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A", "date": "2020", "authors": "Ragamin Avi\u00ebl, Yigit G\u00f6khan, Bousset Kristine, Beleggia Filippo, Verheijen Frans W, de Wit Marie-Claire Y, Strom Tim M, D\u00f6rk Thilo, Wollnik Bernd, Mancini Grazia M S", "reference": { "type": "PubMed", "id": "32212377", "url": "https://pubmed.ncbi.nlm.nih.gov/32212377" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92878-1", "protein_name": "DNA repair protein RAD50", "gene_name": "RAD50", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q92878", "url": "https://www.uniprot.org/uniprotkb/Q92878" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.32212377", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", 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}, { "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": "Bone Marrow Failure and Immunodeficiency Associated with Human RAD50 Variants.", "journal": "Journal of clinical immunology", "date": "2023-11", "authors": "Takagi Masatoshi, Hoshino Akihiro, Bousset Kristine, R\u00f6ddecke Jule, Martin Hanna Luisa, Folcut Iulia, Tomomasa Dan, Yang Xi, Kobayashi Junya, Sakata Naoki, Yoshida Kenichi, Miyano Satoru, Ogawa Seishi, Kojima Seiji, Morio Tomohiro, D\u00f6rk Thilo, Kanegane Hirokazu", "reference": { "type": "PubMed", "id": "37794136", "url": "https://pubmed.ncbi.nlm.nih.gov/37794136" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q92878-1", "protein_name": "DNA repair protein RAD50", "gene_name": "RAD50", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q92878", "url": "https://www.uniprot.org/uniprotkb/Q92878" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.37794136", "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", "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": 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"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": "Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2.", "journal": "Gene", "date": "1999", "authors": "Afshar G, Murnane J P", "reference": { "type": "PubMed", "id": "10393250", "url": "https://pubmed.ncbi.nlm.nih.gov/10393250" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8IXJ6-1", "protein_name": "NAD-dependent protein deacetylase sirtuin-2", "gene_name": "SIRT2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.10393250", "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", "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": "A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast.", "journal": "EMBO J.", "date": "2001", "authors": "Perrod S, Cockell M M, Laroche T, Renauld H, Ducrest A L, Bonnard C, Gasser S M", "reference": { "type": "PubMed", "id": "11226170", "url": "https://pubmed.ncbi.nlm.nih.gov/11226170" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8IXJ6-1", "protein_name": "NAD-dependent protein deacetylase sirtuin-2", "gene_name": "SIRT2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P53686-1", "protein_name": "NAD-dependent protein deacetylase HST2", "gene_name": "HST2", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": 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"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": "Structure of the histone deacetylase SIRT2.", "journal": "Nature structural biology", "date": "2001", "authors": "Finnin MS, Donigian JR, Pavletich NP", "reference": { 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Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-168 and A-187.", "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" }, { "database": "PubMed", "id": "11427894", "url": "https://pubmed.ncbi.nlm.nih.gov/11427894" }, { "database": "PubMed", "id": "16909107", "url": "https://pubmed.ncbi.nlm.nih.gov/16909107" } ], "uniprot_canonical_ac": "Q8IXJ6-1" }, { "start_pos": 168, "end_pos": 168, "sequence_org": "N", "sequence_mut": "A", "comment": "Abolishes deacetylation of alpha-tubulin. Inhibits deacetylation of histone H3 at 'Lys-18'. 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No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. Strongly reduced activity toward long-chain fatty acyl groups.", "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" }, { "database": "PubMed", "id": "24681946", "url": "https://pubmed.ncbi.nlm.nih.gov/24681946" }, { "database": "PubMed", "id": "17516032", "url": "https://pubmed.ncbi.nlm.nih.gov/17516032" }, { "database": "PubMed", "id": "10381378", "url": "https://pubmed.ncbi.nlm.nih.gov/10381378" }, { "database": "PubMed", "id": "17726514", "url": "https://pubmed.ncbi.nlm.nih.gov/17726514" }, { "database": "PubMed", "id": "22014574", "url": "https://pubmed.ncbi.nlm.nih.gov/22014574" }, { "database": "PubMed", "id": "11427894", "url": "https://pubmed.ncbi.nlm.nih.gov/11427894" }, { "database": "PubMed", "id": "16909107", "url": "https://pubmed.ncbi.nlm.nih.gov/16909107" }, { "database": "PubMed", "id": "27512957", "url": "https://pubmed.ncbi.nlm.nih.gov/27512957" }, { "database": "PubMed", "id": "12620231", "url": "https://pubmed.ncbi.nlm.nih.gov/12620231" }, { "database": "PubMed", "id": "29239724", "url": "https://pubmed.ncbi.nlm.nih.gov/29239724" }, { "database": "PubMed", "id": "11812793", "url": "https://pubmed.ncbi.nlm.nih.gov/11812793" }, { "database": "PubMed", "id": "17488717", "url": "https://pubmed.ncbi.nlm.nih.gov/17488717" }, { "database": "PubMed", "id": "12697818", "url": "https://pubmed.ncbi.nlm.nih.gov/12697818" } ], "uniprot_canonical_ac": "Q8IXJ6-1" }, { "start_pos": 