH", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q86SK9-1", "protein_name": "Stearoyl-CoA desaturase 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"sequence_mut": "Q", "comment": "Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25)complex; when associated with R-546 and R-554.", "evidence": [ { "database": "UniProtKB", "id": "P53396", "url": "https://www.uniprot.org/uniprotkb/P53396" }, { "database": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, { "database": "PubMed", "id": "27664236", "url": "https://pubmed.ncbi.nlm.nih.gov/27664236" } ], "uniprot_canonical_ac": "P53396-1" }, { "start_pos": 540, "end_pos": 540, "sequence_org": "K", "sequence_mut": "R", "comment": "Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25)complex; when associated with R-546 and R-554.", "evidence": [ { "database": "UniProtKB", "id": "P53396", "url": "https://www.uniprot.org/uniprotkb/P53396" }, { "database": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, { "database": "PubMed", "id": "27664236", "url": "https://pubmed.ncbi.nlm.nih.gov/27664236" } ], "uniprot_canonical_ac": "P53396-1" }, { "start_pos": 546, "end_pos": 546, "sequence_org": "K", "sequence_mut": "Q", "comment": "Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-554.", "evidence": [ { "database": "UniProtKB", "id": "P53396", "url": "https://www.uniprot.org/uniprotkb/P53396" }, { "database": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, { "database": "PubMed", "id": "27664236", "url": "https://pubmed.ncbi.nlm.nih.gov/27664236" } ], "uniprot_canonical_ac": "P53396-1" }, { "start_pos": 546, "end_pos": 546, "sequence_org": "K", "sequence_mut": "R", "comment": "Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-554.", "evidence": [ { "database": "UniProtKB", "id": "P53396", "url": "https://www.uniprot.org/uniprotkb/P53396" }, { "database": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, { "database": "PubMed", "id": "27664236", "url": "https://pubmed.ncbi.nlm.nih.gov/27664236" } ], "uniprot_canonical_ac": "P53396-1" }, { "start_pos": 554, "end_pos": 554, "sequence_org": "K", "sequence_mut": "Q", "comment": "Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-546.", "evidence": [ { "database": "UniProtKB", "id": "P53396", "url": "https://www.uniprot.org/uniprotkb/P53396" }, { "database": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, { "database": "PubMed", "id": "27664236", "url": "https://pubmed.ncbi.nlm.nih.gov/27664236" } ], "uniprot_canonical_ac": "P53396-1" }, { "start_pos": 554, "end_pos": 554, "sequence_org": "K", "sequence_mut": "R", "comment": "Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-546.", "evidence": [ { "database": "UniProtKB", "id": "P53396", "url": "https://www.uniprot.org/uniprotkb/P53396" }, { "database": "PubMed", "id": "23932781", "url": "https://pubmed.ncbi.nlm.nih.gov/23932781" }, { "database": "PubMed", "id": "27664236", "url": "https://pubmed.ncbi.nlm.nih.gov/27664236" } ], "uniprot_canonical_ac": "P53396-1" } ], "record_id": "pubmed.23932781", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 16 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": 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"count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": 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"Q86SK9-1", "protein_name": "Stearoyl-CoA desaturase 5", "gene_name": "SCD5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8N4T8-1", "protein_name": "3-oxoacyl-[acyl-carrier-protein] reductase", "gene_name": "CBR4", "tax_name": "Human" }, { "uniprot_canonical_ac": "O00767-1", "protein_name": "Stearoyl-CoA desaturase", "gene_name": "SCD", "tax_name": "Human" }, { "uniprot_canonical_ac": "P49327-1", "protein_name": "Fatty acid synthase", "gene_name": "FASN", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9Y6X9-1", "protein_name": "ATPase MORC2", "gene_name": "MORC2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UMR5-1", "protein_name": "Lysosomal thioesterase PPT2", "gene_name": "PPT2-EGFL8; PPT2", "tax_name": "Human" }, { "uniprot_canonical_ac": "O14975-1", "protein_name": "Long-chain fatty acid transport protein 2", "gene_name": "SLC27A2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P86397-1", "protein_name": "Hydroxyacyl-thioester dehydratase type 2, 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"sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase.", "journal": "Nature communications", "date": "2014", "authors": "Venkatesan R, Sah-Teli SK, Awoniyi LO, Jiang G, Prus P, Kastaniotis AJ, Hiltunen JK, Wierenga RK, Chen Z", "reference": { "type": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92506-1", "protein_name": "(3R)-3-hydroxyacyl-CoA dehydrogenase", "gene_name": "HSD17B8", "tax_name": "Human" }, { "uniprot_canonical_ac": 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"PPT2-EGFL8; PPT2", "tax_name": "Human" }, { "uniprot_canonical_ac": "O14975-1", "protein_name": "Long-chain fatty acid transport protein 2", "gene_name": "SLC27A2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P86397-1", "protein_name": "Hydroxyacyl-thioester