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Loss of glycine hydroxymethyltransferase activity; when associated with A-82 and F-83. Does not affect location at nucleus; when associated with A-82 and F-83. Reduces the proliferation rate of almost 60% after 48h; when associated with A-82 and F-83. Reduces the cytoplasmic incorporation of SHMT1-derived one-carbon units into methionine synthesis; when associated with F-82 and F-83. Enhances the nucleus incorporation of SHMT1-derived one-carbon units into de novo thymidylate synthesis; when associated with F-82 and F-83.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" }, { "database": "PubMed", "id": "22235121", "url": "https://pubmed.ncbi.nlm.nih.gov/22235121" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 82, "end_pos": 82, "sequence_org": "Y", "sequence_mut": "A", "comment": "Does not affect protein homotetramerization; when associated with F-83 and Q-257. Loss of glycine hydroxymethyltransferase activity; when associated with F-83 and Q-257. Does not affect location at nucleus; when associated with F-83 and Q-257. Reduces the proliferation rate of almost 60% after 48h; when associated with F-83 and Q-257. Reduces the cytoplasmic incorporation of SHMT1-derived one-carbon units into methionine synthesis; when associated with F-83 and Q-257. Enhances the nucleus incorporation of SHMT1-derived one-carbon units into de novo thymidylate synthesis; when associated with F-83 and Q-257.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" }, { "database": "PubMed", "id": "22235121", "url": "https://pubmed.ncbi.nlm.nih.gov/22235121" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 83, "end_pos": 83, "sequence_org": "Y", "sequence_mut": "F", "comment": "Does not affect protein homotetramerization; when associated with A-82 and Q-257. Loss of glycine hydroxymethyltransferase activity; when associated with A-82 and Q-257. Does not affect location at nucleus; when associated with A-82 and Q-257. Reduces the proliferation rate of almost 60% after 48h; when associated with A-82 and Q-257. Reduces the cytoplasmic incorporation of SHMT1-derived one-carbon units into methionine synthesis; when associated with F-82 and Q-257. Enhances the nucleus incorporation of SHMT1-derived one-carbon units into de novo thymidylate synthesis; when associated with F-82 and Q-257.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "22235121", "url": "https://pubmed.ncbi.nlm.nih.gov/22235121" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" } ], "record_id": "pubmed.22235121", "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 }, { 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"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": "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde.", "journal": "The Journal of biological chemistry", "date": "1989", "authors": "Kurys G, Ambroziak W, Pietruszko R", "reference": { "type": "PubMed", "id": "2925663", "url": "https://pubmed.ncbi.nlm.nih.gov/2925663" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P49189-1", "protein_name": "4-trimethylaminobutyraldehyde dehydrogenase", "gene_name": "ALDH9A1", "tax_name": "Human" }, { "uniprot_canonical_ac": "O75936-1", "protein_name": "Gamma-butyrobetaine dioxygenase", "gene_name": "BBOX1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NVH6-1", "protein_name": "Trimethyllysine dioxygenase, mitochondrial", "gene_name": "TMLHE", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.2925663", "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": "The catalytic activity of serine hydroxymethyltransferase is essential for de\u00a0novo nuclear dTMP synthesis in lung cancer cells.", "journal": "The FEBS journal", "date": "2018-09", "authors": "Giardina Giorgio, Paone Alessio, Tramonti Angela, Lucchi Roberta, Marani Marina, Magnifico Maria Chiara, Bouzidi Amani, Pontecorvi Valentino, Guiducci Giulia, Zamparelli Carlotta, Rinaldo Serena, Paiardini Alessandro, Contestabile Roberto, Cutruzzol\u00e0 Francesca", "reference": { "type": "PubMed", "id": "30035852", "url": "https://pubmed.ncbi.nlm.nih.gov/30035852" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.30035852", "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 }, { 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"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": "Kinetic and structural analysis of human ALDH9A1.", "journal": "Bioscience reports", "date": "2019", "authors": "Koncitikova R, Vigouroux A, Kopecna M, Sebela M, Morera S, Kopecny D", "reference": { "type": "PubMed", "id": "30914451", "url": "https://pubmed.ncbi.nlm.nih.gov/30914451" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P49189-1", "protein_name": "4-trimethylaminobutyraldehyde dehydrogenase", "gene_name": "ALDH9A1", "tax_name": "Human" }, { "uniprot_canonical_ac": "O75936-1", "protein_name": "Gamma-butyrobetaine dioxygenase", "gene_name": "BBOX1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NVH6-1", "protein_name": "Trimethyllysine dioxygenase, mitochondrial", "gene_name": "TMLHE", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.30914451", "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": "Affinity