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ETO-2 (MTG16) interactions with nuclear receptor corepressor, an effect that impairs granulocyte differentiation.", "journal": "Cancer research", "date": "2004", "authors": "Ibanez V, Sharma A, Buonamici S, Verma A, Kalakonda S, Wang J, Kadkol S, Saunthararajah Y", "reference": { "type": "PubMed", "id": "15231665", "url": "https://pubmed.ncbi.nlm.nih.gov/15231665" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O54972-1", "protein_name": "Transcriptional corepressor CBFA2T3", "gene_name": "Cbfa2t3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O75081-1", "protein_name": "Transcriptional corepressor CBFA2T3", "gene_name": "CBFA2T3", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "O54972", "url": "https://www.uniprot.org/uniprotkb/O54972" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.15231665", 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Iborra FJ, Rodriguez P, Strouboulis J, Enver T, Vyas P, Porcher C", "reference": { "type": "PubMed", "id": "16287841", "url": "https://pubmed.ncbi.nlm.nih.gov/16287841" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O54972-1", "protein_name": "Transcriptional corepressor CBFA2T3", "gene_name": "Cbfa2t3", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "O54972", "url": "https://www.uniprot.org/uniprotkb/O54972" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.16287841", "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", 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"species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8C3P7", "url": "https://www.uniprot.org/uniprotkb/Q8C3P7" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.28809392", "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": 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Neurogenesis by m6A Methylation.", "journal": "Cell", "date": "2017-11-02", "authors": "Yoon Ki-Jun, Ringeling Francisca Rojas, Vissers Caroline, Jacob Fadi, Pokrass Michael, Jimenez-Cyrus Dennisse, Su Yijing, Kim Nam-Shik, Zhu Yunhua, Zheng Lily, Kim Sunghan, Wang Xinyuan, Dor\u00e9 Louis C, Jin Peng, Regot Sergi, Zhuang Xiaoxi, Canzar Stefan, He Chuan, Ming Guo-Li, Song Hongjun", "reference": { "type": "PubMed", "id": "28965759", "url": "https://pubmed.ncbi.nlm.nih.gov/28965759" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8C3P7-1", "protein_name": "N(6)-adenosine-methyltransferase catalytic subunit METTL3", "gene_name": "Mettl3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q3UIK4-1", "protein_name": "N(6)-adenosine-methyltransferase non-catalytic subunit METTL14", "gene_name": "Mettl14", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8C3P7", "url": 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expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis.", "journal": "European journal of immunology", "date": "2002", "authors": "Rongvaux A, Shea RJ, Mulks MH, Gigot D, Urbain J, Leo O, Andris F", "reference": { "type": "PubMed", "id": "12555668", "url": "https://pubmed.ncbi.nlm.nih.gov/12555668" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q99KQ4-1", "protein_name": "Nicotinamide phosphoribosyltransferase", "gene_name": "Nampt", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q99KQ4", "url": "https://www.uniprot.org/uniprotkb/Q99KQ4" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.12555668", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], 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Gastrointestinal and liver physiology", "date": "2004", "authors": "DiMagno MJ, Williams JA, Hao Y, Ernst SA, Owyang C", "reference": { "type": "PubMed", "id": "14962849", "url": "https://pubmed.ncbi.nlm.nih.gov/14962849" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P60324-1", "protein_name": "Nanos homolog 3", "gene_name": "Nanos3", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P60324", "url": "https://www.uniprot.org/uniprotkb/P60324" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.14962849", "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" ] }, { 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"Suzuki Hitomi, Tsuda Masayuki, Kiso Makoto, Saga