[ { "title": "Short-interfering-RNA-mediated gene silencing in mammalian cells requires Dicer and eIF2C translation initiation factors.", "journal": "Curr. Biol.", "date": "2003", "authors": "Doi N, Zenno S, Ueda R, Ohki-Hamazaki H, Ui-Tei K, Saigo K", "reference": { "type": "PubMed", "id": "12526743", "url": "https://pubmed.ncbi.nlm.nih.gov/12526743" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8CJG0-1", "protein_name": "Protein argonaute-2", "gene_name": "Ago2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8CJF9-1", "protein_name": "Protein argonaute-3", "gene_name": "Ago3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8R418-1", "protein_name": "Endoribonuclease Dicer", "gene_name": "Dicer1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8CJG1-1", "protein_name": "Protein argonaute-1", "gene_name": "Ago1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8CJF8-1", "protein_name": "Protein argonaute-4", "gene_name": "Ago4", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8CJG0", "url": 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Biol. Chem.", "date": "2002", "authors": "Furusawa Makoto, Taira Takahiro, Iguchi-Ariga Sanae M M, Ariga Hiroyoshi", "reference": { "type": "PubMed", "id": "12414807", "url": "https://pubmed.ncbi.nlm.nih.gov/12414807" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9DBR0-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "Akap8", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9DBR0", "url": "https://www.uniprot.org/uniprotkb/Q9DBR0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.12414807", "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 novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95.", "journal": "Biochem. J.", "date": "2004", "authors": "Arsenijevic T, Degraef C, Dumont JE, Roger PP, Pirson I", "reference": { "type": "PubMed", "id": "14641107", "url": "https://pubmed.ncbi.nlm.nih.gov/14641107" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9DBR0-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "Akap8", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O43823-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "AKAP8", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9DBR0", "url": "https://www.uniprot.org/uniprotkb/Q9DBR0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.14641107", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 2 } ], "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-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association.", "journal": "Mol. Cell. Biol.", "date": "2005", "authors": "Kamada S, Kikkawa U, Tsujimoto Y, Hunter T", "reference": { "type": "PubMed", "id": "16227597", "url": "https://pubmed.ncbi.nlm.nih.gov/16227597" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9DBR0-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "Akap8", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O43823-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "AKAP8", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9DBR0", "url": "https://www.uniprot.org/uniprotkb/Q9DBR0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 290, "end_pos": 290, "sequence_org": "R", "sequence_mut": "S", "comment": "No nuclear localization; when associated with 304-N-S-305.", "evidence": [ { "database": "UniProtKB", "id": "O43823", "url": "https://www.uniprot.org/uniprotkb/O43823" }, { "database": "PubMed", "id": "16227597", "url": "https://pubmed.ncbi.nlm.nih.gov/16227597" } ], "uniprot_canonical_ac": "O43823-1" }, { "start_pos": 304, "end_pos": 305, "sequence_org": "KR", "sequence_mut": "NS", "comment": "No nuclear localization; when associated with S-290.", "evidence": [ { "database": "UniProtKB", "id": "O43823", "url": "https://www.uniprot.org/uniprotkb/O43823" }, { "database": "PubMed", "id": "16227597", "url": "https://pubmed.ncbi.nlm.nih.gov/16227597" } ], "uniprot_canonical_ac": "O43823-1" } ], "record_id": "pubmed.16227597", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 2 } ], "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": "Interaction between fidgetin and protein kinase A-anchoring protein AKAP95 is critical for palatogenesis in the mouse.", "journal": "J. Biol. Chem.", "date": "2006", "authors": "Yang Yan, Mahaffey Connie L, B\u00e9rub\u00e9 Nathalie, Frankel Wayne N", "reference": { "type": "PubMed", "id": "16751186", "url": "https://pubmed.ncbi.nlm.nih.gov/16751186" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9DBR0-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "Akap8", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q9ERZ6-1", "protein_name": "Fidgetin", "gene_name": "Fign", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9DBR0", "url": "https://www.uniprot.org/uniprotkb/Q9DBR0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.16751186", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 2 } ], "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": "Suppression of LPS-induced TNF-alpha production in macrophages by cAMP is mediated by PKA-AKAP95-p105.", "journal": "Sci. Signal.", "date": "2009", "authors": "Wall EA, Zavzavadjian JR, Chang MS, Randhawa B, Zhu X, Hsueh RC, Liu J, Driver A, Bao XR, Sternweis PC, Simon MI, Fraser