[ { "title": "C421A polymorphism in the human breast cancer resistance protein gene is associated with low expression of Q141K protein and low-level drug resistance.", "journal": "Molecular cancer therapeutics", "date": "2002", "authors": "Imai Y, Nakane M, Kage K, Tsukahara S, Ishikawa E, Tsuruo T, Miki Y, Sugimoto Y", "reference": { "type": "PubMed", "id": "12479221", "url": "https://pubmed.ncbi.nlm.nih.gov/12479221" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.12479221", "abstract": "", "glycosylation": [], "mutagenesis": [], 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"Effect of Walker A mutation (K86M) on oligomerization and surface targeting of the multidrug resistance transporter ABCG2.", "journal": "Journal of cell science", "date": "2005", "authors": "Henriksen U, Gether U, Litman T", "reference": { "type": "PubMed", "id": "15769853", "url": "https://pubmed.ncbi.nlm.nih.gov/15769853" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 86, "end_pos": 86, "sequence_org": "K", "sequence_mut": "M", "comment": "Decreased protein abundance. 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"uniprot_canonical_ac" ] }, { "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": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_sites", "count": 1 }, { "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 }, { "field": "exact_sites", "count": 1 }, { "field": "exact_n_linked_sites", "count": 1 }, { "field": "fuzzy_sites", "count": 0 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "icn3d_view.label", "icn3d_view.url", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl", "mining_tool", "filter_code", "uniprot_canonical_ac" ] } ] }, { "title": "Single nucleotide polymorphisms modify the transporter activity of ABCG2.", "journal": "Cancer chemotherapy and pharmacology", "date": "2005", "authors": "Morisaki K, Robey RW, Ozvegy-Laczka C, Honjo Y, Polgar O, Steadman K, Sarkadi B, Bates SE", "reference": { "type": "PubMed", "id": "15838659", "url": "https://pubmed.ncbi.nlm.nih.gov/15838659" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.15838659", "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", "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", 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"title": "Breast cancer resistance protein (BCRP)-mediated glyburide transport: effect of the C421A/Q141K BCRP single-nucleotide polymorphism.", "journal": "Drug metabolism and disposition: the biological fate of chemicals", "date": "2010", "authors": "Pollex EK, Anger G, Hutson J, Koren G, Piquette-Miller M", "reference": { "type": "PubMed", "id": "20159988", "url": "https://pubmed.ncbi.nlm.nih.gov/20159988" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.20159988", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], 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Biol. Chem.", "date": "2010", "authors": "Brechbuhl Heather M, Gould Neal, Kachadourian Remy, Riekhof Wayne R, Voelker Dennis R, Day Brian J", "reference": { "type": "PubMed", "id": "20332504", "url": "https://pubmed.ncbi.nlm.nih.gov/20332504" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.20332504", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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Hideharu, Watanabe Satoru, Fujita Masanori, Morimoto Yuji, Naito Mariko, Nishio Kazuko, Hishida Asahi, Wakai Kenji, Asai Yatami, Niwa Kazuki, Kamakura Keiko, Nonoyama Shigeaki, Sakurai Yutaka, Hosoya Tatsuo, Kanai Yoshikatsu, Suzuki Hiroshi, Hamajima Nobuyuki, Shinomiya Nariyoshi", "reference": { "type": "PubMed", "id": "20368174", "url": "https://pubmed.ncbi.nlm.nih.gov/20368174" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.20368174", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], 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Genet.", "date": "2012", "authors": "Saison Carole, Helias Virginie, Ballif Bryan A, Peyrard Thierry, Puy Herv\u00e9, Miyazaki Toru, Perrot S\u00e9bastien, Vayssier-Taussat Muriel, Waldner Mauro, Le Pennec Pierre-Yves, Cartron Jean-Pierre, Arnaud Lionel", "reference": { "type": "PubMed", "id": "22246505", "url": "https://pubmed.ncbi.nlm.nih.gov/22246505" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.22246505", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": 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"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": "ABCG2 null alleles define the Jr(a-) blood group phenotype.", "journal": "Nature genetics", "date": "2012", "authors": "Zelinski T, Coghlan G, Liu XQ, Reid ME", "reference": { "type": "PubMed", "id": "22246507", "url": "https://pubmed.ncbi.nlm.nih.gov/22246507" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": 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Pharmacol.", "date": "2013", "authors": "Gauthier Charlotte, Ozvegy-Laczka Csilla, Szakacs Gergely, Sarkadi Balazs, Di Pietro Attilio", "reference": { "type": "PubMed", "id": "24312054", "url": "https://pubmed.ncbi.nlm.nih.gov/24312054" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.24312054", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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"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": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_sites", "count": 1 }, { "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 }, { "field": "exact_sites", "count": 1 }, { "field": "exact_n_linked_sites", "count": 1 }, { "field": "fuzzy_sites", "count": 0 