purification and characterization of serine hydroxymethyltransferases from rat liver.", "journal": "Journal of biochemistry", "date": "1987", "authors": "Masuda T, Sakamoto M, Nishizaki I, Hayashi H, Yamamoto M, Wada H", "reference": { "type": "PubMed", "id": "3110140", "url": "https://pubmed.ncbi.nlm.nih.gov/3110140" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P49189-1", "protein_name": "4-trimethylaminobutyraldehyde dehydrogenase", "gene_name": "ALDH9A1", "tax_name": "Human" }, { "uniprot_canonical_ac": "O75936-1", "protein_name": "Gamma-butyrobetaine dioxygenase", "gene_name": "BBOX1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NVH6-1", "protein_name": "Trimethyllysine dioxygenase, mitochondrial", "gene_name": "TMLHE", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.3110140", "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": "Serine hydroxymethyltransferase 1 promotes low-grade glioma progression by activating mTORC1 signaling.", "journal": "Neurological research", "date": "2022-11-23", "authors": "Gao Ye, Jing Nianliang, Teng Xukun, Wang Yong", "reference": { "type": "PubMed", "id": "36417280", "url": "https://pubmed.ncbi.nlm.nih.gov/36417280" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.36417280", "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": "One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse.", "journal": "Nature communications", "date": "2024-04-13", "authors": "Malatesta Marco, Fornasier Emanuele, Di Salvo Martino Luigi, Tramonti Angela, Zangelmi Erika, Peracchi Alessio, Secchi Andrea, Polverini Eugenia, Giachin Gabriele, Battistutta Roberto, Contestabile Roberto, Percudani Riccardo", "reference": { "type": "PubMed", "id": "38615009", "url": "https://pubmed.ncbi.nlm.nih.gov/38615009" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.38615009", "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": "Structure-based mechanism of riboregulation of the metabolic enzyme SHMT1.", "journal": "Molecular cell", "date": "2024-07-25", "authors": "Spizzichino Sharon, Di Fonzo Federica, Marabelli Chiara, Tramonti Angela, Chaves-Sanjuan Antonio, Parroni Alessia, Boumis Giovanna, Liberati Francesca Romana, Paone Alessio, Montemiglio Linda Celeste, Ardini Matteo, Jakobi Arjen J, Bharadwaj Alok, Swuec Paolo, Tartaglia Gian Gaetano, Paiardini Alessandro, Contestabile Roberto, Mai Antonello, Rotili Dante, Fiorentino Francesco, Macone Alberto, Giorgi Alessandra, Tria Giancarlo, Rinaldo Serena, Bolognesi Martino, Giardina Giorgio, Cutruzzol\u00e0 Francesca", "reference": { "type": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 135, "end_pos": 135, "sequence_org": "H", "sequence_mut": "N", "comment": "Does not affect protein homotetramerization; when associated with A-137 and N-168. Loss of protein homotetramerization; when associated with A-137. Slightly decreases pyridoxal-5'-phosphate binding; when associated with A-137 and N-168. Decreases pyridoxal-5'-phosphate binding; when associated with A-137. Loss of glycine hydroxymethyltransferase activity; when associated A-137. Does not affect location at nucleus; when associated with A-137 and N-168. Does not affect location at nucleus; when associated with A-137. Does not affect cell proliferation; when associated with A-137. Does not affect cell proliferation; when associated with A-137 and N-168.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 137, "end_pos": 137, "sequence_org": "R", "sequence_mut": "A", "comment": "Does not affect protein homotetramerization; when associated with N-135 and N-168. Loss of protein homotetramerization; when associated with N-135. Slightly decreases pyridoxal-5'-phosphate binding; when associated with N-135 and N-168. Decreases pyridoxal-5'-phosphate binding; when associated with N-135. Loss of glycine hydroxymethyltransferase activity; when associated with N-135. Does not affect location at nucleus; when associated with N-135 and N-168. Does not affect location at nucleus; when associated with N-135. Does not affect cell proliferation; when associated with N-135. Does not affect cell proliferation; when associated with N-135 and N-168.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 168, "end_pos": 168, "sequence_org": "E", "sequence_mut": "N", "comment": "Does not affect protein homotetramerization; when associated with N-135 and A-137. Slightly decreases pyridoxal-5'-phosphate binding; when associated with A-135 and A-137. Does not affect location at nucleus; when associated with A-135 and A-137.Does not affect cell proliferation rate of almost 60% after 48h; when associated with A-137. Does not affect cell proliferation; when associated with N-135. Does not affect cell proliferation; when associated with N-135 and N-168.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 257, "end_pos": 257, "sequence_org": "K", "sequence_mut": "Q", "comment": "Does not affect protein homotetramerization; when associated with A-82 and F-83. Loss of glycine hydroxymethyltransferase activity; when associated with A-82 and F-83. Does not affect location at nucleus; when associated with A-82 and F-83. Reduces the proliferation rate of almost 60% after 48h; when associated with A-82 and F-83. Reduces the cytoplasmic incorporation of SHMT1-derived one-carbon units into methionine synthesis; when associated with F-82 and F-83. Enhances the nucleus incorporation of SHMT1-derived one-carbon units into de novo thymidylate synthesis; when associated with F-82 and F-83.