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Rosenfeld Jill A, Ramanathan Subhadra, Staton Michael, Oberg Kerby C, Clark Robin D, Wenman Catharina, Loughlin Sam, Saad Ramy, Ashraf Tazeen, Male Alison, Tadros Shereen, Boostani Reza, Abdel-Salam Ghada M H, Zaki Maha, Mardi Ali, Hashemi-Gorji Farzad, Abdalla Ebtesam, Manzini M Chiara, Pehlivan Davut, Posey Jennifer E, Gibbs Richard A, Houlden Henry, Alkuraya Fowzan S, Bujakowska Kinga, Maroofian Reza, Lupski James R, Nguyen Long N", "reference": { "type": "PubMed", "id": "39306721", "url": "https://pubmed.ncbi.nlm.nih.gov/39306721" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9Y5Y0-1", "protein_name": "Choline/ethanolamine transporter FLVCR1", "gene_name": "FLVCR1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9Y5Y0", "url": "https://www.uniprot.org/uniprotkb/Q9Y5Y0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } 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MA, Wevers RA, Morava E, Foulquier F, Veltman JA, Lefeber DJ", "reference": { "type": "PubMed", "id": "26833330", "url": "https://pubmed.ncbi.nlm.nih.gov/26833330" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N511-1", "protein_name": "Vacuolar ATPase assembly protein VMA12", "gene_name": "VMA12", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8N511", "url": "https://www.uniprot.org/uniprotkb/Q8N511" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.26833330", "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", 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Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear-cytoplasmic communication.", "journal": "J. Biol. 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U.S.A.", "date": "2001", "authors": "Rai S K, Duh F M, Vigdorovich V, Danilkovitch-Miagkova A, Lerman M I, Miller A D", "reference": { "type": "PubMed", "id": "11296287", "url": "https://pubmed.ncbi.nlm.nih.gov/11296287" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q12891-1", "protein_name": "Hyaluronidase-2", "gene_name": "HYAL2", "tax_name": "Human" }, { "uniprot_canonical_ac": "O35632-1", "protein_name": "Hyaluronidase-2", "gene_name": "Hyal2", "tax_name": "Mouse" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q12891", "url": "https://www.uniprot.org/uniprotkb/Q12891" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.11296287", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": 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"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": 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Natl. Acad. Sci. U.S.A.", "date": "2003", "authors": "Danilkovitch-Miagkova Alla, Duh Fuh-Mei, Kuzmin Igor, Angeloni Debora, Liu Shan-Lu, Miller A Dusty, Lerman Michael I", "reference": { "type": "PubMed", "id": "12676986", "url": "https://pubmed.ncbi.nlm.nih.gov/12676986" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q12891-1", "protein_name": "Hyaluronidase-2", "gene_name": "HYAL2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q04912-1", "protein_name": "Macrophage-stimulating protein receptor", "gene_name": "MST1R", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q12891", "url": "https://www.uniprot.org/uniprotkb/Q12891" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.12676986", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { 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], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 6 }, { "field": "total_sites", "count": 6 }, { "field": "n_linked_sites", "count": 6 }, { "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": 6 }, { "field": "exact_n_linked_sites", "count": 6 }, { "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", "mining_tool", "filter_code", "uniprot_canonical_ac" ] } ] }, { "title": "Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes.", "journal": "The Journal of biological chemistry", "date": "1992-12-05", "authors": "Weston B W, Smith P L, Kelly R J, Lowe J B", "reference": { "type": "PubMed", "id": "1339443", "url": "https://pubmed.ncbi.nlm.nih.gov/1339443" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P51993-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6", "gene_name": "FUT6", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.1339443", "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": "Site-specific fucosylation of sialylated polylactosamines by alpha1,3/4-fucosyltransferases-V and -VI Is defined by amino acids near the N terminus of the catalytic domain.", "journal": "The Journal of biological chemistry", "date": "2007", "authors": "Shetterly S, Jost F, Watson SR, Knegtel R, Macher BA, Holmes EH", "reference": { "type": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P51993-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6", "gene_name": "FUT6", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q11128-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5", "gene_name": "FUT5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 110, "end_pos": 110, "sequence_org": "R", "sequence_mut": "W", "comment": "Reduces dramatically alpha(1,3)fucosyltransferase activity towards type 2 chain acceptors. Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; D-111 and I-112. Increases VIM2 glycolipid product; when associated with T-73; D-111 and I-112.", "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "P51993-1" }, { "start_pos": 111, "end_pos": 111, "sequence_org": "E", "sequence_mut": "D", "comment": "Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; W-110 and I-112. Increases VIM2 glycolipid product; when associated with T-73; W-110 and I-112.", "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "P51993-1" }, { "start_pos": 112, "end_pos": 112, "sequence_org": "V", "sequence_mut": "I", "comment": "Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; W-110 and D-111. Increases VIM2 glycolipid product; when associated with T-73; W-110 and D-111.", "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "P51993-1" }, { "start_pos": 73, "end_pos": 73, "sequence_org": "K", "sequence_mut": "T", "comment": "Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with W-110; D-111 and I-112. Increases VIM2 glycolipid product; when associated with W-110; D-111 and I-112.", "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "P51993-1" }, { "start_pos": 124, "end_pos": 124, "sequence_org": "W", "sequence_mut": "R", "comment": "Increases alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity. Loss of site-specific fucosylation; when associated with E-125 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; E-125 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; E-125 and V-126.", "evidence": [ { "database": "UniProtKB", "id": "Q11128", "url": "https://www.uniprot.org/uniprotkb/Q11128" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" }, { "database": "PubMed", "id": "14718375", "url": "https://pubmed.ncbi.nlm.nih.gov/14718375" } ], "uniprot_canonical_ac": "Q11128-1" }, { "start_pos": 125, "end_pos": 125, "sequence_org": "D", "sequence_mut": "E", "comment": "Loss of site-specific fucosylation; when associated with R-124 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and V-126.", "evidence": [ { "database": "UniProtKB", "id": "Q11128", "url": "https://www.uniprot.org/uniprotkb/Q11128" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "Q11128-1" }, { "start_pos": 126, "end_pos": 126, "sequence_org": "I", "sequence_mut": "V", "comment": "Loss of site-specific fucosylation; when associated with R-124 and E-125. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and E-125. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and E-125.", "evidence": [ { "database": "UniProtKB", "id": "Q11128", "url": "https://www.uniprot.org/uniprotkb/Q11128" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "Q11128-1" }, { "start_pos": 87, "end_pos": 87, "sequence_org": "T", "sequence_mut": "K", "comment": "Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with R-124; E-125 and V-126. Significantly decreases cell-surface expression of VIM2 antigen; when associated with R-124; E-125 and V-126.", "evidence": [ { "database": "UniProtKB", "id": "Q11128", "url": "https://www.uniprot.org/uniprotkb/Q11128" }, { "database": "PubMed", "id": "17604274", "url": "https://pubmed.ncbi.nlm.nih.gov/17604274" } ], "uniprot_canonical_ac": "Q11128-1" } ], "record_id": "pubmed.17604274", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 2 } ], "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": "Distinct human alpha(1,3)-fucosyltransferases drive Lewis-X/sialyl Lewis-X assembly in human cells.", "journal": "J. Biol. Chem.", "date": "2018", "authors": "Mondal N, Dykstra B, Lee J, Ashline DJ, Reinhold VN, Rossi DJ, Sackstein R", "reference": { "type": "PubMed", "id": "29593094", "url": "https://pubmed.ncbi.nlm.nih.gov/29593094" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P51993-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6", "gene_name": "FUT6", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q11128-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5", "gene_name": "FUT5", "tax_name": "Human" }, { "uniprot_canonical_ac": "P21217-1", "protein_name": "3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3", "gene_name": "FUT3", "tax_name": "Human" }, { "uniprot_canonical_ac": "P22083-1", "protein_name": "Alpha-(1,3)-fucosyltransferase 4", "gene_name": "FUT4", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q11130-1", "protein_name": "Alpha-(1,3)-fucosyltransferase 7", "gene_name": "FUT7", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9Y231-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9", "gene_name": "FUT9", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.29593094", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 6 } ], "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": "Using Eukaryotic Expression Systems to Generate Human alpha1,3-Fucosyltransferases That Effectively Create Selectin-Binding Glycans on Stem Cells.", "journal": "Biochemistry", "date": "2020", "authors": "Al-Amoodi AS, Sakashita K, Ali AJ, Zhou R, Lee JM, Tehseen M, Li M, Belmonte JCI, Kusakabe T, Merzaban JS", "reference": { "type": "PubMed", "id": "32901486", "url": "https://pubmed.ncbi.nlm.nih.gov/32901486" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P51993-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6", "gene_name": "FUT6", "tax_name": "Human" }, { "uniprot_canonical_ac": "P16581-1", "protein_name": "E-selectin", "gene_name": "SELE", "tax_name": 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"o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "FUT6 deficiency compromises basophil function by selectively abrogating their sialyl-Lewis x expression.", "journal": "Communications biology", "date": "2021", "authors": "Puan KJ, San Luis B, Yusof N, Kumar D, Andiappan AK, Lee W, Cajic S, Vuckovic D, Chan J, Dollner T, Hou HW, Jiang Y, Tian C, Rapp E, Poidinger M, Wang Y, Soranzo N, Lee B, Rotzschke O", "reference": { "type": "PubMed", "id": "34215830", "url": "https://pubmed.ncbi.nlm.nih.gov/34215830" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P51993-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6", "gene_name": "FUT6", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo 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therapy", "date": "2022-09-23", "authors": "Wang Qian, Liao Chengcheng, Tan Zhangxue, Li Xiaolan, Guan Xiaoyan, Li Hao, Tian Zhongjia, Liu Jianguo, An Jiaxing", "reference": { "type": "PubMed", "id": "36151332", "url": "https://pubmed.ncbi.nlm.nih.gov/36151332" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P51993-1", "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6", "gene_name": "FUT6", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P51993", "url": "https://www.uniprot.org/uniprotkb/P51993" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.36151332", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], 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