[
    {
        "title": "Heat shock factor 1, an inhibitor of non-homologous end joining repair.",
        "journal": "Oncotarget",
        "date": "2015",
        "authors": "Kang GY, Kim EH, Lee HJ, Gil NY, Cha HJ, Lee YS",
        "reference": {
            "type": "PubMed",
            "id": "26359349",
            "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
        },
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        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P12956-1",
                "protein_name": "DNA repair protein Ku70",
                "gene_name": "XRCC6",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P13010-1",
                "protein_name": "DNA repair protein Ku80",
                "gene_name": "XRCC5",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q00613-1",
                "protein_name": "Heat shock factor protein 1",
                "gene_name": "HSF1",
                "tax_name": "Human"
            }
        ],
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                "name": "Homo sapiens",
                "taxid": 9606,
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
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        ],
        "mutagenesis": [
            {
                "start_pos": 216,
                "end_pos": 216,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Does not change interaction with XRCC5 and XRCC6. No PLK1-induced phosphorylation in mitosis. Inhibits PLK1-stimulated ubiquitinylation. Increased protein stability.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                        "id": "26359349",
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                        "id": "18794143",
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                    }
                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 216,
                "end_pos": 216,
                "sequence_org": "S",
                "sequence_mut": "E",
                "comment": "Does not change interaction with XRCC5 and XRCC6. No change in spindle pole localization. Increases weakly PLK1-stimulated ubiquitinylation. No change in protein stability. Increased interaction with BTRC.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
                    },
                    {
                        "database": "PubMed",
                        "id": "26359349",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
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                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
                    }
                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 298,
                "end_pos": 298,
                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Abolishes sumoylation. No effect on phosphorylation of S-303 nor of S-307. No change in subcellular location to nuclear stress granules upon heat shock. Loss of colocalization with SUMO1 to nuclear stress granules upon heat shock. Does not change interaction with XRCC5 and XRCC6. No effect on binding to HSE nor on transactivation of HSP70. Increases transcriptional activity in a DAXX-dependent manner. No change in protein abundance.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
                    },
                    {
                        "database": "PubMed",
                        "id": "24581496",
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                    },
                    {
                        "database": "PubMed",
                        "id": "26359349",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
                    },
                    {
                        "database": "PubMed",
                        "id": "12665592",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12665592"
                    },
                    {
                        "database": "PubMed",
                        "id": "12646186",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12646186"
                    },
                    {
                        "database": "PubMed",
                        "id": "11514557",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/11514557"
                    },
                    {
                        "database": "PubMed",
                        "id": "8946918",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/8946918"
                    },
                    {
                        "database": "PubMed",
                        "id": "15016915",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15016915"
                    }
                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 326,
                "end_pos": 326,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "No phosphorylation. Increased nuclear localization upon heat shock. No effect on oligomerization, DNA-binding activities and nuclear localization. Significant decrease in transcriptional activity by heat shock. Decreases transcriptional activity in a DAXX-dependent manner. Does not change interaction with XRCC5 and XRCC6. Weak decreased PLK1-induced phosphorylation.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
                    },
                    {
                        "database": "PubMed",
                        "id": "15016915",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15016915"
                    },
                    {
                        "database": "PubMed",
                        "id": "15760475",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15760475"
                    },
                    {
                        "database": "PubMed",
                        "id": "26359349",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
                    },
                    {
                        "database": "PubMed",
                        "id": "15661742",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15661742"
                    },
                    {
                        "database": "PubMed",
                        "id": "27354066",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/27354066"
                    }
                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 326,
                "end_pos": 326,
                "sequence_org": "S",
                "sequence_mut": "E",
                "comment": "Does not change interaction with XRCC5 and XRCC6.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
                    },
                    {
                        "database": "PubMed",
                        "id": "26359349",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 419,
                "end_pos": 419,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Does not change interaction with XRCC5 and XRCC6. Decreased nuclear localization upon heat shock. Strongly decreases PLK1-induced phosphorylation. No change in PLK1-induced phosphorylation in mitosis.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                    {
                        "database": "PubMed",
                        "id": "26359349",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
                    },
                    {
                        "database": "PubMed",
                        "id": "15661742",
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                    },
                    {
                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
                    }
                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 419,
                "end_pos": 419,
                "sequence_org": "S",
                "sequence_mut": "E",
                "comment": "Does not change interaction with XRCC5 and XRCC6.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
                    },
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                        "database": "PubMed",
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            },
            {
                "start_pos": 80,
                "end_pos": 80,
                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Does not change interaction with XRCC5 and XRCC6. Loss of nuclear stress bodies localization. Decreased nuclear stress bodies localization. Loss of DNA-binding and transcriptional activities upon heat shock.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                        "id": "19229036",
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                    }
                ],
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        ],
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        "abstract": "",
        "glycosylation": [],
        "snv": [],
        "phosphorylation": [],
        "glycation": [],
        "section_stats": [
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                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation_reported_with_glycan",
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                "table_id": "glycosylation_automatic_literature_mining",
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        ]
    },
    {
        "title": "The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins.",
        "journal": "Nat. Commun.",
        "date": "2016",
        "authors": "Grundy GJ, Rulten SL, Arribas-Bosacoma R, Davidson K, Kozik Z, Oliver AW, Pearl LH, Caldecott KW",
        "reference": {
            "type": "PubMed",
            "id": "27063109",
            "url": "https://pubmed.ncbi.nlm.nih.gov/27063109"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "P12956-1",
                "protein_name": "DNA repair protein Ku70",
                "gene_name": "XRCC6",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9BUH6-1",
                "protein_name": "Protein PAXX",
                "gene_name": "PAXX",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q14191-1",
                "protein_name": "Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN",
                "gene_name": "WRN",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9BWK5-1",
                "protein_name": "Cell cycle regulator of non-homologous end joining",
                "gene_name": "CYREN",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q8IW19-1",
                "protein_name": "Aprataxin and PNK-like factor",
                "gene_name": "APLF",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P13010-1",
                "protein_name": "DNA repair protein Ku80",
                "gene_name": "XRCC5",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9H9Q4-1",
                "protein_name": "Non-homologous end-joining factor 1",
                "gene_name": "NHEJ1",
                "tax_name": "Human"
            }
        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P12956",
                        "url": "https://www.uniprot.org/uniprotkb/P12956"
                    }
                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
            }
        ],
        "mutagenesis": [
            {
                "start_pos": 18,
                "end_pos": 18,
                "sequence_org": "W",
                "sequence_mut": "G",
                "comment": "Abolished interaction with XRCC5 and XRCC6.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q14191",
                        "url": "https://www.uniprot.org/uniprotkb/Q14191"
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                        "id": "27063109",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/27063109"
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                "uniprot_canonical_ac": "Q14191-1"
            },
            {
                "start_pos": 84,
                "end_pos": 84,
                "sequence_org": "E",
                "sequence_mut": "A",
                "comment": "Abolishes exonuclease activity. Restores chromosome stability in depletion experiments.",
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                    {
                        "database": "UniProtKB",
                        "id": "Q14191",
                        "url": "https://www.uniprot.org/uniprotkb/Q14191"
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                "comment": "Abolishes interaction with XRCC5/Ku80 and XRCC6/Ku70 and ability to inhibit classical non-homologous end joining (NHEJ). Does not affect interaction with SF3B1.",
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    {
        "title": "MEK drives BRAF activation through allosteric control of KSR proteins.",
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                "start_pos": 222,
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        "title": "Pyroptosis and Apoptosis Pathways Engage in Bidirectional Crosstalk in Monocytes and Macrophages.",
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