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" }, { "database": "PubMed", "id": "22235121", "url": "https://pubmed.ncbi.nlm.nih.gov/22235121" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 279, "end_pos": 279, "sequence_org": "K", "sequence_mut": "S", "comment": "Loss of RNA binding. Decreases ability of RNA to interfere with folate binding. Significantly impairs the ability of RNA to inhibit serine hydroxymethyltransferase activity. Decreases serine hydroxymethyltransferase activity. Does not affect SHMT2 protein expression.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 282, "end_pos": 282, "sequence_org": "K", "sequence_mut": "S", "comment": "Decreases RNA binding. Decreases ability of RNA to interfere with folate binding. Decreases the ability of RNA to inhibit serine hydroxymethyltransferase activity. Decreases serine hydroxymethyltransferase activity.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 393, "end_pos": 393, "sequence_org": "R", "sequence_mut": "S", "comment": "Decreases RNA binding; when associated with S-397. Decreases ability of RNA to interfere with folate binding; when associated with S-397. Decreases the ability of RNA to inhibit serine hydroxymethyltransferase activity; when associated with S-397. Decreases serine hydroxymethyltransferase activity; when associated with S-397.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 397, "end_pos": 397, "sequence_org": "R", "sequence_mut": "S", "comment": "Decreases RNA binding; when associated with S-393. Decreases ability of RNA to interfere with folate binding; when associated with S-393. Decreases the ability of RNA to inhibit serine hydroxymethyltransferase activity; when associated with S-393. Decreases serine hydroxymethyltransferase activity; when associated with S-393.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 82, "end_pos": 82, "sequence_org": "Y", "sequence_mut": "A", "comment": "Does not affect protein homotetramerization; when associated with F-83 and Q-257. Loss of glycine hydroxymethyltransferase activity; when associated with F-83 and Q-257. Does not affect location at nucleus; when associated with F-83 and Q-257. Reduces the proliferation rate of almost 60% after 48h; when associated with F-83 and Q-257. Reduces the cytoplasmic incorporation of SHMT1-derived one-carbon units into methionine synthesis; when associated with F-83 and Q-257. Enhances the nucleus incorporation of SHMT1-derived one-carbon units into de novo thymidylate synthesis; when associated with F-83 and Q-257.", "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" }, { "database": "PubMed", "id": "38996576", "url": "https://pubmed.ncbi.nlm.nih.gov/38996576" }, { "database": "PubMed", "id": "22235121", "url": "https://pubmed.ncbi.nlm.nih.gov/22235121" } ], "uniprot_canonical_ac": "P34896-1" }, { "start_pos": 83, "end_pos": 83, "sequence_org": "Y", "sequence_mut": "F", "comment": "Does not affect protein homotetramerization; when associated with A-82 and Q-257. Loss of glycine hydroxymethyltransferase activity; when associated with A-82 and Q-257. Does not affect location at nucleus; when associated with A-82 and Q-257. Reduces the proliferation rate of almost 60% after 48h; when associated with A-82 and Q-257. Reduces the cytoplasmic incorporation of SHMT1-derived one-carbon units into methionine synthesis; when associated with F-82 and Q-257. 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Soc. Trans.", "date": "1997", "authors": "Chave K J, Snell K, Sanders P G", "reference": { "type": "PubMed", "id": "9056951", "url": "https://pubmed.ncbi.nlm.nih.gov/9056951" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P34896-1", "protein_name": "Serine hydroxymethyltransferase, cytosolic", "gene_name": "SHMT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P34896", "url": "https://www.uniprot.org/uniprotkb/P34896" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.9056951", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": 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Wnt/\u03b2-catenin Signaling Pathway.", "journal": "International journal of biological sciences", "date": "2022", "authors": "Zhang Junchang, Wang Han, Wu Jing, Yuan Cheng, Chen Songyao, Liu Shuhao, Huo Mingyu, Zhang Changhua, He Yulong", "reference": { "type": "PubMed", "id": "36439876", "url": "https://pubmed.ncbi.nlm.nih.gov/36439876" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q10472-1", "protein_name": "Polypeptide N-acetylgalactosaminyltransferase 1", "gene_name": "GALNT1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q10472", "url": "https://www.uniprot.org/uniprotkb/Q10472" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.36439876", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": 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