dehydratase type 2, mitochondrial", "gene_name": "HTD2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q13085-1", "protein_name": "Acetyl-CoA carboxylase 1", "gene_name": "ACACA", "tax_name": "Human" }, { "uniprot_canonical_ac": "P53396-1", "protein_name": "ATP-citrate synthase", "gene_name": "ACLY", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 148, "end_pos": 148, "sequence_org": "R", "sequence_mut": "E", "comment": "No effect on the ability to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q92506-1" }, { "start_pos": 169, "end_pos": 169, "sequence_org": "Y", "sequence_mut": "A", "comment": "Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q92506-1" }, { "start_pos": 173, "end_pos": 173, "sequence_org": "K", "sequence_mut": "A", "comment": "Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q92506-1" }, { "start_pos": 189, "end_pos": 189, "sequence_org": "R", "sequence_mut": "E", "comment": "No effect on the ability to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q92506-1" }, { "start_pos": 42, "end_pos": 42, "sequence_org": "D", "sequence_mut": "A", "comment": "Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q92506-1" }, { "start_pos": 12, "end_pos": 12, "sequence_org": "R", "sequence_mut": "A", "comment": "Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 135, "end_pos": 135, "sequence_org": "S", "sequence_mut": "A", "comment": "Unable to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 148, "end_pos": 148, "sequence_org": "Y", "sequence_mut": "A", "comment": "Unable to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 152, "end_pos": 152, "sequence_org": "K", "sequence_mut": "A", "comment": "Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 168, "end_pos": 168, "sequence_org": "R", "sequence_mut": "E", "comment": "Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 169, "end_pos": 169, "sequence_org": "K", "sequence_mut": "E", "comment": "Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 34, "end_pos": 34, "sequence_org": "R", "sequence_mut": "A", "comment": "Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" }, { "start_pos": 9, "end_pos": 9, "sequence_org": "G", "sequence_mut": "S", "comment": "Unable to restore growth of an OAR1-deficient yeast mutant.", "evidence": [ { "database": "UniProtKB", "id": "Q8N4T8", "url": "https://www.uniprot.org/uniprotkb/Q8N4T8" }, { "database": "PubMed", "id": "25203508", "url": "https://pubmed.ncbi.nlm.nih.gov/25203508" } ], "uniprot_canonical_ac": "Q8N4T8-1" } ], "record_id": "pubmed.25203508", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 13 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Liver-specific ATP-citrate lyase inhibition by bempedoic acid decreases LDL-C and attenuates atherosclerosis.", "journal": "Nature communications", "date": "2016", "authors": "Pinkosky SL, Newton RS, Day EA, Ford RJ, Lhotak S, Austin RC, Birch CM, Smith BK, Filippov S, Groot PHE, Steinberg GR, Lalwani ND", "reference": { "type": "PubMed", "id": "27892461", "url": "https://pubmed.ncbi.nlm.nih.gov/27892461" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92506-1", "protein_name": "(3R)-3-hydroxyacyl-CoA dehydrogenase", "gene_name": "HSD17B8", "tax_name": "Human" }, { "uniprot_canonical_ac": "P50897-1", "protein_name": "Palmitoyl-protein thioesterase 1", "gene_name": "PPT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NV23-1", "protein_name": "S-acyl fatty acid synthase thioesterase, medium chain", "gene_name": "OLAH", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q86SK9-1", "protein_name": "Stearoyl-CoA desaturase 5", "gene_name": "SCD5", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8N4T8-1", "protein_name": "3-oxoacyl-[acyl-carrier-protein] reductase", "gene_name": "CBR4", "tax_name": "Human" }, { "uniprot_canonical_ac": "O00767-1", "protein_name": "Stearoyl-CoA desaturase", "gene_name": "SCD", "tax_name": "Human" }, { "uniprot_canonical_ac": "P49327-1", "protein_name": "Fatty acid synthase", "gene_name": "FASN", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9Y6X9-1", "protein_name": "ATPase MORC2", "gene_name": "MORC2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UMR5-1", "protein_name": "Lysosomal thioesterase PPT2", "gene_name": "PPT2-EGFL8; PPT2", "tax_name": "Human" }, { "uniprot_canonical_ac": "O14975-1", "protein_name": "Long-chain fatty acid transport protein 2", "gene_name": "SLC27A2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P86397-1", "protein_name": "Hydroxyacyl-thioester dehydratase type 2, mitochondrial", "gene_name": "HTD2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q13085-1", "protein_name": "Acetyl-CoA carboxylase 1", "gene_name": "ACACA", "tax_name": "Human" }, { "uniprot_canonical_ac": "P53396-1", "protein_name": "ATP-citrate synthase", "gene_name": "ACLY", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q92506", "url": "https://www.uniprot.org/uniprotkb/Q92506" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.27892461", 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"n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] } ]