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Strongly reduced methylation; when associated with K-1401.", "evidence": [ { "database": "UniProtKB", "id": "Q12888", "url": "https://www.uniprot.org/uniprotkb/Q12888" }, { "database": "PubMed", "id": "16294047", "url": "https://pubmed.ncbi.nlm.nih.gov/16294047" }, { "database": "PubMed", "id": "16294045", "url": "https://pubmed.ncbi.nlm.nih.gov/16294045" } ], "uniprot_canonical_ac": "Q12888-1" }, { "start_pos": 1401, "end_pos": 1401, "sequence_org": "R", "sequence_mut": "A", "comment": "No detectable effect on methylation by PRMT1 (in vitro). 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nucleosomal kinase required for the assembly of 53BP1 foci in response to ionizing radiation-induced DNA damage.", "journal": "The Journal of biological chemistry", "date": "2012", "authors": "Sanz-Garcia M, Monsalve DM, Sevilla A, Lazo PA", "reference": { "type": "PubMed", "id": "22621922", "url": "https://pubmed.ncbi.nlm.nih.gov/22621922" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q12888-1", "protein_name": "TP53-binding protein 1", "gene_name": "TP53BP1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q12888", "url": "https://www.uniprot.org/uniprotkb/Q12888" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "phosphorylation": [ { "start_pos": 1219, "end_pos": 1219, "kinase_uniprot_canonical_ac": "Q13315-1", "kinase_gene_name": "ATM", "residue": "Ser", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "Q12888", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q12888" }, { "database": "PubMed", "id": "22621922", "url": "https://pubmed.ncbi.nlm.nih.gov/22621922" } ], "site_lbl": "Ser1219", "uniprot_canonical_ac": "Q12888-1" }, { "start_pos": 302, "end_pos": 302, "kinase_uniprot_canonical_ac": "Q13315-1", "kinase_gene_name": "ATM", "residue": "Thr", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "Q12888", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q12888" }, { "database": "PubMed", "id": "22621922", "url": "https://pubmed.ncbi.nlm.nih.gov/22621922" } ], "site_lbl": "Thr302", "uniprot_canonical_ac": "Q12888-1" }, { "start_pos": 831, "end_pos": 831, "kinase_uniprot_canonical_ac": "Q13315-1", "kinase_gene_name": "ATM", "residue": "Ser", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "Q12888", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q12888" }, { "database": "PubMed", "id": "22621922", "url": "https://pubmed.ncbi.nlm.nih.gov/22621922" } ], "site_lbl": "Ser831", "uniprot_canonical_ac": "Q12888-1" } ], "record_id": "pubmed.22621922", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 3 }, { "field": "total_sites", "count": 3 } ], "sort_fields": [ "start_pos", "end_pos", "kinase_uniprot_canonical_ac", "kinase_gene_name", "residue", "comment", "site_lbl", "uniprot_canonical_ac" ] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Role of 53BP1 oligomerization in regulating double-strand break repair.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2013", "authors": "Lottersberger F, Bothmer A, Robbiani DF, Nussenzweig MC, de Lange T", "reference": { "type": "PubMed", "id": "23345425", "url": "https://pubmed.ncbi.nlm.nih.gov/23345425" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q12888-1", "protein_name": "TP53-binding protein 1", "gene_name": "TP53BP1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q12888", "url": "https://www.uniprot.org/uniprotkb/Q12888" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 105, "end_pos": 105, "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-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-29; 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": 1068, "end_pos": 1068, "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-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": 1086, "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": 1398, "end_pos": 1401, "sequence_org": "RGRR", "sequence_mut": "AGAA", "comment": "No effect on in class-switch recombination (CSR).", "evidence": [ { "database": "UniProtKB", "id": "Q12888", "url": "https://www.uniprot.org/uniprotkb/Q12888" }, { "database": "PubMed", "id": "23345425", "url": "https://pubmed.ncbi.nlm.nih.gov/23345425" } ], "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": 1521, "end_pos": 1521, "sequence_org": "D", "sequence_mut": "R", "comment": "Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR).", "evidence": [ { "database": "UniProtKB", "id": "Q12888", "url": "https://www.uniprot.org/uniprotkb/Q12888" }, { "database": "PubMed", "id": "17190600", "url": "https://pubmed.ncbi.nlm.nih.gov/17190600" }, { "database": "PubMed", "id": "23345425", "url": "https://pubmed.ncbi.nlm.nih.gov/23345425" }, { "database": "PubMed", "id": "23760478", "url": "https://pubmed.ncbi.nlm.nih.gov/23760478" }, { "database": "PubMed", "id": "15525939", "url": "https://pubmed.ncbi.nlm.nih.gov/15525939" } ], "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" }, { "start_pos": 29, "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" }, { "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, "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-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": 674, "end_pos": 674, "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-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": 696, "end_pos": 696, "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-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": 698, "end_pos": 698, "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-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": 6, "end_pos": 6, "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-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; 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-13; 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": 784, "end_pos": 784, "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-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": 831, "end_pos": 831, "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-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.", "evidence": [ { "database": "UniProtKB", "id": "Q12888", "url": 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"https://pubmed.ncbi.nlm.nih.gov/23333306" } ], "uniprot_canonical_ac": "Q12888-1" }, { "start_pos": 892, "end_pos": 892, "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-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" } ], "record_id": "pubmed.23345425", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.", "journal": "Nature", "date": "2013", "authors": "Fradet-Turcotte A, Canny MD, Escribano-Diaz C, Orthwein A, Leung CC, Huang H, Landry MC, Kitevski-LeBlanc J, Noordermeer SM, Sicheri