[
    {
        "title": "Carbohydrate structure of human pancreatic elastase 1.",
        "journal": "The Biochemical journal",
        "date": "1991",
        "authors": "Wendorf P, Linder D, Sziegoleit A, Geyer R",
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    {
        "title": "Phosphorylation by protein kinase a inhibits nuclear import of 5-lipoxygenase.",
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        "title": "Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export.",
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                        "id": "P09917",
                        "url": "https://www.ebi.ac.uk/intact/interactors/id:P09917*"
                    },
                    {
                        "database": "iPTMnet",
                        "id": "P09917",
                        "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09917"
                    },
                    {
                        "database": "PubMed",
                        "id": "24860872",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/24860872"
                    },
                    {
                        "database": "PubMed",
                        "id": "15280375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15280375"
                    },
                    {
                        "database": "PubMed",
                        "id": "16230355",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/16230355"
                    },
                    {
                        "database": "PubMed",
                        "id": "26210919",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26210919"
                    }
                ],
                "site_lbl": "Ser523",
                "uniprot_canonical_ac": "P09917-1"
            },
            {
                "start_pos": 524,
                "end_pos": 524,
                "kinase_uniprot_canonical_ac": "",
                "kinase_gene_name": "",
                "residue": "Ser",
                "comment": "Phosphoserine; by PKA",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    },
                    {
                        "database": "iPTMnet",
                        "id": "P09917",
                        "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09917"
                    },
                    {
                        "database": "PubMed",
                        "id": "26210919",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26210919"
                    },
                    {
                        "database": "PubMed",
                        "id": "15280375",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15280375"
                    }
                ],
                "site_lbl": "Ser524",
                "uniprot_canonical_ac": "P09917-1"
            }
        ],
        "record_id": "pubmed.26210919",
        "abstract": "",
        "glycosylation": [],
        "mutagenesis": [],
        "snv": [],
        "glycation": [],
        "section_stats": [
            {
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                        "count": 1
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            {
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                ],
                "sort_fields": []
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            {
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                    {
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                        "count": 2
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                    {
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                        "count": 2
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                ],
                "sort_fields": [
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                    "end_pos",
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                    "kinase_gene_name",
                    "residue",
                    "comment",
                    "site_lbl",
                    "uniprot_canonical_ac"
                ]
            },
            {
                "table_id": "glycosylation_reported",
                "table_stats": [
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                        "count": 0
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                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
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                    {
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                    {
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                    {
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                    }
                ],
                "sort_fields": []
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            {
                "table_id": "glycosylation_reported_with_glycan",
                "table_stats": [
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                    {
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                    {
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                ],
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            {
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                    {
                        "field": "o_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "n_linked_glycans",
                        "count": 0
                    },
                    {
                        "field": "o_linked_glycans",
                        "count": 0
                    }
                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation_automatic_literature_mining",
                "table_stats": [
                    {
                        "field": "total",
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                    {
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                    {
                        "field": "o_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "n_linked_glycans",
                        "count": 0
                    },
                    {
                        "field": "o_linked_glycans",
                        "count": 0
                    }
                ],
                "sort_fields": []
            }
        ]
    },
    {
        "title": "Molecular cloning and amino acid sequence of human 5-lipoxygenase.",
        "journal": "Proc. Natl. Acad. Sci. U.S.A.",
        "date": "1988",
        "authors": "Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B",
        "reference": {
            "type": "PubMed",
            "id": "2829172",
            "url": "https://pubmed.ncbi.nlm.nih.gov/2829172"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P09917-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "ALOX5",
                "tax_name": "Human"
            }
        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    }
                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
            }
        ],
        "record_id": "pubmed.2829172",
        "abstract": "",
        "glycosylation": [],
        "mutagenesis": [],
        "snv": [],
        "phosphorylation": [],
        "glycation": [],
        "section_stats": [
            {
                "table_id": "referenced_proteins",
                "table_stats": [
                    {
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                        "count": 1
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                ],
                "sort_fields": [
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                    "protein_name",
                    "gene_name",
                    "tax_name"
                ]
            },
            {
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                "table_stats": [
                    {
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                        "count": 0
                    }
                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation",
                "table_stats": [
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                        "field": "total",
                        "count": 0
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                        "count": 0
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                    {
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                    },
                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
                    },
                    {
                        "field": "o_linked_glycan_sites",
                        "count": 0
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                        "count": 0
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                        "count": 0
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                ],
                "sort_fields": []
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            {
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                ],
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                ],
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                    {
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                ],
                "sort_fields": []
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                "table_stats": [
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                    {
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                ],
                "sort_fields": []
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        ]
    },
    {
        "title": "Mutations of Triad Determinants Changes the Substrate Alignment at the Catalytic Center of Human ALOX5.",
        "journal": "ACS chemical biology",
        "date": "2019",
        "authors": "Ivanov I, Golovanov AB, Ferretti C, Canyelles-Nino M, Heydeck D, Stehling S, Lluch JM, Gonzalez-Lafont A, Kuhn H",
        "reference": {
            "type": "PubMed",
            "id": "31664810",
            "url": "https://pubmed.ncbi.nlm.nih.gov/31664810"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P09917-1",
                "protein_name": "Polyunsaturated fatty acid 5-lipoxygenase",
                "gene_name": "ALOX5",
                "tax_name": "Human"
            }
        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
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                        "database": "UniProtKB",
                        "id": "P09917",
                        "url": "https://www.uniprot.org/uniprotkb/P09917"
                    }
                ],
                "common_name": "Human",
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                "reference_species": "Homo sapiens [9606]"
            }
        ],
        "mutagenesis": [
            {
                "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.31664810",
        "abstract": "",
        "glycosylation": [],
        "snv": [],
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