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                "table_id": "glycosylation_reported_with_glycan",
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                ],
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            {
                "table_id": "glycosylation_automatic_literature_mining",
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    },
    {
        "title": "Molecular bases of catalysis and ADP-ribose preference of human Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase and conversion by mutagenesis to a preferential cyclic ADP-ribose phosphohydrolase.",
        "journal": "PloS one",
        "date": "2015",
        "authors": "Cabezas A, Ribeiro JM, Rodrigues JR, Lopez-Villamizar I, Fernandez A, Canales J, Pinto RM, Costas MJ, Cameselle JC",
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            "url": "https://pubmed.ncbi.nlm.nih.gov/25692488"
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            {
                "uniprot_canonical_ac": "Q9UKK9-1",
                "protein_name": "ADP-sugar pyrophosphatase",
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                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q96DE0-1",
                "protein_name": "U8 snoRNA-decapping enzyme",
                "gene_name": "NUDT16",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9NV35-1",
                "protein_name": "Nucleotide triphosphate diphosphatase NUDT15",
                "gene_name": "NUDT15",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q3LIE5-1",
                "protein_name": "Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase",
                "gene_name": "ADPRM",
                "tax_name": "Human"
            }
        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
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                    {
                        "database": "UniProtKB",
                        "id": "Q9UKK9",
                        "url": "https://www.uniprot.org/uniprotkb/Q9UKK9"
                    }
                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
            }
        ],
        "mutagenesis": [
            {
                "start_pos": 110,
                "end_pos": 110,
                "sequence_org": "N",
                "sequence_mut": "A",
                "comment": "Catalytic efficiency is reduced 40-fold with ADP-D-ribose and 100-fold with CDP-choline as substrates.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q3LIE5",
                        "url": "https://www.uniprot.org/uniprotkb/Q3LIE5"
                    },
                    {
                        "database": "PubMed",
                        "id": "25692488",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/25692488"
                    }
                ],
                "uniprot_canonical_ac": "Q3LIE5-1"
            },
            {
                "start_pos": 111,
                "end_pos": 111,
                "sequence_org": "H",
                "sequence_mut": "A",
                "comment": "Catalytic efficiency is reduced 200-fold with ADP-D-ribose and 500-fold with CDP-choline as substrates.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q3LIE5",
                        "url": "https://www.uniprot.org/uniprotkb/Q3LIE5"
                    },
                    {
                        "database": "PubMed",
                        "id": "25692488",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/25692488"
                    }
                ],
                "uniprot_canonical_ac": "Q3LIE5-1"
            },
            {
                "start_pos": 111,
                "end_pos": 111,
                "sequence_org": "H",
                "sequence_mut": "N",
                "comment": "Catalytic efficiency is reduced 20-fold with ADP-D-ribose and 75-fold with CDP-choline as substrates.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q3LIE5",
                        "url": "https://www.uniprot.org/uniprotkb/Q3LIE5"
                    },
                    {
                        "database": "PubMed",
                        "id": "25692488",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/25692488"
                    }
                ],
                "uniprot_canonical_ac": "Q3LIE5-1"
            },
            {
                "start_pos": 196,
                "end_pos": 196,
                "sequence_org": "L",
                "sequence_mut": "A",
                "comment": "Catalytic efficiency is reduced 5-fold with ADP-D-ribose and 2-fold with CDP-choline as substrates. Catalytic efficiency is reduced 100-fold with ADP-D-ribose; when associated with A-37.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q3LIE5",
                        "url": "https://www.uniprot.org/uniprotkb/Q3LIE5"
                    },
                    {
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                ],
                "uniprot_canonical_ac": "Q3LIE5-1"
            },
            {
                "start_pos": 210,
                "end_pos": 210,
                "sequence_org": "F",
                "sequence_mut": "A",
                "comment": "Catalytic efficiency is reduced 70-fold with ADP-D-ribose and 40-fold with CDP-choline as substrates.",
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                    {
                        "database": "UniProtKB",
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                    {
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                ],
                "uniprot_canonical_ac": "Q3LIE5-1"
            },
            {
                "start_pos": 253,
                "end_pos": 253,
                "sequence_org": "C",
                "sequence_mut": "A",
                "comment": "Has a very mild effect on enzymatic activity; catalytic efficiency is increased 1.7-fold with ADP-D-ribose and is unchanged with CDP-choline as substrates.",
                "evidence": [
                    {
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                "start_pos": 27,
                "end_pos": 27,
                "sequence_org": "Q",
                "sequence_mut": "H",
                "comment": "Catalytic efficiency is reduced 11-fold with ADP-D-ribose or CDP-choline as substrate.",
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                    {
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                "start_pos": 37,
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                "sequence_org": "F",
                "sequence_mut": "A",
                "comment": "Catalytic efficiency is reduced 50-fold with ADP-D-ribose and 4-fold with CDP-choline as substrates. Catalytic efficiency is reduced 100-fold with ADP-D-ribose as substrate; when associated with A-196.",
                "evidence": [
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            {
                "start_pos": 37,
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                "sequence_org": "F",
                "sequence_mut": "Y",
                "comment": "Does not affect enzymatic activity.",
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            {
                "start_pos": 43,
                "end_pos": 43,
                "sequence_org": "R",
                "sequence_mut": "A",
                "comment": "Loss of enzymatic activity.",
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        ],
        "record_id": "pubmed.25692488",
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                "table_id": "glycosylation_reported",
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                ],
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    },
    {
        "title": "ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling.",
        "journal": "Science (New York, N.Y.)",
        "date": "2016",
        "authors": "Wright RH, Lioutas A, Le Dily F, Soronellas D, Pohl A, Bonet J, Nacht AS, Samino S, Font-Mateu J, Vicent GP, Wierer M, Trabado MA, Schelhorn C, Carolis C, Macias MJ, Yanes O, Oliva B, Beato M",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "Q86W56-1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "P09874-1",
                "protein_name": "Poly [ADP-ribose] polymerase 1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "Q9HAN9-1",
                "protein_name": "Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1",
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        ],
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                "name": "Homo sapiens",
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
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        ],
        "mutagenesis": [
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                "start_pos": 112,
                "end_pos": 112,
                "sequence_org": "E",
                "sequence_mut": "Q",
                "comment": "Catalytic inactive mutant for both ADP-sugar pyrophosphatase and nuclear ATP-synthesis activities. Reduces catalytic rate 6300-fold.",
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        "date": "2004",
        "authors": "Carman Julie A, Nadler Steven G",
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