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "icn3d_view.label", "icn3d_view.url", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl", "mining_tool", "filter_code", "uniprot_canonical_ac" ] } ] }, { "title": "Localization of the placental BCRP/ABCG2 transporter to lipid rafts: Role for cholesterol in mediating efflux activity.", "journal": "Placenta", "date": "2017", "authors": "Szilagyi John T, Vetrano Anna M, Laskin Jeffrey D, Aleksunes Lauren M", "reference": { "type": "PubMed", "id": "28623970", "url": "https://pubmed.ncbi.nlm.nih.gov/28623970" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], 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"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": "Associations between ABCG2 gene polymorphisms and gefitinib toxicity in non-small cell lung cancer: a meta-analysis.", "journal": "OncoTargets and therapy", "date": "2018", "authors": "Tang L, Zhang C, He H, Pan Z, Fan D, He Y, You H, Li Y", "reference": { "type": "PubMed", "id": "29440914", "url": "https://pubmed.ncbi.nlm.nih.gov/29440914" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.29440914", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": 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Struct. Mol. Biol.", "date": "2018", "authors": "Jackson SM, Manolaridis I, Kowal J, Zechner M, Taylor NMI, Bause M, Bauer S, Bartholomaeus R, Bernhardt G, Koenig B, Buschauer A, Stahlberg H, Altmann KH, Locher KP", "reference": { "type": "PubMed", "id": "29610494", "url": "https://pubmed.ncbi.nlm.nih.gov/29610494" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.29610494", "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", "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": "Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states.", "journal": "Nature", "date": "2018", "authors": "Manolaridis I, Jackson SM, Taylor NMI, Kowal J, Stahlberg H, Locher KP", "reference": { "type": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UNQ0-1", "protein_name": "Broad substrate specificity ATP-binding cassette transporter ABCG2", "gene_name": "ABCG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 211, "end_pos": 211, "sequence_org": "E", "sequence_mut": "Q", "comment": "Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Loss of ATP-dependent itaconate export resulting in itaconate cytosolic accumulation.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "28554189", "url": "https://pubmed.ncbi.nlm.nih.gov/28554189" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" }, { "database": "PubMed", "id": "38181789", "url": "https://pubmed.ncbi.nlm.nih.gov/38181789" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 435, "end_pos": 435, "sequence_org": "T", "sequence_mut": "A", "comment": "No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased substrate-induced ATP hydrolysis. Increased substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 435, "end_pos": 435, "sequence_org": "T", "sequence_mut": "F", "comment": "No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 436, "end_pos": 436, "sequence_org": "N", "sequence_mut": "A", "comment": "No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 439, "end_pos": 439, "sequence_org": "F", "sequence_mut": "A", "comment": "No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 546, "end_pos": 546, "sequence_org": "V", "sequence_mut": "A", "comment": "No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 546, "end_pos": 546, "sequence_org": "V", "sequence_mut": "F", "comment": "No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Decreased substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 549, "end_pos": 549, "sequence_org": "M", "sequence_mut": "A", "comment": "No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNQ0", "url": "https://www.uniprot.org/uniprotkb/Q9UNQ0" }, { "database": "PubMed", "id": "30405239", "url": "https://pubmed.ncbi.nlm.nih.gov/30405239" } ], "uniprot_canonical_ac": "Q9UNQ0-1" }, { "start_pos": 554, "end_pos": 554, "sequence_org": "L", "sequence_mut": "A", "comment": "No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. 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"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": "Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex.", "journal": "J. Mol. Biol.", "date": "2000", "authors": "Tissot A C, Ciatto C, Mittl P R, Gr\u00fctter M G, Pl\u00fcckthun A", "reference": { "type": "PubMed", "id": "10993729", "url": "https://pubmed.ncbi.nlm.nih.gov/10993729" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P14427-1", "protein_name": "H-2 class I histocompatibility antigen, D-P alpha chain", "gene_name": "H2-D1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P14427", "url": "https://www.uniprot.org/uniprotkb/P14427" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.10993729", "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", "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": "MHC class I ubiquitination by a viral PHD/LAP finger protein.", "journal": "Immunity", "date": "2001", "authors": "Boname JM, Stevenson PG", "reference": { "type": "PubMed", "id": "11672544", "url": "https://pubmed.ncbi.nlm.nih.gov/11672544" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P14427-1", "protein_name": "H-2 class I histocompatibility antigen, D-P alpha chain", "gene_name": "H2-D1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P14427", "url": "https://www.uniprot.org/uniprotkb/P14427" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.11672544", "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", "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": "Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3.", "journal": "The Journal of cell biology", "date": "2007", "authors": "Wang X, Herr RA, Chua WJ, Lybarger L, Wiertz EJ, Hansen TH", "reference": { "type": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P14427-1", "protein_name": "H-2 class I histocompatibility antigen, D-P alpha chain", "gene_name": "H2-D1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P14427", "url": "https://www.uniprot.org/uniprotkb/P14427" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 155, "end_pos": 155, "sequence_org": "T", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-170, R-197, R-210, R-220, R-267 and R-277.