[ { "title": "Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates Arrhythmogenic Ca Waves and Sparks.", "journal": "Circulation. 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Sala L, Dreizehnter L, Crotti L, Sinnecker D, Mura M, Pane LS, Altomare C, Torre E, Mostacciuolo G, Severi S, Porta A, De Ferrari GM, George AL Jr, Schwartz PJ, Gnecchi M, Moretti A, Zaza A", "reference": { "type": "PubMed", "id": "28158429", "url": "https://pubmed.ncbi.nlm.nih.gov/28158429" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P0DP23-1", "protein_name": "Calmodulin-1", "gene_name": "CALM1; CALM2; CALM3", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P0DP23", "url": "https://www.uniprot.org/uniprotkb/P0DP23" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.28158429", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], 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J. Hum. 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"count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Association study of hypertension susceptibility genes ITGA9, MOV10, and CACNB2 with preeclampsia in Chinese Han population.", "journal": "The journal of maternal-fetal & neonatal medicine : the official journal of the European Association of Perinatal Medicine, the Federation of Asia and Oceania Perinatal Societies, the International Society of Perinatal Obstetricians", "date": "2022-12", "authors": "Xin Qian, Xin Gang, Li Li, Sun Wenjuan, Jiang Wen, Wang Jue, Luan Yun, Zhang Ying, Cheng Ling, Duan Shuhong, Hong Fanzhen, Ji Qinghong, Ma Weihong", "reference": { "type": "PubMed", "id": "33491517", "url": "https://pubmed.ncbi.nlm.nih.gov/33491517" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q08289-1", "protein_name": "Voltage-dependent L-type calcium channel subunit beta-2", "gene_name": "CACNB2", "tax_name": 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"Molecular cloning and characterization of the human voltage-gated calcium channel alpha(2)delta-4 subunit.", "journal": "Mol. Pharmacol.", "date": "2002", "authors": "Qin N, Yagel S, Momplaisir ML, Codd EE, D'Andrea MR", "reference": { "type": "PubMed", "id": "12181424", "url": "https://pubmed.ncbi.nlm.nih.gov/12181424" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P54284-1", "protein_name": "Voltage-dependent L-type calcium channel subunit beta-3", "gene_name": "CACNB3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8IZS8-1", "protein_name": "Voltage-dependent calcium channel subunit alpha-2/delta-3", "gene_name": "CACNA2D3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q7Z3S7-1", "protein_name": "Voltage-dependent calcium channel subunit alpha-2/delta-4", "gene_name": "CACNA2D4", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q13936-1", "protein_name": "Voltage-dependent L-type calcium channel subunit alpha-1C", "gene_name": "CACNA1C", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P54284", "url": "https://www.uniprot.org/uniprotkb/P54284" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.12181424", "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": "Alternative Splicing at N Terminus and Domain I Modulates CaV1.2 Inactivation and Surface Expression.", "journal": "Biophys. 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Cell Biol.", "date": "2002", "authors": "Mailand N, Lukas C, Kaiser BK, Jackson PK, Bartek J, Lukas J", "reference": { "type": "PubMed", "id": "11901424", "url": "https://pubmed.ncbi.nlm.nih.gov/11901424" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O60729-1", "protein_name": "Dual specificity protein phosphatase CDC14B", "gene_name": "CDC14B", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UNH5-1", "protein_name": "Dual specificity protein phosphatase CDC14A", "gene_name": "CDC14A", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O60729", "url": "https://www.uniprot.org/uniprotkb/O60729" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 362, "end_pos": 362, "sequence_org": "M", "sequence_mut": "A", "comment": "Inappropriate nucleolar localization; when associated with A-364.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNH5", "url": "https://www.uniprot.org/uniprotkb/Q9UNH5" }, { "database": "PubMed", "id": "11901424", "url": "https://pubmed.ncbi.nlm.nih.gov/11901424" } ], "uniprot_canonical_ac": "Q9UNH5-1" }, { "start_pos": 364, "end_pos": 364, "sequence_org": "I", "sequence_mut": "A", "comment": "Inappropriate nucleolar localization; when associated with A-362.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNH5", "url": "https://www.uniprot.org/uniprotkb/Q9UNH5" }, { "database": "PubMed", "id": "11901424", "url": "https://pubmed.ncbi.nlm.nih.gov/11901424" } ], "uniprot_canonical_ac": "Q9UNH5-1" } ], "record_id": "pubmed.11901424", "abstract": "", "glycosylation": [], "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": "Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase.", "journal": "Mol. Biol. Cell", "date": "2002", "authors": "Kaiser BK, Zimmerman ZA, Charbonneau H, Jackson PK", "reference": { "type": "PubMed", "id": "12134069", "url": "https://pubmed.ncbi.nlm.nih.gov/12134069" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O60729-1", "protein_name": "Dual specificity protein phosphatase CDC14B", "gene_name": "CDC14B", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UNH5-1", "protein_name": "Dual specificity protein phosphatase CDC14A", "gene_name": "CDC14A", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O60729", "url": "https://www.uniprot.org/uniprotkb/O60729" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 251, "end_pos": 251, "sequence_org": "D", "sequence_mut": "A", "comment": "Loss of phosphatase activity.", "evidence": [ { "database": "UniProtKB", "id": "Q9UNH5", 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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_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 structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase.", "journal": "EMBO J.", "date": "2003", "authors": "Gray Christopher H, Good Valerie M, Tonks Nicholas 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No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. 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Abolishes CDK2-dependent phosphorylation. Inhibits cellular proliferation delay in the early metaphase to prevent chromosomal instability. Does not inhibit interaction with a cyclin E-CDK2 complex. Does not inhibit interaction with HDAC6 and ubiquitination. Inhibits cell adhesion and migration and neurite outgrowth. Inhibits deacetylase activity; when associated with A-372.", "evidence": [ { "database": "UniProtKB", "id": "Q8IXJ6", "url": "https://www.uniprot.org/uniprotkb/Q8IXJ6" }, { "database": "PubMed", "id": "17516032", "url": "https://pubmed.ncbi.nlm.nih.gov/17516032" }, { "database": "PubMed", "id": "18332217", "url": "https://pubmed.ncbi.nlm.nih.gov/18332217" }, { "database": "PubMed", "id": "17488717", "url": "https://pubmed.ncbi.nlm.nih.gov/17488717" } ], "uniprot_canonical_ac": "Q8IXJ6-1" }, { "start_pos": 368, "end_pos": 368, "sequence_org": "S", "sequence_mut": "D", "comment": "Abolishes CDK2-dependent phosphorylation. Inhibits interaction with a cyclin E-CDK2 complex. 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