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Physiol. 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Polyubiquitination of NKCC2.", "journal": "Cells", "date": "2024-02-24", "authors": "Frachon Nadia, Demaretz Sylvie, Seaayfan Elie, Chelbi Lydia, Bakhos-Douaihy Dalal, Laghmani Kamel", "reference": { "type": "PubMed", "id": "38474353", "url": "https://pubmed.ncbi.nlm.nih.gov/38474353" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q13621-1", "protein_name": "Solute carrier family 12 member 1", "gene_name": "SLC12A1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9Y679-2", "protein_name": "Lipid droplet-regulating VLDL assembly factor AUP1", "gene_name": "AUP1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q13621", "url": "https://www.uniprot.org/uniprotkb/Q13621" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.38474353", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], 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"count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.", "journal": "Journal of virology", "date": "2006", "authors": "Oostra M, de Haan CA, de Groot RJ, Rottier PJ", "reference": { "type": "PubMed", "id": "16474139", "url": "https://pubmed.ncbi.nlm.nih.gov/16474139" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q11201-1", "protein_name": "CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1", "gene_name": "ST3GAL1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q11206-1", "protein_name": "CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4", "gene_name": "ST3GAL4", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8NDV1-1", "protein_name": "Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3", "gene_name": "ST6GALNAC3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q16842-1", "protein_name": "CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2", "gene_name": "ST3GAL2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UJ37-1", "protein_name": "Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2", "gene_name": "ST6GALNAC2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P15907-1", "protein_name": "Beta-galactoside alpha-2,6-sialyltransferase 1", "gene_name": "ST6GAL1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q11203-1", "protein_name": "CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase", "gene_name": "ST3GAL3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9H4F1-1", "protein_name": "Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase", "gene_name": "ST6GALNAC4", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q10472-1", "protein_name": "Polypeptide N-acetylgalactosaminyltransferase 1", "gene_name": "GALNT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P59632-1", "protein_name": "ORF3a protein", "gene_name": "3a", "tax_name": "SARS-CoV" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "glycosylation": [ { "glytoucan_ac": "", "type": "O-linked", "subtype": "O-GalNAcylation", "prediction_tool_list": [], "site_category": "reported", "site_category_dict": { "reported": true }, "site_seq": "T", "relation": "attached", "comment": "O-linked (GalNAc...) threonine;O-GalNAcylation", "icn3d_view": {}, "start_pos": 28, "start_aa": "Thr", "end_pos": 28, "end_aa": "Thr", "residue": "Thr", "site_lbl": "Thr28", "evidence": [ { "id": "P59632", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P59632#ptm_processing" }, { "id": "16474139", "database": "PubMed", 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loss of O-glycosylation; when associated with A-28; A-32 and A-34.", "evidence": [ { "database": "UniProtKB", "id": "P59632", "url": "https://www.uniprot.org/uniprotkb/P59632" }, { "database": "PubMed", "id": "16474139", "url": "https://pubmed.ncbi.nlm.nih.gov/16474139" } ], "uniprot_canonical_ac": "P59632-1" }, { "start_pos": 28, "end_pos": 28, "sequence_org": "T", "sequence_mut": "A", "comment": "Complete loss of O-glycosylation; when associated with A-27; A-32 and A-34.", "evidence": [ { "database": "UniProtKB", "id": "P59632", "url": "https://www.uniprot.org/uniprotkb/P59632" }, { "database": "PubMed", "id": "16474139", "url": "https://pubmed.ncbi.nlm.nih.gov/16474139" } ], "uniprot_canonical_ac": "P59632-1" }, { "start_pos": 32, "end_pos": 32, "sequence_org": "T", "sequence_mut": "A", "comment": "Complete loss of O-glycosylation; when associated with A-27; A-28 and A-34.", "evidence": [ { "database": "UniProtKB", "id": "P59632", "url": "https://www.uniprot.org/uniprotkb/P59632" }, { "database": "PubMed", "id": "16474139", "url": "https://pubmed.ncbi.nlm.nih.gov/16474139" } ], "uniprot_canonical_ac": "P59632-1" }, { "start_pos": 34, "end_pos": 34, "sequence_org": "T", "sequence_mut": "A", "comment": "Complete loss of O-glycosylation; when associated with A-27; A-28 and A-32.", "evidence": [ { "database": "UniProtKB", "id": "P59632", "url": "https://www.uniprot.org/uniprotkb/P59632" }, { "database": "PubMed", "id": "16474139", "url": "https://pubmed.ncbi.nlm.nih.gov/16474139" } ], "uniprot_canonical_ac": "P59632-1" } ], "record_id": "pubmed.16474139", "abstract": "", "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 10 } ], "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": 2 }, { "field": "total_sites", "count": 2 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 2 }, { "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": 2 }, { "field": "exact_o_linked_sites", "count": 2 }, { "field": "fuzzy_sites", "count": 0 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl", "filter_code", "uniprot_canonical_ac" ] }, { "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": 