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 170, "end_pos": 170, "sequence_org": "Q", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-197, R-210, R-220, R-267 and R-277.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 197, "end_pos": 197, "sequence_org": "N", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-210, R-220, R-267 and R-277.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 210, "end_pos": 210, "sequence_org": "V", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-220, R-267 and R-277.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 220, "end_pos": 220, "sequence_org": "V", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-267 and R-277.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 267, "end_pos": 267, "sequence_org": "A", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-220 and R-277.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 277, "end_pos": 277, "sequence_org": "N", "sequence_mut": "R", "comment": "In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-220 and R-267.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": 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In Ld tail 1S, restores ubiquitination; when associated I-337; R-340; 350-A--A-352; A-356 and 360-R-R-361.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "19951915", "url": "https://pubmed.ncbi.nlm.nih.gov/19951915" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" }, { "database": "PubMed", "id": "19531064", "url": "https://pubmed.ncbi.nlm.nih.gov/19531064" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 337, "end_pos": 337, "sequence_org": "K", "sequence_mut": "I", "comment": "In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; R-340; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated R-332; R-340; 350-A--A-352; A-356 and 360-R-R-361.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "19951915", "url": "https://pubmed.ncbi.nlm.nih.gov/19951915" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" }, { "database": "PubMed", "id": "19531064", "url": "https://pubmed.ncbi.nlm.nih.gov/19531064" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 340, "end_pos": 340, "sequence_org": "D", "sequence_mut": "R", "comment": "In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; 350-A--A-352; A-356 and 360-R-R-361.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "19951915", "url": "https://pubmed.ncbi.nlm.nih.gov/19951915" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" }, { "database": "PubMed", "id": "19531064", "url": "https://pubmed.ncbi.nlm.nih.gov/19531064" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 350, "end_pos": 356, "sequence_org": "SEMSLRD", "sequence_mut": "AQGAEMA", "comment": "In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337 and 360-R-R-361.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 360, "end_pos": 361, "sequence_org": "MV", "sequence_mut": "RR", "comment": "In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; R-340 and 350-A--A-356. 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when associated with I-337; R-340; 350-A--A-356 and 360-R-R-361. 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In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; 350-A--A-352; A-356 and 360-R-R-361.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "19951915", "url": "https://pubmed.ncbi.nlm.nih.gov/19951915" }, { "database": "PubMed", "id": "17502423", "url": "https://pubmed.ncbi.nlm.nih.gov/17502423" }, { "database": "PubMed", "id": "19531064", "url": "https://pubmed.ncbi.nlm.nih.gov/19531064" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 350, "end_pos": 352, "sequence_org": "SEM", "sequence_mut": "AQG", "comment": "In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "19951915", "url": "https://pubmed.ncbi.nlm.nih.gov/19951915" }, { "database": "PubMed", "id": "19531064", "url": "https://pubmed.ncbi.nlm.nih.gov/19531064" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 356, "end_pos": 356, "sequence_org": "D", "sequence_mut": "A", "comment": "In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340 and A-356.", "evidence": [ { "database": "UniProtKB", "id": "P01899", "url": "https://www.uniprot.org/uniprotkb/P01899" }, { "database": "PubMed", "id": "19951915", "url": "https://pubmed.ncbi.nlm.nih.gov/19951915" }, { "database": "PubMed", "id": "19531064", "url": "https://pubmed.ncbi.nlm.nih.gov/19531064" } ], "uniprot_canonical_ac": "P14427-1" }, { "start_pos": 360, "end_pos": 361, "sequence_org": "MV", "sequence_mut": "RR", "comment": "In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; R-340 and 350-A--A-356. 