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                        "field": "o_linked_sites",
                        "count": 0
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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": []
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            {
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                    {
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                    {
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                ],
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        ]
    },
    {
        "title": "Caspase-1 interdomain linker cleavage is required for pyroptosis.",
        "journal": "Life science alliance",
        "date": "2020",
        "authors": "Ball DP, Taabazuing CY, Griswold AR, Orth EL, Rao SD, Kotliar IB, Vostal LE, Johnson DC, Bachovchin DA",
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            {
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        ],
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                ],
                "common_name": "Human",
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                "reference_species": "Homo sapiens [9606]"
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        ],
        "mutagenesis": [
            {
                "start_pos": 285,
                "end_pos": 285,
                "sequence_org": "C",
                "sequence_mut": "A",
                "comment": "Loss of protease activity. Loss of SPHK2 cleavage and release in apoptotic cells.",
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                    {
                        "database": "UniProtKB",
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                    {
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                    {
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                    {
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                    {
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                    {
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                ],
                "uniprot_canonical_ac": "P29466-1"
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            {
                "start_pos": 285,
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                "sequence_org": "C",
                "sequence_mut": "S",
                "comment": "Loss of protease activity. Loss of SPHK2 cleavage and release in apoptotic cells.",
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                    {
                        "database": "UniProtKB",
                        "id": "P29466",
                        "url": "https://www.uniprot.org/uniprotkb/P29466"
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                    {
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                    {
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                    {
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                    {
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                    {
                        "database": "PubMed",
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                        "url": "https://pubmed.ncbi.nlm.nih.gov/32553275"
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                ],
                "uniprot_canonical_ac": "P29466-1"
            },
            {
                "start_pos": 297,
                "end_pos": 297,
                "sequence_org": "D",
                "sequence_mut": "N",
                "comment": "In IDL(uncl); abolished cleavage in the interdomain region; when associated with 315-N-N-316.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P29466",
                        "url": "https://www.uniprot.org/uniprotkb/P29466"
                    },
                    {
                        "database": "PubMed",
                        "id": "32051255",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/32051255"
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                ],
                "uniprot_canonical_ac": "P29466-1"
            },
            {
                "start_pos": 315,
                "end_pos": 316,
                "sequence_org": "DD",
                "sequence_mut": "NN",
                "comment": "In IDL(uncl); abolished cleavage in the interdomain region; when associated with N-297.",
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                    {
                        "database": "UniProtKB",
                        "id": "P29466",
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                    {
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                ],
                "uniprot_canonical_ac": "P29466-1"
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            {
                "start_pos": 1213,
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                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Complete loss of autocatalytic processing and of IL1B release. Autocatalytic processing cannot be restored by treatment with hydroxylamine. Abolished interaction with DPP9. Loss of activation by dsRNA or positive-strand RNA virus.",
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                    {
                        "database": "UniProtKB",
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                    {
                        "database": "PubMed",
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                    {
                        "database": "PubMed",
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                    {
                        "database": "PubMed",
                        "id": "33731932",
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                    {
                        "database": "PubMed",
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                    {
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                ],
                "uniprot_canonical_ac": "Q9C000-1"
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            {
                "start_pos": 297,
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                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Complete loss of autocatalytic cleavage. Abolished ability to form the CARD8 inflammasome and trigger pyroptosis. Abolished sensitivity to Val-boroPro. Does not affect interaction with DPP9.",
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                    {
                        "database": "UniProtKB",
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                    {
                        "database": "PubMed",
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                        "database": "PubMed",
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                    {
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                    {
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                        "id": "31525884",
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                    {
                        "database": "PubMed",
                        "id": "33542150",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/33542150"
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                    {
                        "database": "PubMed",
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            {
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                ],
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            {
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                ],
                "sort_fields": []
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        ]