Yumiko", "reference": { "type": "PubMed", "id": "18436203", "url": "https://pubmed.ncbi.nlm.nih.gov/18436203" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P60324-1", "protein_name": "Nanos homolog 3", "gene_name": "Nanos3", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P60324", "url": "https://www.uniprot.org/uniprotkb/P60324" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.18436203", "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": 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Mol. Genet.", "date": "2011", "authors": "Julaton VT, Reijo Pera RA", "reference": { "type": "PubMed", "id": "21421998", "url": "https://pubmed.ncbi.nlm.nih.gov/21421998" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P60324-1", "protein_name": "Nanos homolog 3", "gene_name": "Nanos3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P60323-1", "protein_name": "Nanos homolog 3", "gene_name": "NANOS3", "tax_name": "Human" }, { "uniprot_canonical_ac": "O75626-1", "protein_name": "PR domain zinc finger protein 1", "gene_name": "PRDM1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q6W0C5-1", "protein_name": "Developmental pluripotency-associated protein 3", "gene_name": "DPPA3", "tax_name": "Human" }, { "uniprot_canonical_ac": "P60321-1", "protein_name": "Nanos homolog 2", "gene_name": "NANOS2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NQI0-1", "protein_name": "Probable ATP-dependent RNA helicase DDX4", "gene_name": "DDX4", "tax_name": "Human" 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Montag D, Schachner M", "reference": { "type": "PubMed", "id": "10103075", "url": "https://pubmed.ncbi.nlm.nih.gov/10103075" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P70232-1", "protein_name": "Neural cell adhesion molecule L1-like protein", "gene_name": "Chl1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P70232", "url": "https://www.uniprot.org/uniprotkb/P70232" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.10103075", "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", 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"authors": "Holm J, Hillenbrand R, Steuber V, Bartsch U, Moos M, Lubbert H, Montag D, Schachner M", "reference": { "type": "PubMed", "id": "8921253", "url": "https://pubmed.ncbi.nlm.nih.gov/8921253" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P70232-1", "protein_name": "Neural cell adhesion molecule L1-like protein", "gene_name": "Chl1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q90479-1", "protein_name": "Neural cell adhesion molecule L1.2", "gene_name": "l1cama; nadl1.2", "tax_name": "Zebrafish" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P70232", "url": "https://www.uniprot.org/uniprotkb/P70232" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.8921253", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": 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"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": "MNADK, a novel liver-enriched mitochondrion-localized NAD kinase.", "journal": "Biology open", "date": "2013", "authors": "Zhang R", "reference": { "type": "PubMed", "id": "23616928", "url": "https://pubmed.ncbi.nlm.nih.gov/23616928" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8C5H8-1", "protein_name": "NAD kinase 2, mitochondrial", 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major metabolic regulator upon increased energy demand.", "journal": "Molecular metabolism", "date": "2022", "authors": "Kim H, Fu Z, Yang Z, Song Z, Shamsa EH, Yumnamcha T, Sun S, Liu W, Ibrahim AS, Qi NR, Zhang R, Zhang K", "reference": { "type": "PubMed", "id": "35944895", "url": "https://pubmed.ncbi.nlm.nih.gov/35944895" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8C5H8-1", "protein_name": "NAD kinase 2, mitochondrial", "gene_name": "Nadk2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q4G0N4-1", "protein_name": "NAD kinase 2, mitochondrial", "gene_name": "NADK2", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8C5H8", "url": "https://www.uniprot.org/uniprotkb/Q8C5H8" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.35944895", "abstract": "", "glycosylation": [], "mutagenesis": [], 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Pan