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Strongly reduces interaction with JNM1.", "evidence": [ { "database": "UniProtKB", "id": "P38696", "url": "https://www.uniprot.org/uniprotkb/P38696" }, { "database": "PubMed", "id": "15975903", "url": "https://pubmed.ncbi.nlm.nih.gov/15975903" } ], "uniprot_canonical_ac": "P38696-1" }, { "start_pos": 326, "end_pos": 326, "sequence_org": "D", "sequence_mut": "A", "comment": "Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-328.", "evidence": [ { "database": "UniProtKB", "id": "P38696", "url": "https://www.uniprot.org/uniprotkb/P38696" }, { "database": "PubMed", "id": "16415535", "url": "https://pubmed.ncbi.nlm.nih.gov/16415535" }, { "database": "PubMed", "id": "15975903", "url": "https://pubmed.ncbi.nlm.nih.gov/15975903" } ], "uniprot_canonical_ac": "P38696-1" }, { "start_pos": 328, "end_pos": 328, "sequence_org": "E", "sequence_mut": "A", "comment": "Temperature-sensitive. Reduces nuclear migration in mitosis. 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J. 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"count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop.", "journal": "FEBS letters", "date": "2005-02-14", "authors": "W\u00e4chter Andrea, Schwappach Blanche", "reference": { "type": "PubMed", "id": "15710404", "url": "https://pubmed.ncbi.nlm.nih.gov/15710404" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37020-1", "protein_name": "Anion/proton exchange transporter GEF1", "gene_name": "GEF1", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37020", "url": "https://www.uniprot.org/uniprotkb/P37020" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.15710404", "abstract": "", 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Biol. Chem.", "date": "2006", "authors": "Metz Jutta, W\u00e4chter Andrea, Schmidt Bastian, Bujnicki Janusz M, Schwappach Blanche", "reference": { "type": "PubMed", "id": "16260785", "url": "https://pubmed.ncbi.nlm.nih.gov/16260785" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37020-1", "protein_name": "Anion/proton exchange transporter GEF1", "gene_name": "GEF1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "Q12154-1", "protein_name": "ATPase GET3", "gene_name": "GET3", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37020", "url": "https://www.uniprot.org/uniprotkb/P37020" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.16260785", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], 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Mol. Biol.", "date": "1994", "authors": "Huang M E, Chuat J C, Galibert F", "reference": { "type": "PubMed", "id": "7932715", "url": "https://pubmed.ncbi.nlm.nih.gov/7932715" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37020-1", "protein_name": "Anion/proton exchange transporter GEF1", "gene_name": "GEF1", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37020", "url": "https://www.uniprot.org/uniprotkb/P37020" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.7932715", "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", 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Saccharomyces cerevisiae encodes a bifunctional enzyme.", "journal": "Yeast (Chichester, England)", "date": "1993-06", "authors": "Edman J C, Goldstein A L, Erbe J G", "reference": { "type": "PubMed", "id": "8346682", "url": "https://pubmed.ncbi.nlm.nih.gov/8346682" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37254-1", "protein_name": "Aminodeoxychorismate synthase", "gene_name": "ABZ1", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37254", "url": "https://www.uniprot.org/uniprotkb/P37254" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.8346682", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": 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], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.9509572", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 5 } ], "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": [] }, { 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"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": "Phosphorylation by casein kinase 2 regulates Nap1 localization and function.", "journal": "Mol. Cell. Biol.", "date": "2008", "authors": "Calvert Meredith E K, Keck Kristin M, Ptak Celeste, Shabanowitz Jeffrey, Hunt Donald F, Pemberton Lucy F", "reference": { "type": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37292-1", "protein_name": "Serine hydroxymethyltransferase, mitochondrial", "gene_name": "SHM1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P53848-1", "protein_name": "Folic acid synthesis protein