[ { "title": "RIPK3 causes mitochondrial dysfunction and albuminuria in diabetic podocytopathy through PGAM5-Drp1 signaling.", "journal": "Metabolism: clinical and experimental", "date": "2024-10", "authors": "Kang Jeong Suk, Cho Nam-Jun, Lee Seong Woo, Lee Jeong Geon, Lee Ji-Hye, Yi Jawoon, Choi Min Sun, Park Samel, Gil Hyo-Wook, Oh Joon Cheol, Son Seung Seob, Park Mi Ju, Moon Jong-Seok, Lee Donghyeong, Kim So-Young, Yang Seung-Hoon, Kim Sang Soo, Lee Eun Soo, Chung Choon Hee, Park Jihwan, Lee Eun Young", "reference": { "type": "PubMed", "id": "39089491", "url": "https://pubmed.ncbi.nlm.nih.gov/39089491" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9Y572-1", "protein_name": "Receptor-interacting serine/threonine-protein kinase 3", "gene_name": "RIPK3", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9Y572", "url": "https://www.uniprot.org/uniprotkb/Q9Y572" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.39089491", "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", 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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": "Characterization of a novel human protein phosphatase 2C family member, PP2Ckappa.", "journal": "International journal of molecular medicine", "date": "2006", "authors": "Dai J, Zhang J, Sun Y, Wu Q, Sun L, Ji C, Gu S, Feng C, Xie Y, Mao Y", "reference": { "type": "PubMed", "id": "16685424", "url": "https://pubmed.ncbi.nlm.nih.gov/16685424" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3J5-1", "protein_name": "Protein phosphatase Mn(2+)-dependent 1K", "gene_name": "PPM1K", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8N3J5", "url": "https://www.uniprot.org/uniprotkb/Q8N3J5" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.16685424", "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", 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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": "The role of PP5 and PP2C in cardiac health and disease.", "journal": "Cellular signalling", "date": "2021", "authors": "Neumann J, Boknik P, Kirchhefer U, Gergs U", "reference": { "type": "PubMed", "id": "33964402", "url": "https://pubmed.ncbi.nlm.nih.gov/33964402" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3J5-1", "protein_name": "Protein phosphatase Mn(2+)-dependent 1K", "gene_name": "PPM1K", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8N3J5", "url": "https://www.uniprot.org/uniprotkb/Q8N3J5" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.33964402", "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", 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"Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase.", "journal": "Biochemistry", "date": "2000", "authors": "Schmidt A, Wu H, MacKenzie RE, Chen VJ, Bewly JR, Ray JE, Toth JE, Cygler M", "reference": { "type": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P11586-1", "protein_name": "C-1-tetrahydrofolate synthase, cytoplasmic", "gene_name": "MTHFD1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 147, "end_pos": 147, "sequence_org": "C", "sequence_mut": "Q", "comment": "Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 50%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 87%.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 49, "end_pos": 49, "sequence_org": "S", "sequence_mut": "A", "comment": "No effect on methylenetetrahydrofolate dehydrogenase (NADP+) activity. No effect on methenyltetrahydrofolate cyclohydrolase activity. Decreased affinity for NADP.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 49, "end_pos": 49, "sequence_org": "S", "sequence_mut": "Q", "comment": "Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 75%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 99%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 52, "end_pos": 52, "sequence_org": "Y", "sequence_mut": "A", "comment": "Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 99%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 70%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 52, "end_pos": 52, "sequence_org": "Y", "sequence_mut": "F", "comment": "Slightly reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity. Slightly reduced methenyltetrahydrofolate cyclohydrolase activity. Decreased affinity for NADP and for 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 52, "end_pos": 52, "sequence_org": "Y", "sequence_mut": "S", "comment": "Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 99%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 70%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "A", "comment": "Decreased methylenetetrahydrofolate dehydrogenase (NADP+) activity over 90%. Loss of methenyltetrahydrofolate cyclohydrolase activity.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "E", "comment": "Moderate decrease of methylenetetrahydrofolate dehydrogenase (NADP+) activity. Loss of methenyltetrahydrofolate cyclohydrolase activity. Strongly decreased affinity for NADP. Increased affinity for 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "I", "comment": "Decreased methylenetetrahydrofolate dehydrogenase (NADP+) activity over 90%. Loss of methenyltetrahydrofolate cyclohydrolase activity.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "M", "comment": "Moderate decrease of methylenetetrahydrofolate dehydrogenase (NADP+) activity. Loss of methenyltetrahydrofolate cyclohydrolase activity. Strongly decreased affinity for NADP. Increased affinity for 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "Q", "comment": "Moderate decrease of methylenetetrahydrofolate dehydrogenase (NADP+) activity. Loss of methenyltetrahydrofolate cyclohydrolase activity. Strongly decreased affinity for NADP. Increased affinity for 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity. Reduced methenyltetrahydrofolate cyclohydrolase activity by 99%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.", "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" }, { "database": "PubMed", "id": "10828945", "url": "https://pubmed.ncbi.nlm.nih.gov/10828945" } ], "uniprot_canonical_ac": "P11586-1" }, { "start_pos": 56, "end_pos": 56, "sequence_org": "K", "sequence_mut": "S", "comment": "Decreased methylenetetrahydrofolate dehydrogenase (NADP+) activity over 90%. 