Jingying, Yang Riyun, Mao Liming, Bao Jingyin", "reference": { "type": "PubMed", "id": "36631013", "url": "https://pubmed.ncbi.nlm.nih.gov/36631013" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8C5H8-1", "protein_name": "NAD kinase 2, mitochondrial", "gene_name": "Nadk2", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8C5H8", "url": "https://www.uniprot.org/uniprotkb/Q8C5H8" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.36631013", "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": 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Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-239 and A-260.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" }, { "database": "PubMed", "id": "27010430", "url": "https://pubmed.ncbi.nlm.nih.gov/27010430" }, { "database": "PubMed", "id": "25026077", "url": "https://pubmed.ncbi.nlm.nih.gov/25026077" } ], "uniprot_canonical_ac": "Q4VGL6-1" }, { "start_pos": 239, "end_pos": 239, "sequence_org": "K", "sequence_mut": "A", "comment": "Strongly decreases CDE and ADERNA-binding. Increases target-mRNA expression. Abolishes CDERNA-binding and highly increases target-mRNA expression; when associated with A-260. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-220 and A-260.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" }, { "database": "PubMed", "id": "27010430", "url": "https://pubmed.ncbi.nlm.nih.gov/27010430" }, { "database": "PubMed", "id": "25026077", "url": "https://pubmed.ncbi.nlm.nih.gov/25026077" } ], "uniprot_canonical_ac": "Q4VGL6-1" }, { "start_pos": 260, "end_pos": 260, "sequence_org": "R", "sequence_mut": "A", "comment": "Strongly decreases CDE and ADERNA-binding. Increases target-mRNA expression. Abolishes CDERNA-binding and highly increases target-mRNA expression; when associated with A-239. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-220 and A-239.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" }, { "database": "PubMed", "id": "27010430", "url": "https://pubmed.ncbi.nlm.nih.gov/27010430" }, { "database": "PubMed", "id": "25026077", "url": "https://pubmed.ncbi.nlm.nih.gov/25026077" } ], "uniprot_canonical_ac": "Q4VGL6-1" }, { "start_pos": 488, "end_pos": 488, "sequence_org": "R", "sequence_mut": "G", "comment": "No effect on cleavage.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" } ], "uniprot_canonical_ac": "Q4VGL6-1" }, { "start_pos": 510, "end_pos": 510, "sequence_org": "R", "sequence_mut": "G", "comment": "Abolishes the formation of a preferential cleavage product. Abolishes protein cleavage; when associated with G-579.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" } ], "uniprot_canonical_ac": "Q4VGL6-1" }, { "start_pos": 560, "end_pos": 560, "sequence_org": "R", "sequence_mut": "G", "comment": "No effect on cleavage.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" } ], "uniprot_canonical_ac": "Q4VGL6-1" }, { "start_pos": 579, "end_pos": 579, "sequence_org": "R", "sequence_mut": "G", "comment": "Abolishes the formation of an alternative cleavage product. Abolishes protein cleavage; when associated with G-510.", "evidence": [ { "database": "UniProtKB", "id": "Q4VGL6", "url": "https://www.uniprot.org/uniprotkb/Q4VGL6" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" } ], "uniprot_canonical_ac": "Q4VGL6-1" } ], "record_id": "pubmed.25282160", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 6 } ], "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": "Transcription factors STAT6 and KLF4 implement macrophage polarization via the dual catalytic powers of MCPIP.", "journal": "Journal of immunology (Baltimore, Md. : 1950)", "date": "2015", "authors": "Kapoor N, Niu J, Saad Y, Kumar S, Sirakova T, Becerra E, Li X, Kolattukudy PE", "reference": { "type": "PubMed", "id": "25934862", "url": "https://pubmed.ncbi.nlm.nih.gov/25934862" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q5D1E7-1", "protein_name": "Endoribonuclease ZC3H12A", "gene_name": "Zc3h12a", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q5D1E7", "url": "https://www.uniprot.org/uniprotkb/Q5D1E7" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 141, "end_pos": 141, "sequence_org": "D", "sequence_mut": "N", "comment": "Loss of RNase activity. Loss of mRNAs and miRNAs degradation. Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activation. Inhibits induction of angiogenesis and macrophage M2 polarization. Mislocalized in stress granule (SG). Loss of the ability to inhibit SG formation under stress. Does not inhibit binding to IL6 mRNA. Increases ICOS surface expression.", "evidence": [ { "database": "UniProtKB", "id": "Q5D1E7", "url": "https://www.uniprot.org/uniprotkb/Q5D1E7" }, { "database": "PubMed", "id": "25934862", "url": "https://pubmed.ncbi.nlm.nih.gov/25934862" }, { "database": "PubMed", "id": "21115689", "url": "https://pubmed.ncbi.nlm.nih.gov/21115689" }, { "database": "PubMed", "id": "23706741", "url": "https://pubmed.ncbi.nlm.nih.gov/23706741" }, { "database": "PubMed", "id": "26000482", "url": "https://pubmed.ncbi.nlm.nih.gov/26000482" }, { "database": "PubMed", "id": "19322177", "url": "https://pubmed.ncbi.nlm.nih.gov/19322177" }, { "database": "PubMed", "id": "21971051", "url": "https://pubmed.ncbi.nlm.nih.gov/21971051" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" } ], "uniprot_canonical_ac": "Q5D1E7-1" } ], "record_id": "pubmed.25934862", "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": "Regnase-1 and Roquin Regulate a Common Element in Inflammatory mRNAs by Spatiotemporally Distinct Mechanisms.", "journal": "Cell", "date": "2015", "authors": "Mino T, Murakawa Y, Fukao A, Vandenbon A, Wessels HH, Ori D, Uehata T, Tartey S, Akira S, Suzuki Y, Vinuesa CG, Ohler U, Standley DM, Landthaler M, Fujiwara T, Takeuchi O", "reference": { "type": "PubMed", "id": "26000482", "url": "https://pubmed.ncbi.nlm.nih.gov/26000482" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q5D1E7-1", "protein_name": "Endoribonuclease ZC3H12A", "gene_name": "Zc3h12a", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q4VGL6-1", "protein_name": "Roquin-1", "gene_name": "Rc3h1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q92900-1", "protein_name": "Regulator of nonsense transcripts 1", "gene_name": "UPF1", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q5D1E7", "url": "https://www.uniprot.org/uniprotkb/Q5D1E7" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 141, "end_pos": 141, "sequence_org": "D", "sequence_mut": "N", "comment": "Loss of RNase activity. Loss of mRNAs and miRNAs degradation. Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activation. Inhibits induction of angiogenesis and macrophage M2 polarization. Mislocalized in stress granule (SG). Loss of the ability to inhibit SG formation under stress. Does not inhibit binding to IL6 mRNA. Increases ICOS surface expression.", "evidence": [ { "database": "UniProtKB", "id": "Q5D1E7", "url": "https://www.uniprot.org/uniprotkb/Q5D1E7" }, { "database": "PubMed", "id": "25934862", "url": "https://pubmed.ncbi.nlm.nih.gov/25934862" }, { "database": "PubMed", "id": "21115689", "url": "https://pubmed.ncbi.nlm.nih.gov/21115689" }, { "database": "PubMed", "id": "23706741", "url": "https://pubmed.ncbi.nlm.nih.gov/23706741" }, { "database": "PubMed", "id": "26000482", "url": "https://pubmed.ncbi.nlm.nih.gov/26000482" }, { "database": "PubMed", "id": "19322177", "url": "https://pubmed.ncbi.nlm.nih.gov/19322177" }, { "database": "PubMed", "id": "21971051", "url": "https://pubmed.ncbi.nlm.nih.gov/21971051" }, { "database": "PubMed", "id": "25282160", "url": "https://pubmed.ncbi.nlm.nih.gov/25282160" } ], "uniprot_canonical_ac": "Q5D1E7-1" }, { "start_pos": 647, "end_pos": 648, "sequence_org": "DE", "sequence_mut": "AA", "comment": "Loss of ATPase activity and helicase activity. Inhibits ZC3H12A-mediated IL6 mRNA degradation.", "evidence": [ { "database": "UniProtKB", "id": "Q92900", "url": "https://www.uniprot.org/uniprotkb/Q92900" }, { "database": "PubMed", "id": "26000482", "url": "https://pubmed.ncbi.nlm.nih.gov/26000482" }, { "database": "PubMed", "id": "17159905", "url": "https://pubmed.ncbi.nlm.nih.gov/17159905" }, { "database": "PubMed", "id": "10999600", "url": "https://pubmed.ncbi.nlm.nih.gov/10999600" } ], "uniprot_canonical_ac": "Q92900-1" } ], "record_id": "pubmed.26000482", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 