F, Durocher D", "reference": { "type": "PubMed", "id": "23760478", "url": 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GABAA receptor (GABRG3: rs208129) and RELN (rs73670) genes to autism spectrum disorder among peadiatric Iraqi Arabs.", "journal": "Molecular biology reports", "date": "2022", "authors": "Ali ZA, Yasseen AA, McAllister KA, Al-Dujailli A, Al-Karaqully AJ, Jumaah AS", "reference": { "type": "PubMed", "id": "35403940", "url": "https://pubmed.ncbi.nlm.nih.gov/35403940" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q99928-1", "protein_name": "Gamma-aminobutyric acid receptor subunit gamma-3", "gene_name": "GABRG3", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q99928", "url": "https://www.uniprot.org/uniprotkb/Q99928" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.35403940", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { 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[] } ] }, { "title": "Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity.", "journal": "Proc. 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S, Tysoe C, Noh G, Tarnopolsky M, Brady L, Zafar M, Schrier Vergano SA, Murray B, Sawyer L, Hainline BE, Sapp K, DeMarzo D, Huismann DJ, Wentzensen IM, Schnur RE, Monaghan KG, Juusola J, Rhodes L, Dobyns WB, Lecoquierre F, Goldenberg A, Polster T, Axer-Schaefer S, Platzer K, Klockner C, Hoffman TL, MacArthur DG, O'Leary MC, VanNoy GE, England E, Varghese VC, Mefford HC", "reference": { "type": "PubMed", "id": "33473207", "url": "https://pubmed.ncbi.nlm.nih.gov/33473207" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P63096-1", "protein_name": "Guanine nucleotide-binding protein G(i) subunit alpha-1", "gene_name": "GNAI1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P63096", "url": "https://www.uniprot.org/uniprotkb/P63096" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.33473207", "abstract": "", 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Genet.", "date": "1992", "authors": "del Castillo I, Cohen-Salmon M, Blanchard S, Lutfalla G, Petit C", "reference": { "type": "PubMed", "id": "1303284", "url": "https://pubmed.ncbi.nlm.nih.gov/1303284" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23352-1", "protein_name": "Anosmin-1", "gene_name": "ANOS1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23352", "url": "https://www.uniprot.org/uniprotkb/P23352" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.1303284", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": 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"table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "The product of X-linked Kallmann's syndrome gene (KAL1) affects the migratory activity of gonadotropin-releasing hormone (GnRH)-producing neurons.", "journal": "Human molecular genetics", "date": "2004", "authors": "Cariboni A, Pimpinelli F, Colamarino S, Zaninetti R, Piccolella M, Rumio C, Piva F, Rugarli EI, Maggi R", "reference": { "type": "PubMed", "id": "15471890", "url": "https://pubmed.ncbi.nlm.nih.gov/15471890" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23352-1", "protein_name": "Anosmin-1", "gene_name": "ANOS1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23352", "url": "https://www.uniprot.org/uniprotkb/P23352" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.15471890", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", 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"count": 0 } ], "sort_fields": [] } ] }, { "title": "Kallmann syndrome: 14 novel mutations in KAL1 and FGFR1 (KAL2).", "journal": "Human mutation", "date": "2005", "authors": "Albuisson J, Pecheux C, Carel JC, Lacombe D, Leheup B, Lapuzina P, Bouchard P, Legius E, Matthijs G, Wasniewska M, Delpech M, Young J, Hardelin JP, Dode C", "reference": { "type": "PubMed", "id": "15605412", "url": "https://pubmed.ncbi.nlm.nih.gov/15605412" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23352-1", "protein_name": "Anosmin-1", "gene_name": "ANOS1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P11362-1", "protein_name": "Fibroblast growth factor receptor 1", "gene_name": "FGFR1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23352", "url": "https://www.uniprot.org/uniprotkb/P23352" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } 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Mol. 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[] } ] }, { "title": "Clinical assessment and molecular analysis of GnRHR and KAL1 genes in males with idiopathic hypogonadotrophic hypogonadism.", "journal": "Clinical endocrinology", "date": "2007", "authors": "Versiani BR, Trarbach E, Koenigkam-Santos M, Dos Santos AC, Elias LL, Moreira AC, Latronico AC, de Castro M", "reference": { "type": "PubMed", "id": "17223984", "url": "https://pubmed.ncbi.nlm.nih.gov/17223984" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23352-1", "protein_name": "Anosmin-1", "gene_name": "ANOS1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23352", "url": "https://www.uniprot.org/uniprotkb/P23352" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.17223984", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], 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"o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Identification of two novel missense mutations in the KAL1 gene in Han Chinese subjects with Kallmann Syndrome.", "journal": "Journal of endocrinological investigation", "date": "2011", "authors": "Jap TS, Chiu CY, Lirng JF, Won GS", "reference": { "type": "PubMed", "id": "20530987", "url": "https://pubmed.ncbi.nlm.nih.gov/20530987" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23352-1", "protein_name": "Anosmin-1", "gene_name": "ANOS1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23352", "url": "https://www.uniprot.org/uniprotkb/P23352" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.20530987", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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"count": 0 } ], "sort_fields": [] } ] }, { "title": "A novel splice site variant in ANOS1 gene leads to Kallmann syndrome in three siblings.", "journal": "Gene", "date": "2020", "authors": "Jiang X, Li D, Gao Y, Zhang X, Wang X, Yang Y, Shen Y", "reference": { "type": "PubMed", "id": "31669640", "url": "https://pubmed.ncbi.nlm.nih.gov/31669640" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23352-1", "protein_name": "Anosmin-1", "gene_name": "ANOS1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23352", "url": "https://www.uniprot.org/uniprotkb/P23352" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.31669640", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": 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