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patients with neural tube defects.", "journal": "Clinical genetics", "date": "1998", "authors": "Hol FA, van der Put NM, Geurds MP, Heil SG, Trijbels FJ, Hamel BC, Mariman EC, Blom HJ", "reference": { "type": "PubMed", "id": "9611072", "url": "https://pubmed.ncbi.nlm.nih.gov/9611072" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P11586-1", "protein_name": "C-1-tetrahydrofolate synthase, cytoplasmic", "gene_name": "MTHFD1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P11586", "url": "https://www.uniprot.org/uniprotkb/P11586" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.9611072", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], 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bipolar disorder increase the sensitivity to stress.", "journal": "Molecular psychiatry", "date": "2022", "authors": "Sitbon J, Nestvogel D, Kappeler C, Nicolas A, Maciuba S, Henrion A, Troudet R, Courtois E, Grannec G, Latapie V, Barau C, Le Corvoisier P, Pietrancosta N, Henry C, Leboyer M, Etain B, Nosten-Bertrand M, Martin TFJ, Rhee J, Jamain S", "reference": { "type": "PubMed", "id": "35169262", "url": "https://pubmed.ncbi.nlm.nih.gov/35169262" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9ULU8-1", "protein_name": "Calcium-dependent secretion activator 1", "gene_name": "CADPS", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q80TJ1-1", "protein_name": "Calcium-dependent secretion activator 1", "gene_name": "Cadps", "tax_name": "Mouse" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9ULU8", "url": "https://www.uniprot.org/uniprotkb/Q9ULU8" } ], "common_name": "Human", "glygen_name": 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"authors": "Wang Zi-Jian, Dai Zhi-Zheng, Hu Mei-Zhen, Liu Jun-Nan, Liang Hang, Shen Mei-Mei, Zhu Shu-Juan, Sheng Hua-Jun, Gao Jian, Huang Ai-Long, Tang Kai-Fu", "reference": { "type": "PubMed", "id": "36792863", "url": "https://pubmed.ncbi.nlm.nih.gov/36792863" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P23258-1", "protein_name": "Tubulin gamma-1 chain", "gene_name": "TUBG1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P23258", "url": "https://www.uniprot.org/uniprotkb/P23258" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.36792863", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", 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"o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an X-linked mental retardation syndrome associated with aggressive outbursts, seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus, and tremor.", "journal": "American journal of human genetics", "date": "2007", "authors": "Tarpey PS, Raymond FL, O'Meara S, Edkins S, Teague J, Butler A, Dicks E, Stevens C, Tofts C, Avis T, Barthorpe S, Buck G, Cole J, Gray K, Halliday K, Harrison R, Hills K, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Varian J, West S, Widaa S, Mallya U, Moon J, Luo Y, Holder S, Smithson SF, Hurst JA, Clayton-Smith J, Kerr B, Boyle J, Shaw M, Vandeleur L, Rodriguez J, Slaugh R, Easton DF, Wooster R, Bobrow M, Srivastava AK, Stevenson RE, Schwartz CE, Turner G, Gecz J, Futreal PA, Stratton MR, Partington M", "reference": { "type": "PubMed", "id": 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"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", 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J. Hum. Genet.", "date": "2007", "authors": "Zou Yongxin, Liu Qiji, Chen Bingxi, Zhang Xiyu, Guo Chenhong, Zhou Haibin, Li Jiangxia, Gao Guimin, Guo Yishou, Yan Chuanzhu, Wei Jianjun, Shao Changshun, Gong Yaoqin", "reference": { "type": "PubMed", "id": "17273978", "url": "https://pubmed.ncbi.nlm.nih.gov/17273978" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q13620-2", "protein_name": "Cullin-4B", "gene_name": "CUL4B", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q13620", "url": "https://www.uniprot.org/uniprotkb/Q13620" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.17273978", "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": "Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression.", "journal": "The Journal of biological chemistry", "date": "2009", "authors": "Zou Y, Mi J, Cui J, Lu D, Zhang X, Guo C, Gao G, Liu Q, Chen B, Shao C, Gong Y", "reference": { "type": "PubMed", "id": "19801544", "url": "https://pubmed.ncbi.nlm.nih.gov/19801544" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q13620-2", "protein_name": "Cullin-4B", "gene_name": "CUL4B", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q13620", "url": "https://www.uniprot.org/uniprotkb/Q13620" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 55, "end_pos": 55, "sequence_org": "K", "sequence_mut": "A", "comment": "No impairment in nuclear localization.", "evidence": [ { "database": "UniProtKB", "id": "Q13620", "url": "https://www.uniprot.org/uniprotkb/Q13620" }, { "database": "PubMed", "id": "19801544", "url": "https://pubmed.ncbi.nlm.nih.gov/19801544" } ], "uniprot_canonical_ac": "Q13620-2" }, { "start_pos": 55, "end_pos": 58, "sequence_org": "KKRK", "sequence_mut": "", "comment": "Distributed in cytoplasm. 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Genet.", "date": "2010", "authors": "Badura-Stronka M, Jamsheer A, Materna-Kiryluk A, Sowi\u0144ska A, Kiryluk K, Budny B, Latos-Biele\u0144ska A", "reference": { "type": "PubMed", "id": "20002452", "url": "https://pubmed.ncbi.nlm.nih.gov/20002452" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q13620-2", "protein_name": "Cullin-4B", "gene_name": "CUL4B", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q13620", "url": "https://www.uniprot.org/uniprotkb/Q13620" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.20002452", "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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"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": "Cardiac anomalies in Axenfeld-Rieger syndrome due to a novel FOXC1 mutation.", "journal": "American journal of medical genetics. Part A", "date": "2013", "authors": "Gripp KW, Hopkins E, Jenny K, Thacker D, Salvin J", "reference": { "type": "PubMed", "id": "23239455", "url": "https://pubmed.ncbi.nlm.nih.gov/23239455" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q12948-1", "protein_name": "Forkhead box protein C1", "gene_name": "FOXC1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q12948", "url": "https://www.uniprot.org/uniprotkb/Q12948" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.23239455", "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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