    },
    {
        "title": "PIM1 controls GBP1 activity to limit self-damage and to guard against pathogen infection.",
        "journal": "Science (New York, N.Y.)",
        "date": "2023-10-06",
        "authors": "Fisch Daniel, Pfleiderer Moritz M, Anastasakou Eleni, Mackie Gillian M, Wendt Fabian, Liu Xiangyang, Clough Barbara, Lara-Reyna Samuel, Encheva Vesela, Snijders Ambrosius P, Bando Hironori, Yamamoto Masahiro, Beggs Andrew D, Mercer Jason, Shenoy Avinash R, Wollscheid Bernd, Maslowski Kendle M, Galej Wojtek P, Frickel Eva-Maria",
        "reference": {
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            "id": "37797010",
            "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
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        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P29466-1",
                "protein_name": "Caspase-1",
                "gene_name": "CASP1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P11309-1",
                "protein_name": "Serine/threonine-protein kinase pim-1",
                "gene_name": "PIM1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P32455-1",
                "protein_name": "Guanylate-binding protein 1",
                "gene_name": "GBP1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P31947-1",
                "protein_name": "14-3-3 protein sigma",
                "gene_name": "SFN",
                "tax_name": "Human"
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        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
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                        "database": "UniProtKB",
                        "id": "P29466",
                        "url": "https://www.uniprot.org/uniprotkb/P29466"
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
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        ],
        "mutagenesis": [
            {
                "start_pos": 81,
                "end_pos": 81,
                "sequence_org": "P",
                "sequence_mut": "S",
                "comment": "Abolished kinase activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P11309",
                        "url": "https://www.uniprot.org/uniprotkb/P11309"
                    },
                    {
                        "database": "PubMed",
                        "id": "15808862",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15808862"
                    },
                    {
                        "database": "PubMed",
                        "id": "37797010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
                    }
                ],
                "uniprot_canonical_ac": "P11309-1"
            },
            {
                "start_pos": 151,
                "end_pos": 151,
                "sequence_org": "R",
                "sequence_mut": "A",
                "comment": "Reduced phosphorylation by PIM1.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P32455",
                        "url": "https://www.uniprot.org/uniprotkb/P32455"
                    },
                    {
                        "database": "PubMed",
                        "id": "37797010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
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                ],
                "uniprot_canonical_ac": "P32455-1"
            },
            {
                "start_pos": 153,
                "end_pos": 153,
                "sequence_org": "R",
                "sequence_mut": "A",
                "comment": "Abolished phosphorylation by PIM1.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P32455",
                        "url": "https://www.uniprot.org/uniprotkb/P32455"
                    },
                    {
                        "database": "PubMed",
                        "id": "37797010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
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                ],
                "uniprot_canonical_ac": "P32455-1"
            },
            {
                "start_pos": 153,
                "end_pos": 158,
                "sequence_org": "RSKSSP",
                "sequence_mut": "ASKSSA",
                "comment": "Abolished phosphorylation by PIM1 and interaction with 14-3-3 protein sigma (SFN).",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P32455",
                        "url": "https://www.uniprot.org/uniprotkb/P32455"
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                    {
                        "database": "PubMed",
                        "id": "37797010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
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                ],
                "uniprot_canonical_ac": "P32455-1"
            },
            {
                "start_pos": 155,
                "end_pos": 155,
                "sequence_org": "K",
                "sequence_mut": "A",
                "comment": "Abolished phosphorylation by PIM1.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P32455",
                        "url": "https://www.uniprot.org/uniprotkb/P32455"
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                    {
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                        "id": "37797010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
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                ],
                "uniprot_canonical_ac": "P32455-1"
            },
            {
                "start_pos": 156,
                "end_pos": 156,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Reduced phosphorylation by PIM1, leading to hyperactivation and Golgi fragmentation.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P32455",
                        "url": "https://www.uniprot.org/uniprotkb/P32455"
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                    {
                        "database": "PubMed",
                        "id": "37797010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/37797010"
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                ],
                "uniprot_canonical_ac": "P32455-1"
            },
            {
                "start_pos": 157,
                "end_pos": 157,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "No effect.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P32455",
                        "url": "https://www.uniprot.org/uniprotkb/P32455"
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                        "id": "37797010",
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                ],
                "uniprot_canonical_ac": "P32455-1"
            },
            {
                "start_pos": 427,
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                "sequence_org": "Y",
                "sequence_mut": "F",
                "comment": "No effect.",
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                "sequence_org": "T",
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                "comment": "Does not affect interaction with 14-3-3 protein sigma (SFN).",
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        "authors": "Park S, Osmers U, Raman G, Schwantes RH, Diaz MO, Bushweller JH",
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        "title": "Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase.",
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    {
        "title": "Farber lipogranulomatosis: clinical and molecular genetic analysis reveals a novel mutation in an Indian family.",
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        "authors": "Devi ARR, Gopikrishna M, Ratheesh R, Savithri G, Swarnalata G, Bashyam M",
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