FOL1", "gene_name": "FOL1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P53067-1", "protein_name": "Importin subunit beta-5", "gene_name": "KAP114", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "Q12692-1", "protein_name": "Histone H2A.Z", "gene_name": "HTZ1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P40210-1", "protein_name": "Protein SIP5", "gene_name": "SIP5", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P19454-1", "protein_name": "Casein kinase II subunit alpha'", "gene_name": "CKA2", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P20485-1", "protein_name": "Choline kinase", "gene_name": "CKI1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P25389-1", "protein_name": "Probable serine/threonine-protein kinase KCC4", "gene_name": "KCC4", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P53939-1", "protein_name": "Protein NIS1", "gene_name": "NIS1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P02294-1", "protein_name": "Histone H2B.2", "gene_name": "HTB2", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P02994-1", "protein_name": "Elongation factor 1-alpha", "gene_name": "TEF1; TEF2", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P04912-1", "protein_name": "Histone H2A.2", "gene_name": "HTA2", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P0CS90-1", "protein_name": "Import motor subunit, mitochondrial", "gene_name": "SSC1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P0CX49-1", "protein_name": "Large ribosomal subunit protein eL18A", "gene_name": "RPL18A", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P0CX50-1", "protein_name": "Large ribosomal subunit protein eL18B", "gene_name": "RPL18B", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P10591-1", "protein_name": "Heat shock protein SSA1", "gene_name": "SSA1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P10592-1", "protein_name": "Heat shock protein SSA2", "gene_name": "SSA2", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P11484-1", "protein_name": "Ribosome-associated molecular chaperone SSB1", "gene_name": "SSB1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P15108-1", "protein_name": "ATP-dependent molecular chaperone HSC82", "gene_name": "HSC82", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "P25293-1", "protein_name": "Nucleosome assembly protein", "gene_name": "NAP1", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "Q08229-1", "protein_name": "Protein NBA1", "gene_name": "NBA1", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37292", "url": "https://www.uniprot.org/uniprotkb/P37292" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "mutagenesis": [ { "start_pos": 159, "end_pos": 159, "sequence_org": "S", "sequence_mut": "A", "comment": "Significant reduction in phosphorylation; when associated with A-397. Complete inhibition of phosphorylation; when associated with A-177 and A-397. Leads to a prolonged S phase and a shortened passage through G1; when associated with A-177 and A-397. Predominantly cytoplasmic; when associated with S-99, A-177 and A-397.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": "https://www.uniprot.org/uniprotkb/P25293" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" } ], "uniprot_canonical_ac": "P25293-1" }, { "start_pos": 159, "end_pos": 159, "sequence_org": "S", "sequence_mut": "D", "comment": "Leads to a prolonged S phase and a shortened passage through G1; when associated with A-177 and A-397.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": "https://www.uniprot.org/uniprotkb/P25293" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" } ], "uniprot_canonical_ac": "P25293-1" }, { "start_pos": 177, "end_pos": 177, "sequence_org": "S", "sequence_mut": "A", "comment": "Significant reduction in phosphorylation; when associated with A-397. Complete inhibition of phosphorylation; when associated with A-159 and A-397. Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-397. Predominantly cytoplasmic; when associated with S-99, A-159 and A-397.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": "https://www.uniprot.org/uniprotkb/P25293" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" } ], "uniprot_canonical_ac": "P25293-1" }, { "start_pos": 177, "end_pos": 177, "sequence_org": "S", "sequence_mut": "D", "comment": "Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-397.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": "https://www.uniprot.org/uniprotkb/P25293" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" } ], "uniprot_canonical_ac": "P25293-1" }, { "start_pos": 397, "end_pos": 397, "sequence_org": "S", "sequence_mut": "A", "comment": "Significant reduction in phosphorylation; when associated with either A-159 or A-177. Complete inhibition of phosphorylation; when associated with A-159 and A-177. Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-177. Predominantly cytoplasmic; when associated with S-99; A-159 and A-177.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": "https://www.uniprot.org/uniprotkb/P25293" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" } ], "uniprot_canonical_ac": "P25293-1" }, { "start_pos": 397, "end_pos": 397, "sequence_org": "S", "sequence_mut": "D", "comment": "Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-177.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": "https://www.uniprot.org/uniprotkb/P25293" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" } ], "uniprot_canonical_ac": "P25293-1" }, { "start_pos": 99, "end_pos": 99, "sequence_org": "L", "sequence_mut": "S", "comment": "Predominantly cytoplasmic; when associated with A-159, A-177 and S-397.", "evidence": [ { "database": "UniProtKB", "id": "P25293", "url": 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"database": "PubMed", "id": "17330950", "url": "https://pubmed.ncbi.nlm.nih.gov/17330950" }, { "database": "PubMed", "id": "17563356", "url": "https://pubmed.ncbi.nlm.nih.gov/17563356" }, { "database": "PubMed", "id": "18086883", "url": "https://pubmed.ncbi.nlm.nih.gov/18086883" }, { "database": "PubMed", "id": "18407956", "url": "https://pubmed.ncbi.nlm.nih.gov/18407956" }, { "database": "PubMed", "id": "19684113", "url": "https://pubmed.ncbi.nlm.nih.gov/19684113" }, { "database": "PubMed", "id": "19779198", "url": "https://pubmed.ncbi.nlm.nih.gov/19779198" }, { "database": "PubMed", "id": "19795423", "url": "https://pubmed.ncbi.nlm.nih.gov/19795423" }, { "database": "PubMed", "id": "19823750", "url": "https://pubmed.ncbi.nlm.nih.gov/19823750" }, { "database": "PubMed", "id": "20489023", "url": "https://pubmed.ncbi.nlm.nih.gov/20489023" }, { "database": "PubMed", "id": "21126336", "url": "https://pubmed.ncbi.nlm.nih.gov/21126336" }, { "database": "PubMed", "id": "21177495", "url": 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Chem.", "date": "1994", "authors": "Bullis B L, Lemire B D", "reference": { "type": "PubMed", "id": "8120006", "url": "https://pubmed.ncbi.nlm.nih.gov/8120006" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37298-1", "protein_name": "Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial", "gene_name": "SDH4", "tax_name": "Baker's yeast" }, { "uniprot_canonical_ac": "Q00711-1", "protein_name": "Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial", "gene_name": "SDH1", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37298", "url": "https://www.uniprot.org/uniprotkb/P37298" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.8120006", "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": "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine -- expression of the gene in Escherichia coli and purification and characterization of the enzyme.", "journal": "Eur. 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Biochem.", "date": "1997", "authors": "Liu J Q, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H", "reference": { "type": "PubMed", "id": "9151955", "url": "https://pubmed.ncbi.nlm.nih.gov/9151955" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P37303-1", "protein_name": "Low specificity L-threonine aldolase", "gene_name": "GLY1", "tax_name": "Baker's yeast" } ], "species": [ { "name": "Saccharomyces cerevisiae S288C", "taxid": 559292, "evidence": [ { "database": "UniProtKB", "id": "P37303", "url": "https://www.uniprot.org/uniprotkb/P37303" } ], "common_name": "Baker's yeast", "glygen_name": "Yeast", "reference_species": "Saccharomyces cerevisiae S288C [559292]" } ], "record_id": "pubmed.9151955", "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": "Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: a key enzyme in glycine biosynthesis.", "journal": "FEMS Microbiol. 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], "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": "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II.", "journal": "Yeast", "date": "1995", "authors": "Obermaier B, Gassenhuber J, Piravandi E, Domdey H", "reference": { "type": "PubMed", "id": "7502586", "url": "https://pubmed.ncbi.nlm.nih.gov/7502586" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P38041-1", "protein_name": "BEM1-interacting protein 1", "gene_name": "BOI1", "tax_name": "Baker's yeast" }, { 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