ID", "reference": { "type": "PubMed", "id": "19531803", "url": "https://pubmed.ncbi.nlm.nih.gov/19531803" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9DBR0-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "Akap8", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9DBR0", "url": "https://www.uniprot.org/uniprotkb/Q9DBR0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.19531803", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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"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": "DNA methylation, histone modifications and behaviour of AKAP95 during mouse oocyte growth and upon nuclear transfer of foreign chromatin into fully grown prophase oocytes.", "journal": "Folia biologica", "date": "2012", "authors": "Hoffmann S, Tomasik G, Polanski Z", "reference": { "type": "PubMed", "id": "23342911", "url": "https://pubmed.ncbi.nlm.nih.gov/23342911" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9DBR0-1", "protein_name": "A-kinase anchor protein 8", "gene_name": "Akap8", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9DBR0", "url": "https://www.uniprot.org/uniprotkb/Q9DBR0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.23342911", "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 }, { 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Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-316; A-462 and A-463.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 316, "end_pos": 316, "sequence_org": "S", "sequence_mut": "A", "comment": "Decreases insulin-induced phosphorylation by approximately 30%. 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"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": 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"mutagenesis": [ { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced acetylation and transcriptional activity increased by about 1.5 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-245 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-245; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-245; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced acetylation and transcriptional activity increased by about 1.5-fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 253, "end_pos": 253, "sequence_org": "S", "sequence_mut": "A", "comment": "Abolishes insulin-induced phosphorylation when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-316; A-462 and A-463.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "R", "comment": "Significant reduction in acetylation and transcriptional activity increased by about 2.0 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-245. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" } ], "phosphorylation": [ { "start_pos": 253, "end_pos": 253, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine; by PKB/AKT1 and SGK1", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "iPTMnet", "id": "Q9R1E0", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q9R1E0" }, { "database": "PubMed", "id": "22532369", "url": "https://pubmed.ncbi.nlm.nih.gov/22532369" }, { "database": "PubMed", "id": "23705021", "url": "https://pubmed.ncbi.nlm.nih.gov/23705021" }, { "database": "PubMed", "id": "24116102", "url": "https://pubmed.ncbi.nlm.nih.gov/24116102" }, { "database": "PubMed", "id": "28270438", "url": "https://pubmed.ncbi.nlm.nih.gov/28270438" }, { "database": "PubMed", "id": "28644433", "url": "https://pubmed.ncbi.nlm.nih.gov/28644433" }, { "database": "PubMed", "id": "30014903", "url": "https://pubmed.ncbi.nlm.nih.gov/30014903" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "18388859", "url": "https://pubmed.ncbi.nlm.nih.gov/18388859" }, { "database": "PubMed", "id": "19965929", "url": "https://pubmed.ncbi.nlm.nih.gov/19965929" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" }, { "database": "PubMed", "id": "27827363", "url": "https://pubmed.ncbi.nlm.nih.gov/27827363" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" } ], "site_lbl": "Ser253", "uniprot_canonical_ac": "Q9R1E0-1" } ], "record_id": "pubmed.16076959", "abstract": "", "glycosylation": [], "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": 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"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": "The LXXLL motif of murine forkhead transcription factor FoxO1 mediates Sirt1-dependent transcriptional activity.", "journal": "The Journal of clinical investigation", "date": "2006", "authors": "Nakae J, Cao Y, Daitoku H, Fukamizu A, Ogawa W, Yano Y, Hayashi Y", "reference": { "type": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R1E0-1", "protein_name": "Forkhead box protein O1", "gene_name": "Foxo1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 24, "end_pos": 24, "sequence_org": "T", "sequence_mut": "A", "comment": "Decreases insulin-induced phosphorylation by approximately 30%. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-253; A-316; A-462 and A-463. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with Q-219; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with R-219; R-242; R-245; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 253, "end_pos": 253, "sequence_org": "S", "sequence_mut": "A", "comment": "Abolishes insulin-induced phosphorylation when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-316; A-462 and A-463.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 316, "end_pos": 316, "sequence_org": "S", "sequence_mut": "A", "comment": "Decreases insulin-induced phosphorylation by approximately 30%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-462 and A-463.