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II. Additional amino acid sequence information, localization of a third site of glycosylation and evidence for K and D region specific sequences.", "journal": "Immunogenetics", "date": "1982", "authors": "Maloy WL, Coligan JE", "reference": { "type": "PubMed", "id": "7118212", "url": "https://pubmed.ncbi.nlm.nih.gov/7118212" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P14427-1", "protein_name": "H-2 class I histocompatibility antigen, D-P alpha chain", "gene_name": "H2-D1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P14427", "url": "https://www.uniprot.org/uniprotkb/P14427" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.7118212", "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", "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": "Primary structure of murine major histocompatibility complex alloantigens. Amino acid sequence of the NH2-terminal ninety-eight residues of the H-2Db glycoprotein.", "journal": "J. Biol. Chem.", "date": "1981", "authors": "Maloy W L, Nathenson S G, Coligan J E", "reference": { "type": "PubMed", "id": "7225204", "url": "https://pubmed.ncbi.nlm.nih.gov/7225204" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P14427-1", "protein_name": "H-2 class I histocompatibility antigen, D-P alpha chain", "gene_name": "H2-D1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P14427", "url": "https://www.uniprot.org/uniprotkb/P14427" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.7225204", "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", "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": "Amino acid sequence of cyanogen bromide fragment CN-C (residues 24-98) of the mouse histocompatibility antigen H-2Dd. A comparison of the amino-terminal 100 residues of H-2Dd, Dd, Kd, and Kb reveals discrete areas of diversity.", "journal": "Biochemistry", "date": "1981", "authors": "Nairn R, Nathenson S G, Coligan J E", "reference": { "type": "PubMed", "id": "7295646", "url": "https://pubmed.ncbi.nlm.nih.gov/7295646" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P14427-1", "protein_name": "H-2 class I histocompatibility antigen, D-P alpha chain", "gene_name": "H2-D1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P14427", "url": "https://www.uniprot.org/uniprotkb/P14427" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.7295646", "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", "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", 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Biol.", "date": "1989", "authors": "Ghogawala Z, Choi E, Daly K R, Blanco L R, Griffith I J, Glimcher L H", "reference": { "type": "PubMed", "id": "2555693", "url": "https://pubmed.ncbi.nlm.nih.gov/2555693" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P01921-1", "protein_name": "H-2 class II histocompatibility antigen, A-D beta chain", "gene_name": "H2-Ab1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P01921", "url": "https://www.uniprot.org/uniprotkb/P01921" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.2555693", "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", "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": "Extensive polymorphism surrounding the murine Ia A-beta chain gene.", "journal": "J. 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"journal": "Histochemistry and cell biology", "date": "2016", "authors": "Ikpa PT, Sleddens HF, Steinbrecher KA, Peppelenbosch MP, de Jonge HR, Smits R, Bijvelds MJ", "reference": { "type": "PubMed", "id": "27246004", "url": "https://pubmed.ncbi.nlm.nih.gov/27246004" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O09051-1", "protein_name": "Guanylate cyclase activator 2B", "gene_name": "Guca2b", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P33680-1", "protein_name": "Guanylin", "gene_name": "Guca2a", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "O09051", "url": "https://www.uniprot.org/uniprotkb/O09051" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.27246004", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { 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Med.", "date": "1990", "authors": "Sugita T, Totsuka T, Saito M, Yamasaki K, Taga T, Hirano T, Kishimoto T", "reference": { "type": "PubMed", "id": "2112585", "url": "https://pubmed.ncbi.nlm.nih.gov/2112585" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P22272-1", "protein_name": "Interleukin-6 receptor subunit alpha", "gene_name": "Il6ra", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P22272", "url": "https://www.uniprot.org/uniprotkb/P22272" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.2112585", "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", "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": "Molecular cloning and expression analyses of mouse betaklotho, which encodes a novel Klotho family protein.", "journal": "Mech. Dev.", "date": "2000", "authors": "Ito S, Kinoshita S, Shiraishi N, Nakagawa S, Sekine S, Fujimori T, Nabeshima YI", "reference": { "type": "PubMed", "id": "11044614", "url": "https://pubmed.ncbi.nlm.nih.gov/11044614" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q99N32-1", "protein_name": "Beta-klotho", "gene_name": "Klb", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q99N32", "url": "https://www.uniprot.org/uniprotkb/Q99N32" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.11044614", "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", "gene_name", "tax_name" ] }, { "table_id": 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