[
    {
        "title": "Protein phosphatase 5 regulates the function of 53BP1 after neocarzinostatin-induced DNA damage.",
        "journal": "The Journal of biological chemistry",
        "date": "2009",
        "authors": "Kang Y, Lee JH, Hoan NN, Sohn HM, Chang IY, You HJ",
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                    {
                        "field": "o_linked_glycans",
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                ],
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    {
        "title": "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage.",
        "journal": "Cell",
        "date": "2009",
        "authors": "Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES, Nakada S, Ylanko J, Olivarius S, Mendez M, Oldreive C, Wildenhain J, Tagliaferro A, Pelletier L, Taubenheim N, Durandy A, Byrd PJ, Stankovic T, Taylor AM, Durocher D",
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                "protein_name": "Mediator of DNA damage checkpoint protein 1",
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                "uniprot_canonical_ac": "O94953-1",
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                "uniprot_canonical_ac": "P53041-1",
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                "uniprot_canonical_ac": "P57053-1",
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            {
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        "title": "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins.",
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        "authors": "Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, Pepperkok R, Ellenberg J, Panier S, Durocher D, Bartek J, Lukas J, Lukas C",
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    {
        "title": "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control.",
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        "authors": "Wang B, Hurov K, Hofmann K, Elledge SJ",
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        "title": "Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase.",
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        "title": "NBA1/MERIT40 and BRE interaction is required for the integrity of two distinct deubiquitinating enzyme BRCC36-containing complexes.",
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        "authors": "Hu X, Kim JA, Castillo A, Huang M, Liu J, Wang B",
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        "title": "MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites.",
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    {
        "title": "Structural mechanism of the phosphorylation-dependent dimerization of the MDC1 forkhead-associated domain.",
        "journal": "Nucleic acids research",
        "date": "2012",
        "authors": "Liu J, Luo S, Zhao H, Liao J, Li J, Yang C, Xu B, Stern DF, Xu X, Ye K",
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    {
        "title": "RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites.",
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        "authors": "Mallette FA, Mattiroli F, Cui G, Young LC, Hendzel MJ, Mer G, Sixma TK, Richard S",
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    {
        "title": "Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.",
        "journal": "The Journal of biological chemistry",
        "date": "2012",
        "authors": "Campbell SJ, Edwards RA, Leung CC, Neculai D, Hodge CD, Dhe-Paganon S, Glover JN",
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                "uniprot_canonical_ac": "O96028-1",
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                "uniprot_canonical_ac": "P23527-1",
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    {
        "title": "Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1.",
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        "date": "2012",
        "authors": "Singh N, Basnet H, Wiltshire TD, Mohammad DH, Thompson JR, Heroux A, Botuyan MV, Yaffe MB, Couch FJ, Rosenfeld MG, Mer G",
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    {
        "title": "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling.",
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        "date": "2012",
        "authors": "Mattiroli F, Vissers JH, van Dijk WJ, Ikpa P, Citterio E, Vermeulen W, Marteijn JA, Sixma TK",
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    {
        "title": "53BP1 regulates DSB repair using Rif1 to control 5' end resection.",
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        "authors": "Escribano-Diaz C, Orthwein A, Fradet-Turcotte A, Xing M, Young JT, Tkac J, Cook MA, Rosebrock AP, Munro M, Canny MD, Xu D, Durocher D",
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                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
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                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
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                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
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                "end_pos": 1086,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 1104,
                "end_pos": 1104,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 1148,
                "end_pos": 1148,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 1171,
                "end_pos": 1171,
                "sequence_org": "T",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 1219,
                "end_pos": 1219,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 and A-1171.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 13,
                "end_pos": 13,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-25; A-29; A-105; A-166; A-176 and A-178.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23727112",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23727112"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 166,
                "end_pos": 166,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-176 and A-178.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23727112",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23727112"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 176,
                "end_pos": 176,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-178.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23727112",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23727112"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 178,
                "end_pos": 178,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-176.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23727112",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23727112"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 25,
                "end_pos": 25,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-29; A-105; A-166; A-176 and A-178.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23727112",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23727112"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
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                "end_pos": 29,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-105; A-166; A-176 and A-178.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23727112",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23727112"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 302,
                "end_pos": 302,
                "sequence_org": "T",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 437,
                "end_pos": 437,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 452,
                "end_pos": 452,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 523,
                "end_pos": 523,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 543,
                "end_pos": 543,
                "sequence_org": "T",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
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                "start_pos": 580,
                "end_pos": 580,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12888",
                        "url": "https://www.uniprot.org/uniprotkb/Q12888"
                    },
                    {
                        "database": "PubMed",
                        "id": "23345425",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23345425"
                    },
                    {
                        "database": "PubMed",
                        "id": "23333306",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/23333306"
                    }
                ],
                "uniprot_canonical_ac": "Q12888-1"
            },
            {
                "start_pos": 625,
                "end_pos": 625,
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        "authors": "Gomez-Herreros F, Romero-Granados R, Zeng Z, Alvarez-Quilon A, Quintero C, Ju L, Umans L, Vermeire L, Huylebroeck D, Caldecott KW, Cortes-Ledesma F",
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                "uniprot_canonical_ac": "P23527-1",
                "protein_name": "Histone H2B type 1-O",
                "gene_name": "H2BC17",
                "tax_name": "Human"
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                "tax_name": "Human"
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                "tax_name": "Human"
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                "uniprot_canonical_ac": "Q99879-1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "Q15819-1",
                "protein_name": "Ubiquitin-conjugating enzyme E2 variant 2",
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                "tax_name": "Human"
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                "tax_name": "Human"
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                "uniprot_canonical_ac": "Q96SD1-1",
                "protein_name": "Protein artemis",
                "gene_name": "DCLRE1C",
                "tax_name": "Human"
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                "uniprot_canonical_ac": "Q9H9Q4-1",
                "protein_name": "Non-homologous end-joining factor 1",
                "gene_name": "NHEJ1",
                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "O95714-1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "P06899-1",
                "protein_name": "Histone H2B type 1-J",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "P57053-1",
                "protein_name": "Histone H2B type F-S",
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                "tax_name": "Human"
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                "uniprot_canonical_ac": "Q8N257-1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "Q99877-1",
                "protein_name": "Histone H2B type 1-N",
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                "tax_name": "Human"
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                "uniprot_canonical_ac": "Q99880-1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "P38398-1",
                "protein_name": "Breast cancer type 1 susceptibility protein",
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                "tax_name": "Human"
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                "uniprot_canonical_ac": "Q13315-1",
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                "name": "Homo sapiens",
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            {
                "start_pos": 176,
                "end_pos": 176,
                "sequence_org": "S",
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                "comment": "In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-178.",
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                "start_pos": 178,
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    {
        "title": "Phosphorylation of Tip60 Tyrosine 327 by Abl Kinase Inhibits HAT Activity through Association with FE65.",
        "journal": "The open biochemistry journal",
        "date": "2013",
        "authors": "Shin SH, Kang SS",
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                "kinase_uniprot_canonical_ac": "",
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                "residue": "Tyr",
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        "title": "Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation.",
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        "title": "The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase.",
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        "authors": "Leber R, Wise TW, Mizuta R, Meek K",
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        "title": "Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis.",
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