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Pharmacol.", "date": "2011", "authors": "Yamamoto Naoko, Honma Masashi, Suzuki Hiroshi", "reference": { "type": "PubMed", "id": "21606217", "url": "https://pubmed.ncbi.nlm.nih.gov/21606217" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O94804-1", "protein_name": "Serine/threonine-protein kinase 10", "gene_name": "STK10", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O94804", "url": "https://www.uniprot.org/uniprotkb/O94804" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.21606217", "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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"count": 0 } ], "sort_fields": [] } ] }, { "title": "Mutation in the epsilon subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory neuropathy with spastic paraplegia.", "journal": "Journal of medical genetics", "date": "2006", "authors": "Bouhouche A, Benomar A, Bouslam N, Chkili T, Yahyaoui M", "reference": { "type": "PubMed", "id": "16399879", "url": "https://pubmed.ncbi.nlm.nih.gov/16399879" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P48643-1", "protein_name": "T-complex protein 1 subunit epsilon", "gene_name": "CCT5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P48643", "url": "https://www.uniprot.org/uniprotkb/P48643" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.16399879", "abstract": "", "glycosylation": [], 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J. Hum. Genet.", "date": "2020", "authors": "Schilit SLP, Menon S, Friedrich C, Kammin T, Wilch E, Hanscom C, Jiang S, Kliesch S, Talkowski ME, Tuttelmann F, MacQueen AJ, Morton CC", "reference": { "type": "PubMed", "id": "31866047", "url": "https://pubmed.ncbi.nlm.nih.gov/31866047" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9BX26-1", "protein_name": "Synaptonemal complex protein 2", "gene_name": "SYCP2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9BX26", "url": "https://www.uniprot.org/uniprotkb/Q9BX26" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.31866047", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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Saada V, Suarez F, Pierron G, Vainchenker W, Plo I, Donadieu J", "reference": { "type": "PubMed", "id": "29914977", "url": "https://pubmed.ncbi.nlm.nih.gov/29914977" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P61011-1", "protein_name": "Signal recognition particle subunit SRP54", "gene_name": "SRP54", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P61011", "url": "https://www.uniprot.org/uniprotkb/P61011" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.29914977", "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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}, { "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": "Only the complex N559-glycan in the synaptic vesicle glycoprotein 2C mediates high affinity binding to botulinum neurotoxin serotype A1.", "journal": "The Biochemical journal", "date": "2016", "authors": "Mahrhold S, Bergstrom T, 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Greater reduction in weight; when associated with Q-565.", "evidence": [ { "database": "UniProtKB", "id": "Q496J9", "url": "https://www.uniprot.org/uniprotkb/Q496J9" }, { "database": "PubMed", "id": "27313224", "url": "https://pubmed.ncbi.nlm.nih.gov/27313224" } ], "uniprot_canonical_ac": "Q496J9-1" }, { "start_pos": 561, "end_pos": 561, "sequence_org": "S", "sequence_mut": "A", "comment": "Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/AHC.", "evidence": [ { "database": "UniProtKB", "id": "Q496J9", "url": "https://www.uniprot.org/uniprotkb/Q496J9" }, { "database": "PubMed", "id": "27313224", "url": "https://pubmed.ncbi.nlm.nih.gov/27313224" } ], "uniprot_canonical_ac": "Q496J9-1" }, { "start_pos": 565, "end_pos": 565, "sequence_org": "N", "sequence_mut": "Q", "comment": "Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. 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