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        "title": "Mouse embryonic stem cells have increased capacity for replication fork restart driven by the specific Filia-Floped protein complex.",
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        "title": "The subcortical maternal complex protein Nlrp4f is involved in cytoplasmic lattice formation and organelle distribution.",
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        "authors": "Qin D, Gao Z, Xiao Y, Zhang X, Ma H, Yu X, Nie X, Fan N, Wang X, Ouyang Y, Sun QY, Yi Z, Li L",
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                        "field": "total_sites",
                        "count": 0
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                    {
                        "field": "o_linked_glycans",
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    {
        "title": "Arachidonate 5-lipoxygenase establishes adaptive humoral immunity by controlling primary B cells and their cognate T-cell help.",
        "journal": "The American journal of pathology",
        "date": "2011-01",
        "authors": "Nagashima Tsutomu, Ichimiya Shingo, Kikuchi Tomoki, Saito Yoshiyuki, Matsumiya Hiroshi, Ara Shihoko, Koshiba Shigeru, Zhang Jun, Hatate Chizuru, Tonooka Akiko, Kubo Terufumi, Ye Rui Carrie, Hirose Bungo, Shirasaki Hideaki, Izumi Takashi, Takami Tsuyoshi, Himi Tetsuo, Sato Noriyuki",
        "reference": {
            "type": "PubMed",
            "id": "21224059",
            "url": "https://pubmed.ncbi.nlm.nih.gov/21224059"
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            {
                "uniprot_canonical_ac": "P48999-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "Alox5",
                "tax_name": "Mouse"
            }
        ],
        "species": [
            {
                "name": "Mus musculus",
                "taxid": 10090,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
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                ],
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                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
            }
        ],
        "record_id": "pubmed.21224059",
        "abstract": "",
        "glycosylation": [],
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        "phosphorylation": [],
        "glycation": [],
        "section_stats": [
            {
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                        "count": 0
                    }
                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation",
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                "table_id": "glycosylation_reported",
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                        "count": 0
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                        "count": 0
                    },
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                        "count": 0
                    },
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                        "count": 0
                    },
                    {
                        "field": "n_linked_glycans",
                        "count": 0
                    },
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                        "field": "o_linked_glycans",
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                ],
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    },
    {
        "title": "5-Lipoxygenase metabolite 4-HDHA is a mediator of the antiangiogenic effect of \u03c9-3 polyunsaturated fatty acids.",
        "journal": "Science translational medicine",
        "date": "2011-02-09",
        "authors": "Sapieha Przemyslaw, Stahl Andreas, Chen Jing, Seaward Molly R, Willett Keirnan L, Krah Nathan M, Dennison Roberta J, Connor Kip M, Aderman Christopher M, Liclican Elvira, Carughi Arianna, Perelman Dalia, Kanaoka Yoshihide, Sangiovanni John Paul, Gronert Karsten, Smith Lois E H",
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            "type": "PubMed",
            "id": "21307302",
            "url": "https://pubmed.ncbi.nlm.nih.gov/21307302"
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        "referenced_glycans": [],
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            {
                "uniprot_canonical_ac": "P48999-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "Alox5",
                "tax_name": "Mouse"
            }
        ],
        "species": [
            {
                "name": "Mus musculus",
                "taxid": 10090,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
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                ],
                "common_name": "Mouse",
                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
            }
        ],
        "record_id": "pubmed.21307302",
        "abstract": "",
        "glycosylation": [],
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        "phosphorylation": [],
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        "section_stats": [
            {
                "table_id": "referenced_proteins",
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                        "count": 0
                    }
                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation",
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                        "count": 0
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                        "field": "n_linked_glycan_sites",
                        "count": 0
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                        "field": "o_linked_glycan_sites",
                        "count": 0
                    },
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                        "field": "n_linked_glycans",
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                "table_id": "glycosylation_automatic_literature_mining",
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                        "field": "total",
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    },
    {
        "title": "Conversion of pro-inflammatory murine Alox5 into an anti-inflammatory 15S-lipoxygenating enzyme by multiple mutations of sequence determinants.",
        "journal": "Archives of biochemistry and biophysics",
        "date": "2013",
        "authors": "Hofheinz K, Kakularam KR, Adel S, Anton M, Polymarasetty A, Reddanna P, Kuhn H, Horn T",
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            "type": "PubMed",
            "id": "23246375",
            "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
        },
        "referenced_glycans": [],
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            {
                "uniprot_canonical_ac": "P48999-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "Alox5",
                "tax_name": "Mouse"
            },
            {
                "uniprot_canonical_ac": "P09917-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "ALOX5",
                "tax_name": "Human"
            }
        ],
        "species": [
            {
                "name": "Mus musculus",