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 462, "end_pos": 462, "sequence_org": "L", "sequence_mut": "A", "comment": "Decreased transcriptional activity by about 2-fold in the absence of serum; when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-316 and A-463.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 463, "end_pos": 463, "sequence_org": "L", "sequence_mut": "A", "comment": "Decreased transcriptional activity by about 2-fold in the absence of serum; when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-316 and A-462.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" } ], "uniprot_canonical_ac": "Q9R1E0-1" } ], "record_id": "pubmed.16917544", "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": "Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complex.", "journal": "Genes Dev.", "date": "2006", "authors": "Cooper Marcus P, Qu Lishu, Rohas Lindsay M, Lin Jiandie, Yang Wenli, Erdjument-Bromage Hediye, Tempst Paul, Spiegelman Bruce M", "reference": { "type": "PubMed", "id": "17050673", "url": "https://pubmed.ncbi.nlm.nih.gov/17050673" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R1E0-1", "protein_name": "Forkhead box protein O1", "gene_name": "Foxo1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P42704-1", "protein_name": "Leucine-rich PPR motif-containing protein, mitochondrial", "gene_name": "LRPPRC", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UBK2-1", "protein_name": "Peroxisome proliferator-activated receptor gamma coactivator 1-alpha", "gene_name": "PPARGC1A", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q6PB66-1", "protein_name": "Leucine-rich PPR motif-containing protein, mitochondrial", "gene_name": "Lrpprc", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.17050673", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 4 } ], "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": "SIRT1 regulates adiponectin gene expression through Foxo1-C/enhancer-binding protein alpha transcriptional complex.", "journal": "The Journal of biological chemistry", "date": "2006", "authors": "Qiao L, Shao J", "reference": { "type": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R1E0-1", "protein_name": "Forkhead box protein O1", "gene_name": "Foxo1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P53566-1", "protein_name": "CCAAT/enhancer-binding protein alpha", "gene_name": "Cebpa", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced acetylation and transcriptional activity increased by about 1.5 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-245 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-245; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-245; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced acetylation and transcriptional activity increased by about 1.5-fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "R", "comment": "Significant reduction in acetylation and transcriptional activity increased by about 2.0 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-245. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" } ], "record_id": "pubmed.17090532", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { 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"glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 2 } ], "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": "Uncoupling of acetylation from phosphorylation regulates FoxO1 function independent of its subcellular localization.", "journal": "The Journal of biological chemistry", "date": "2010", "authors": "Qiang L, Banks AS, Accili D", "reference": { "type": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R1E0-1", "protein_name": "Forkhead box protein O1", "gene_name": "Foxo1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 219, "end_pos": 219, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 219, "end_pos": 219, "sequence_org": "K", "sequence_mut": "R", "comment": "Translocates to the cytoplasm after insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-242; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-242; R-245; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 242, "end_pos": 242, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced acetylation and transcriptional activity increased by about 1.5 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-245 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-245; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-245; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 245, "end_pos": 245, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced acetylation and transcriptional activity increased by about 1.5-fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 24, "end_pos": 24, "sequence_org": "T", "sequence_mut": "A", "comment": "Decreases insulin-induced phosphorylation by approximately 30%. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-253; A-316; A-462 and A-463. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with Q-219; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with R-219; R-242; R-245; R-259; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 253, "end_pos": 253, "sequence_org": "S", "sequence_mut": "A", "comment": "Abolishes insulin-induced phosphorylation when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-316; A-462 and A-463.