3 } ], "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": "MCPIP1 endoribonuclease activity negatively regulates interleukin-17-mediated signaling and inflammation.", "journal": "Immunity", "date": "2015", "authors": "Garg AV, Amatya N, Chen K, Cruz JA, Grover P, Whibley N, Conti HR, Hernandez Mir G, Sirakova T, Childs EC, Smithgall TE, Biswas PS, Kolls JK, McGeachy MJ, Kolattukudy PE, Gaffen SL", "reference": { "type": "PubMed", "id": "26320658", "url": "https://pubmed.ncbi.nlm.nih.gov/26320658" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q5D1E7-1", "protein_name": "Endoribonuclease ZC3H12A", "gene_name": "Zc3h12a", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q5D1E8-1", "protein_name": "Endoribonuclease ZC3H12A", "gene_name": "ZC3H12A", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q5D1E7", "url": "https://www.uniprot.org/uniprotkb/Q5D1E7" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 141, "end_pos": 141, "sequence_org": "D", "sequence_mut": "N", "comment": "Loss of pre-miRNARNase activity. Attenuates strongly miRNA silencing activity. Loss of interleukin IL17A and IL6 mRNA instabilities. Reduces angiogenic differentiation. Loss of RNase activity on JEV and DEN viral RNAs and antiviral effects. Loss of HIV-1 antiviral activity. Loss of IL1B mRNA instability; when associated with A-226.", "evidence": [ { "database": "UniProtKB", "id": "Q5D1E8", "url": "https://www.uniprot.org/uniprotkb/Q5D1E8" }, { "database": "PubMed", "id": "24191027", "url": "https://pubmed.ncbi.nlm.nih.gov/24191027" }, { "database": "PubMed", "id": "26320658", "url": "https://pubmed.ncbi.nlm.nih.gov/26320658" }, { "database": "PubMed", "id": "23355615", "url": "https://pubmed.ncbi.nlm.nih.gov/23355615" }, { "database": "PubMed", "id": "19909337", "url": "https://pubmed.ncbi.nlm.nih.gov/19909337" }, { "database": "PubMed", "id": "22055188", "url": "https://pubmed.ncbi.nlm.nih.gov/22055188" }, { "database": "PubMed", "id": "26134560", "url": "https://pubmed.ncbi.nlm.nih.gov/26134560" } ], "uniprot_canonical_ac": "Q5D1E8-1" }, { "start_pos": 225, "end_pos": 225, "sequence_org": "D", "sequence_mut": "A", "comment": "Loss of pre-miRNARNase activity, IL17A mRNA instability and antiviral effects; when associated with A-226.", "evidence": [ { "database": "UniProtKB", "id": "Q5D1E8", "url": "https://www.uniprot.org/uniprotkb/Q5D1E8" }, { "database": "PubMed", "id": "24191027", "url": "https://pubmed.ncbi.nlm.nih.gov/24191027" }, { "database": "PubMed", "id": "26320658", "url": "https://pubmed.ncbi.nlm.nih.gov/26320658" }, { "database": "PubMed", "id": "23355615", "url": "https://pubmed.ncbi.nlm.nih.gov/23355615" } ], "uniprot_canonical_ac": "Q5D1E8-1" }, { "start_pos": 226, "end_pos": 226, "sequence_org": "D", "sequence_mut": "A", "comment": "Loss of pre-miRNARNase activity, IL17A mRNA instability and antiviral effects; when associated with A-225. Loss of IL1B mRNA instability; when associated with N-141.", "evidence": [ { "database": "UniProtKB", "id": "Q5D1E8", "url": "https://www.uniprot.org/uniprotkb/Q5D1E8" }, { "database": "PubMed", "id": "24191027", "url": "https://pubmed.ncbi.nlm.nih.gov/24191027" }, { "database": "PubMed", "id": "26320658", "url": "https://pubmed.ncbi.nlm.nih.gov/26320658" }, { "database": "PubMed", "id": "23355615", "url": "https://pubmed.ncbi.nlm.nih.gov/23355615" }, { "database": "PubMed", "id": "19909337", "url": "https://pubmed.ncbi.nlm.nih.gov/19909337" } ], "uniprot_canonical_ac": "Q5D1E8-1" }, { "start_pos": 306, "end_pos": 306, "sequence_org": "C", "sequence_mut": "R", "comment": "Loss of interleukin IL17A mRNA instability. Reduces weakly pre-miRNARNase activity. Attenuates miRNA silencing activity. Does not inhibit binding to Japanese encephalitis virus (JEV) and dengue virus (DEN) RNAs and weakly attenuates antiviral effects. 