187, "end_pos": 187, "sequence_org": "H", "sequence_mut": "Y", "comment": "Inhibits deacetylase activity toward histone, alpha-tubulin, FZR1 and CDC20. No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. Strongly reduced activity toward long-chain fatty acyl groups.", "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" }, { "database": "PubMed", "id": "24681946", "url": "https://pubmed.ncbi.nlm.nih.gov/24681946" }, { "database": "PubMed", "id": "17516032", "url": "https://pubmed.ncbi.nlm.nih.gov/17516032" }, { "database": "PubMed", "id": "10381378", "url": "https://pubmed.ncbi.nlm.nih.gov/10381378" }, { "database": "PubMed", "id": "17726514", "url": "https://pubmed.ncbi.nlm.nih.gov/17726514" }, { "database": "PubMed", "id": "22014574", "url": "https://pubmed.ncbi.nlm.nih.gov/22014574" }, { "database": "PubMed", "id": "11427894", "url": "https://pubmed.ncbi.nlm.nih.gov/11427894" }, { "database": "PubMed", "id": "16909107", "url": "https://pubmed.ncbi.nlm.nih.gov/16909107" }, { "database": "PubMed", "id": "27512957", "url": "https://pubmed.ncbi.nlm.nih.gov/27512957" }, { "database": "PubMed", "id": "12620231", "url": "https://pubmed.ncbi.nlm.nih.gov/12620231" }, { "database": "PubMed", "id": "29239724", "url": "https://pubmed.ncbi.nlm.nih.gov/29239724" }, { "database": "PubMed", "id": "11812793", "url": "https://pubmed.ncbi.nlm.nih.gov/11812793" }, { "database": "PubMed", "id": "17488717", "url": "https://pubmed.ncbi.nlm.nih.gov/17488717" }, { "database": "PubMed", "id": "12697818", "url": "https://pubmed.ncbi.nlm.nih.gov/12697818" } ], "uniprot_canonical_ac": "Q8IXJ6-1" }, { "start_pos": 97, "end_pos": 97, "sequence_org": "R", "sequence_mut": "A", "comment": "No effect on deacetylase activity.", "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" }, { "database": "PubMed", "id": "11427894", "url": "https://pubmed.ncbi.nlm.nih.gov/11427894" } ], "uniprot_canonical_ac": "Q8IXJ6-1" } ], "record_id": "pubmed.11427894", "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": "Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening.", "journal": "J. Biol. Chem.", "date": "2001", "authors": "Grozinger C M, Chao E D, Blackwell H E, Moazed D, Schreiber S L", "reference": { "type": "PubMed", "id": "11483616", "url": "https://pubmed.ncbi.nlm.nih.gov/11483616" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8IXJ6-1", "protein_name": "NAD-dependent protein deacetylase sirtuin-2", "gene_name": "SIRT2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.11483616", "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", "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": "Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases.", "journal": "The Journal of biological chemistry", "date": "2002", "authors": "Borra MT, O'Neill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR, Denu JM", "reference": { "type": "PubMed", "id": "11812793", "url": "https://pubmed.ncbi.nlm.nih.gov/11812793" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8IXJ6-1", "protein_name": "NAD-dependent protein deacetylase sirtuin-2", "gene_name": "SIRT2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 187, "end_pos": 187, "sequence_org": "H", "sequence_mut": "A", "comment": "Inhibits deacetylase activity toward histone, alpha-tubulin, FZR1 and CDC20. No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. 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No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. 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Biophys. Res. Commun.", "date": "2003", "authors": "Hiratsuka Masaharu, Inoue Toshiaki, Toda Tosifusa, Kimura Narimichi, Shirayoshi Yasuaki, Kamitani Hideki, Watanabe Takashi, Ohama Eisaku, Tahimic Candice G T, Kurimasa Akihiro, Oshimura Mitsuo", "reference": { "type": "PubMed", "id": "12963026", "url": "https://pubmed.ncbi.nlm.nih.gov/12963026" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8IXJ6-1", "protein_name": "NAD-dependent protein deacetylase sirtuin-2", "gene_name": "SIRT2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.12963026", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", 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