                "taxid": 10090,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    }
                ],
                "common_name": "Mouse",
                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
            }
        ],
        "mutagenesis": [
            {
                "start_pos": 360,
                "end_pos": 360,
                "sequence_org": "F",
                "sequence_mut": "W",
                "comment": "Increases formation of (8S)-hydroperoxyicosatetraenoic acid ((8S)-HPETE). Exhibits a (8S)-lipoxygenase activity; when associated with I-425. Exhibits a (15S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with G-411; I-425 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with G-411; I-425 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE;when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize pro-inflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    },
                    {
                        "database": "PubMed",
                        "id": "31642348",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31642348"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P48999-1"
            },
            {
                "start_pos": 411,
                "end_pos": 411,
                "sequence_org": "A",
                "sequence_mut": "G",
                "comment": "Decreases (5S)-lipoxygenase activity. Forms 9-hydroperoxyicosatetraenoic acid (9-HPETE) as the major arachidonic acid oxygenation product. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; I-425 and M-426.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P48999-1"
            },
            {
                "start_pos": 425,
                "end_pos": 425,
                "sequence_org": "A",
                "sequence_mut": "I",
                "comment": "Decreases arachidonate (5S)-lipoxygenase activity. Decreases arachidonate 5 lipoxygenase activity; when associated with A-604. Exhibits a (8S)-lipoxygenase activity; when associated with W-360. Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize pro-inflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    },
                    {
                        "database": "PubMed",
                        "id": "31642348",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31642348"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P48999-1"
            },
            {
                "start_pos": 426,
                "end_pos": 426,
                "sequence_org": "N",
                "sequence_mut": "M",
                "comment": "Increases formation of (8S)-hydroperoxyicosatetraenoic acid ((8S)-HPETE) and (12S)-hydroperoxyicosatetraenoic acid ((12S)-HPETE). Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and I-425. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and I-425.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    },
                    {
                        "database": "PubMed",
                        "id": "31642348",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31642348"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P48999-1"
            },
            {
                "start_pos": 604,
                "end_pos": 604,
                "sequence_org": "A",
                "sequence_mut": "I",
                "comment": "Decreases arachidonate (5S)-lipoxygenase activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P48999-1"
            },
            {
                "start_pos": 360,
                "end_pos": 360,
                "sequence_org": "F",
                "sequence_mut": "W",
                "comment": "Loss of (5S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of (5S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form mostly (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with I-425: M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with I-425: M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with I-425: M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with I-425: M-426 and I-604.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    },
                    {
                        "database": "PubMed",
                        "id": "31664810",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31664810"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P09917-1"
            },
            {
                "start_pos": 425,
                "end_pos": 425,
                "sequence_org": "A",
                "sequence_mut": "I",
                "comment": "Loss of (5S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of (5S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; M-426 and I-604.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    },
                    {
                        "database": "PubMed",
                        "id": "31664810",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31664810"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P09917-1"
            },
            {
                "start_pos": 426,
                "end_pos": 426,
                "sequence_org": "N",
                "sequence_mut": "M",
                "comment": "Loss of (5S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and I-425. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and I-604.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    },
                    {
                        "database": "PubMed",
                        "id": "31664810",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31664810"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P09917-1"
            },
            {
                "start_pos": 604,
                "end_pos": 604,
                "sequence_org": "A",
                "sequence_mut": "I",
                "comment": "Loss of (5S)-lipoxygenase activity. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity;when associated with W-360; I-425 and M-426. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and M-426. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of linoleic acid to (13S)- and (9 S)-HODE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and M-426. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and M-426. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and M-426.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    },
                    {
                        "database": "PubMed",
                        "id": "31664810",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/31664810"
                    },
                    {
                        "database": "PubMed",
                        "id": "23246375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23246375"
                    }
                ],
                "uniprot_canonical_ac": "P09917-1"
            }
        ],
        "record_id": "pubmed.23246375",
        "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": [
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                        "field": "total",
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                    },
                    {
                        "field": "total_sites",
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                    },
                    {
