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        "title": "Polymorphism of the h allele and the population frequency of sporadic nonfunctional alleles.",
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                        "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": [
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                        "field": "total",
                        "count": 0
                    },
                    {
                        "field": "total_sites",
                        "count": 0
                    },
                    {
                        "field": "n_linked_sites",
                        "count": 0
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                    {
                        "field": "o_linked_sites",
                        "count": 0
                    },
                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
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                        "field": "o_linked_glycan_sites",
                        "count": 0
                    },
                    {
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                    },
                    {
                        "field": "o_linked_glycans",
                        "count": 0
                    }
                ],
                "sort_fields": []
            }
        ]
    },
    {
        "title": "Acceptor specificity of different length constructs of human recombinant alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzing activity.",
        "journal": "The Journal of biological chemistry",
        "date": "1995",
        "authors": "de Vries T, Srnka CA, Palcic MM, Swiedler SJ, van den Eijnden DH, Macher BA",
        "reference": {
            "type": "PubMed",
            "id": "7721776",
            "url": "https://pubmed.ncbi.nlm.nih.gov/7721776"
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            {
                "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"
            }
        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
                        "url": "https://www.uniprot.org/uniprotkb/Q11128"
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
            }
        ],
        "record_id": "pubmed.7721776",
        "abstract": "",
        "glycosylation": [],
        "mutagenesis": [],
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        "phosphorylation": [],
        "glycation": [],
        "section_stats": [
            {
                "table_id": "referenced_proteins",
                "table_stats": [
                    {
                        "field": "total",
                        "count": 2
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                ],
                "sort_fields": [
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                    "protein_name",
                    "gene_name",
                    "tax_name"
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            },
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                "table_stats": [
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                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation",
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                    {
                        "field": "n_linked_glycans",
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                ],
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                    {
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        ]
    },
    {
        "title": "Human alpha1,3/4-fucosyltransferases. I. Identification of amino acids involved in acceptor substrate binding by site-directed mutagenesis.",
        "journal": "The Journal of biological chemistry",
        "date": "1998",
        "authors": "Nguyen AT, Holmes EH, Whitaker JM, Ho S, Shetterly S, Macher BA",
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            {
                "uniprot_canonical_ac": "Q11128-1",
                "protein_name": "4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5",
                "gene_name": "FUT5",
                "tax_name": "Human"
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        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
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                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
                        "url": "https://www.uniprot.org/uniprotkb/Q11128"
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
            }
        ],
        "mutagenesis": [
            {
                "start_pos": 101,
                "end_pos": 101,
                "sequence_org": "A",
                "sequence_mut": "T",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-105; R-110; K-111 and T-118.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
                        "url": "https://www.uniprot.org/uniprotkb/Q11128"
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                    {
                        "database": "PubMed",
                        "id": "9737988",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9737988"
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                ],
                "uniprot_canonical_ac": "Q11128-1"
            },
            {
                "start_pos": 105,
                "end_pos": 105,
                "sequence_org": "N",
                "sequence_mut": "H",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; R-110; K-111 and T-118.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
                        "url": "https://www.uniprot.org/uniprotkb/Q11128"
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                    {
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                        "id": "9737988",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9737988"
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                ],
                "uniprot_canonical_ac": "Q11128-1"
            },
            {
                "start_pos": 110,
                "end_pos": 110,
                "sequence_org": "S",
                "sequence_mut": "R",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; K-111 and T-118.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
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                    {
                        "database": "PubMed",
                        "id": "9737988",
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                ],
                "uniprot_canonical_ac": "Q11128-1"
            },
            {
                "start_pos": 111,
                "end_pos": 111,
                "sequence_org": "S",
                "sequence_mut": "K",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and T-118.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
                        "url": "https://www.uniprot.org/uniprotkb/Q11128"
                    },
                    {
                        "database": "PubMed",
                        "id": "9737988",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9737988"
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                ],
                "uniprot_canonical_ac": "Q11128-1"
            },
            {
                "start_pos": 118,
                "end_pos": 118,
                "sequence_org": "A",
                "sequence_mut": "T",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and K-111.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q11128",
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                    {
                        "database": "PubMed",
                        "id": "9737988",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9737988"
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                ],
                "uniprot_canonical_ac": "Q11128-1"
            },
            {
                "start_pos": 86,
                "end_pos": 86,
                "sequence_org": "N",
                "sequence_mut": "H",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 oligosaccharide acceptor; when associated with I-87 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 oligosaccharide acceptors; when associated with I-87 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with I-87 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with I-87 and S-92.",
                "evidence": [
                    {
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                "start_pos": 87,
                "end_pos": 87,
                "sequence_org": "T",
                "sequence_mut": "I",
                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and S-92.",
                "evidence": [
                    {
                        "database": "UniProtKB",
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                "start_pos": 92,
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                "sequence_org": "P",
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                "comment": "Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and I-87. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and I-87.",
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                "table_id": "glycosylation_reported",
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                ],
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        ]
    },
    {
        "title": "Human alpha1,3/4-fucosyltransferases. II. A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties.",
        "journal": "The Journal of biological chemistry",
        "date": "1998-09-25",
        "authors": "Vo L, Lee S, Marcinko M C, Holmes E H, Macher B A",
        "reference": {
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                "gene_name": "FUT5",
                "tax_name": "Human"
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        ],
        "species": [
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                "name": "Homo sapiens",
                "taxid": 9606,
                "evidence": [
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                        "database": "UniProtKB",
                        "id": "Q11128",
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
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        ],
        "record_id": "pubmed.9737989",
        "abstract": "",
        "glycosylation": [],
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