2 }, { "field": "total_sites", "count": 2 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 2 }, { "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": 2 }, { "field": "exact_o_linked_sites", "count": 2 }, { "field": "fuzzy_sites", "count": 0 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl", "filter_code", "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": 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": "Structural and functional role of disulphide bonds and substrate binding residues of the human beta-galactoside alpha-2,3-sialyltransferase 1 (hST3Gal1).", "journal": "Scientific reports", "date": "2019", "authors": "Ortiz-Soto ME, Reising S, Schlosser A, Seibel J", "reference": { "type": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q11201-1", "protein_name": "CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1", "gene_name": "ST3GAL1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 139, "end_pos": 139, "sequence_org": "C", "sequence_mut": "S", "comment": "Loss of the catalytic activity; when associated with S-61.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 142, "end_pos": 142, "sequence_org": "C", "sequence_mut": "S", "comment": "Loss of the catalytic activity; when associated with S-281.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 147, "end_pos": 147, "sequence_org": "N", "sequence_mut": "S", "comment": "Decreases the affinity and the specific activity for both donor and acceptor substrates. Decreases the catalytic efficiency for the donor and acceptor substrates by 17- and 32-fold, respectively.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 148, "end_pos": 148, "sequence_org": "S", "sequence_mut": "A", "comment": "Decreases the affinity for the donor and acceptor substrates by 4.5- and 4-fold, respectively. Almost no change in specific activity.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 170, "end_pos": 170, "sequence_org": "N", "sequence_mut": "A", "comment": "Decreases the affinity and the catalytic efficiency for both donor and acceptor substrates.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 191, "end_pos": 191, "sequence_org": "Y", "sequence_mut": "A", "comment": "Drastic decrease of the catalytic efficiency for both donor and acceptor substrates by 44- and 115-fold, respectively.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 230, "end_pos": 230, "sequence_org": "Y", "sequence_mut": "A", "comment": "Decreases the catalytic efficiency for the donor and acceptor substrates by 2.5- and 35-fold, respectively.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 230, "end_pos": 230, "sequence_org": "Y", "sequence_mut": "F", "comment": "Decreases the catalytic efficiency for the donor and acceptor substrates by 2- and 12-fold, respectively.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 281, "end_pos": 281, "sequence_org": "C", "sequence_mut": "S", "comment": "Loss of the catalytic activity; when associated with S-142.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 315, "end_pos": 315, "sequence_org": "V", "sequence_mut": "A", "comment": "Decreases the catalytic efficiency for the donor and acceptor substrates by 5- and 70-fold, respectively.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 315, "end_pos": 315, "sequence_org": "V", "sequence_mut": "Y", "comment": "Drastic decrease of the catalytic efficiency for both donor and acceptor substrates by 67- and 344-fold, respectively. Does not change the enzyme regioselectivity.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 59, "end_pos": 59, "sequence_org": "C", "sequence_mut": "S", "comment": "Has no effect on the catalytic efficiency; when associated with S-64.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", "url": "https://pubmed.ncbi.nlm.nih.gov/31784620" } ], "uniprot_canonical_ac": "Q11201-1" }, { "start_pos": 61, "end_pos": 61, "sequence_org": "C", "sequence_mut": "S", "comment": "Loss of the catalytic activity; when associated with S-139.", "evidence": [ { "database": "UniProtKB", "id": "Q11201", "url": "https://www.uniprot.org/uniprotkb/Q11201" }, { "database": "PubMed", "id": "31784620", 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"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 }, { 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Pechhacker Monika K, Molnar Anna, Pekkola Pacheco Nadja, Thonberg H\u00e5kan, Querat Laurence, Birkeldh Ulrika, Nordgren Ann, Lindstrand Anna", "reference": { "type": "PubMed", "id": "37246745", "url": "https://pubmed.ncbi.nlm.nih.gov/37246745" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q96NL6-1", "protein_name": "Sodium channel and clathrin linker 1", "gene_name": "SCLT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q96NL6", "url": "https://www.uniprot.org/uniprotkb/Q96NL6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.37246745", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", 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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 sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.", "journal": "FEBS Lett.", "date": "2002", "authors": "Jacobsen Linda, Madsen Peder, Nielsen Morten S, Geraerts Wijnand P M, Gliemann J\u00f8rgen, Smit August B, Petersen Claus M", "reference": { "type": "PubMed", "id": "11821067", "url": "https://pubmed.ncbi.nlm.nih.gov/11821067" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92673-1", "protein_name": 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