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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": "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": "5-Lipoxygenase plays a pivotal role in endothelial adhesion of monocytes via an increased expression of Mac-1.",
        "journal": "Cardiovascular research",
        "date": "2013-09-01",
        "authors": "Lee Seung Jin, Choi Eun Kyoung, Seo Kyo Won, Bae Jin Ung, Kim Yun Hak, Park So Youn, Oh Sae Ock, Kim Chi Dae",
        "reference": {
            "type": "PubMed",
            "id": "23720274",
            "url": "https://pubmed.ncbi.nlm.nih.gov/23720274"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P48999-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "Alox5",
                "tax_name": "Mouse"
            }
        ],
        "species": [
            {
                "name": "Mus musculus",
                "taxid": 10090,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    }
                ],
                "common_name": "Mouse",
                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
            }
        ],
        "record_id": "pubmed.23720274",
        "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
                    },
                    {
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                        "count": 0
                    },
                    {
                        "field": "o_linked_sites",
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                    },
                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
                    },
                    {
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                    },
                    {
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                        "count": 0
                    },
                    {
                        "field": "o_linked_glycans",
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                    }
                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation_predicted",
                "table_stats": [
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                        "field": "total",
                        "count": 0
                    },
                    {
                        "field": "total_sites",
                        "count": 0
                    },
                    {
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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_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": "Critical role of 5-lipoxygenase and heme oxygenase-1 in wound healing.",
        "journal": "The Journal of investigative dermatology",
        "date": "2014-05",
        "authors": "Brogliato Ariane R, Moor Andrea N, Kesl Shannon L, Guilherme Rafael F, Georgii Jana\u00edna L, Peters-Golden Marc, Canetti Claudio, Gould Lisa J, Benjamim Claudia F",
        "reference": {
            "type": "PubMed",
            "id": "24226420",
            "url": "https://pubmed.ncbi.nlm.nih.gov/24226420"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P48999-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "Alox5",
                "tax_name": "Mouse"
            }
        ],
        "species": [
            {
                "name": "Mus musculus",
                "taxid": 10090,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P48999",
                        "url": "https://www.uniprot.org/uniprotkb/P48999"
                    }
                ],
                "common_name": "Mouse",
                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
            }
        ],
        "record_id": "pubmed.24226420",
        "abstract": "",
        "glycosylation": [],
        "mutagenesis": [],
        "snv": [],
        "phosphorylation": [],
        "glycation": [],
        "section_stats": [
            {
                "table_id": "referenced_proteins",
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                    "protein_name",
                    "gene_name",
                    "tax_name"
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                ],
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            },
            {
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                "table_stats": [
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                    },
                    {
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                    },
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                    },
                    {
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                    },
                    {
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                    },
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                    }
                ],
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            },
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                    },
                    {
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                    }
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            },
            {
                "table_id": "glycosylation_reported",
                "table_stats": [
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                    {
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                    },
                    {
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                    {
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                    },
                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
                    },
                    {
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                        "count": 0
                    },
                    {
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                    },
                    {
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                "end_pos": 425,
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                "comment": "Decreases arachidonate (5S)-lipoxygenase activity. Decreases arachidonate 5 lipoxygenase activity; when associated with A-604. Exhibits a (8S)-lipoxygenase activity; when associated with W-360. Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize pro-inflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426.",
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    {
        "title": "Inhibition of host 5-lipoxygenase reduces overexuberant inflammatory responses and mortality associated with Cryptococcus meningoencephalitis.",
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        "authors": "Castro-Lopez Natalia, Campuzano Althea, Mdalel Elysa, Vanegas Difernando, Chaturvedi Ashok, Nguyen Phung, Pulse Mark, Cardona Astrid E, Wormley Floyd L",
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        "title": "cDNA cloning, expression, mutagenesis, intracellular localization, and gene chromosomal assignment of mouse 5-lipoxygenase.",
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        "authors": "Chen XS, Naumann TA, Kurre U, Jenkins NA, Copeland NG, Funk CD",
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