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"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": "Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor devoid of ornithine and arginine decarboxylating activity.", "journal": "The Journal of biological chemistry", "date": "2006", "authors": "Lopez-Contreras AJ, Lopez-Garcia C, Jimenez-Cervantes C, Cremades A, Penafiel R", "reference": { "type": "PubMed", "id": "16916800", "url": "https://pubmed.ncbi.nlm.nih.gov/16916800" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R109-1", "protein_name": "Ornithine decarboxylase antizyme 3", "gene_name": "Oaz3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O08608-1", "protein_name": "Ornithine decarboxylase antizyme 2", "gene_name": "Oaz2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P54369-1", "protein_name": "Ornithine decarboxylase antizyme 1", "gene_name": "Oaz1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8BVM4-1", "protein_name": "Antizyme inhibitor 2", "gene_name": "Azin2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O35484-1", "protein_name": "Antizyme inhibitor 1", "gene_name": "Azin1", "tax_name": "Mouse" } ], "species": [ { 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"count": 0 } ], "sort_fields": [] } ] }, { "title": "ODCp, a brain- and testis-specific ornithine decarboxylase paralogue, functions as an antizyme inhibitor, although less efficiently than AzI1.", "journal": "The Biochemical journal", "date": "2008", "authors": "Snapir Z, Keren-Paz A, Bercovich Z, Kahana C", "reference": { "type": "PubMed", "id": "18062773", "url": "https://pubmed.ncbi.nlm.nih.gov/18062773" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R109-1", "protein_name": "Ornithine decarboxylase antizyme 3", "gene_name": "Oaz3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P54369-1", "protein_name": "Ornithine decarboxylase antizyme 1", "gene_name": "Oaz1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8BVM4-1", "protein_name": "Antizyme inhibitor 2", "gene_name": "Azin2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O35484-1", "protein_name": "Antizyme inhibitor 1", "gene_name": "Azin1", "tax_name": "Mouse" } ], "species": [ { 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"count": 0 } ], "sort_fields": [] } ] }, { "title": "Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in mammalian cells.", "journal": "The Journal of biological chemistry", "date": "2008", "authors": "Lopez-Contreras AJ, Ramos-Molina B, Cremades A, Penafiel R", "reference": { "type": "PubMed", "id": "18508777", "url": "https://pubmed.ncbi.nlm.nih.gov/18508777" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R109-1", "protein_name": "Ornithine decarboxylase antizyme 3", "gene_name": "Oaz3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O08608-1", "protein_name": "Ornithine decarboxylase antizyme 2", "gene_name": "Oaz2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P54369-1", "protein_name": "Ornithine decarboxylase antizyme 1", "gene_name": "Oaz1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8BVM4-1", "protein_name": "Antizyme inhibitor 2", "gene_name": "Azin2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O35484-1", 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"count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests a role in spermiogenesis.", "journal": "The international journal of biochemistry & cell biology", "date": "2009-05", "authors": "L\u00f3pez-Contreras Andr\u00e9s J, Ramos-Molina Bruno, Mart\u00ednez-de-la-Torre Margaret, Pe\u00f1afiel-Verd\u00fa Cristina, Puelles Luis, Cremades Asunci\u00f3n, Pe\u00f1afiel Rafael", "reference": { "type": "PubMed", "id": "18973822", "url": "https://pubmed.ncbi.nlm.nih.gov/18973822" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9R109-1", "protein_name": "Ornithine decarboxylase antizyme 3", "gene_name": "Oaz3", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P00860-1", "protein_name": "Ornithine decarboxylase", "gene_name": "Odc1", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "Q8BVM4-1", "protein_name": "Antizyme inhibitor 2", "gene_name": "Azin2", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "O35484-1", "protein_name": "Antizyme inhibitor 1", "gene_name": "Azin1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9R109", "url": "https://www.uniprot.org/uniprotkb/Q9R109" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.18973822", "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 }, 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