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "10347145", "url": "https://pubmed.ncbi.nlm.nih.gov/10347145" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "16917544", "url": "https://pubmed.ncbi.nlm.nih.gov/16917544" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 259, "end_pos": 259, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-262; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 259, "end_pos": 259, "sequence_org": "K", "sequence_mut": "R", "comment": "Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-262; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "A", "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 262, "end_pos": 262, "sequence_org": "K", "sequence_mut": "R", "comment": "Significant reduction in acetylation and transcriptional activity increased by about 2.0 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-245. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-271 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "15220471", "url": "https://pubmed.ncbi.nlm.nih.gov/15220471" }, { "database": "PubMed", "id": "16076959", "url": "https://pubmed.ncbi.nlm.nih.gov/16076959" }, { "database": "PubMed", "id": "17090532", "url": "https://pubmed.ncbi.nlm.nih.gov/17090532" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 271, "end_pos": 271, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 271, "end_pos": 271, "sequence_org": "K", "sequence_mut": "R", "comment": "Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-291.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 291, "end_pos": 291, "sequence_org": "K", "sequence_mut": "Q", "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24: Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" }, { "start_pos": 291, "end_pos": 291, "sequence_org": "K", "sequence_mut": "R", "comment": "Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-271. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-271. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-271.", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "PubMed", "id": "22510882", "url": "https://pubmed.ncbi.nlm.nih.gov/22510882" }, { "database": "PubMed", "id": "20519497", "url": "https://pubmed.ncbi.nlm.nih.gov/20519497" } ], "uniprot_canonical_ac": "Q9R1E0-1" } ], "phosphorylation": [ { "start_pos": 24, "end_pos": 24, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Thr", "comment": "Phosphothreonine; by PKB/AKT1 or PKB/AKT2 and SGK1", "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" }, { "database": "iPTMnet", "id": "Q9R1E0", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q9R1E0" }, { "database": "PubMed", "id": "24466179", "url": 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Med.", "date": "2011", "authors": "Zhou Yingjiang, Lee Justin, Reno Candace M, Sun Cheng, Park Sang Won, Chung Jason, Lee Jaemin, Fisher Simon J, White Morris F, Biddinger Sudha B, Ozcan Umut", "reference": { "type": "PubMed", "id": "21317886", "url": "https://pubmed.ncbi.nlm.nih.gov/21317886" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R1E0-1", "protein_name": "Forkhead box protein O1", "gene_name": "Foxo1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O35426-1", "protein_name": "X-box-binding protein 1", "gene_name": "Xbp1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9R1E0", "url": "https://www.uniprot.org/uniprotkb/Q9R1E0" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.21317886", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": 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[] } ] }, { "title": "Increased leukocyte survival and accelerated onset of lymphoma in the absence of MCL-1 S159-phosphorylation.", "journal": "Oncogene", "date": "2014", "authors": "Lindner SE, Wissler M, Grunder A, Aumann K, Ottina E, Peintner L, Brauns-Schubert P, Preiss F, Herzog S, Borner C, Charvet C, Villunger A, Pahl HL, Maurer U", "reference": { "type": "PubMed", "id": "24213575", "url": "https://pubmed.ncbi.nlm.nih.gov/24213575" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P97287-1", "protein_name": "Induced myeloid leukemia cell differentiation protein Mcl-1 homolog", "gene_name": "Mcl1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P97287", "url": "https://www.uniprot.org/uniprotkb/P97287" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "phosphorylation": [ { "start_pos": 159, "end_pos": 159, 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suppress the growth of ovarian cancer cells.", "journal": "Oncotarget", "date": "2016", "authors": "Li B, Li X, Ni Z, Zhang Y, Zeng Y, Yan X, Huang Y, He J, Lyu X, Wu Y, Wang Y, Zheng Y, He F", "reference": { "type": "PubMed", "id": "27449090", "url": "https://pubmed.ncbi.nlm.nih.gov/27449090" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P97287-1", "protein_name": "Induced myeloid leukemia cell differentiation protein Mcl-1 homolog", "gene_name": "Mcl1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P97287", "url": "https://www.uniprot.org/uniprotkb/P97287" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "phosphorylation": [ { "start_pos": 159, "end_pos": 159, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "P97287", "url": 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"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": 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Biophys. 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