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Cloning of the cDNA and further characterization.", "journal": "J. Biol. Chem.", "date": "1993", "authors": "Kieffer LJ, Seng TW, Li W, Osterman DG, Handschumacher RE, Bayney RM", "reference": { "type": "PubMed", "id": "8509368", "url": "https://pubmed.ncbi.nlm.nih.gov/8509368" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P26882-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase D", "gene_name": "PPID", "tax_name": "Bovine" }, { "uniprot_canonical_ac": "Q08752-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase D", "gene_name": "PPID", "tax_name": "Human" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "P26882", "url": "https://www.uniprot.org/uniprotkb/P26882" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "record_id": "pubmed.8509368", "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 cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59).", "journal": "J. Biol. Chem.", "date": "1993", "authors": "Ratajczak T, Carrello A, Mark P J, Warner B J, Simpson R J, Moritz R L, House A K", "reference": { "type": "PubMed", "id": "8514757", "url": "https://pubmed.ncbi.nlm.nih.gov/8514757" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P26882-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase D", "gene_name": "PPID", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "P26882", "url": "https://www.uniprot.org/uniprotkb/P26882" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "record_id": "pubmed.8514757", "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": "Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding.", "journal": "J. 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Chem.", "date": "1999", "authors": "Carrello A, Ingley E, Minchin R F, Tsai S, Ratajczak T", "reference": { "type": "PubMed", "id": "9915798", "url": "https://pubmed.ncbi.nlm.nih.gov/9915798" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P26882-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase D", "gene_name": "PPID", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "P26882", "url": "https://www.uniprot.org/uniprotkb/P26882" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "record_id": "pubmed.9915798", "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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Androl.", "date": "2010", "authors": "Nagdas Subir K, Hamilton Shatasha L, Raychoudhury Samirsubas", "reference": { "type": "PubMed", "id": "19478333", "url": "https://pubmed.ncbi.nlm.nih.gov/19478333" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "A6H782-1", "protein_name": "Tektin-3", "gene_name": "TEKT3", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "A6H782", "url": "https://www.uniprot.org/uniprotkb/A6H782" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "record_id": "pubmed.19478333", "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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Abolishes the transient current establishes in the presence of ATP and the negatively charged lipid substrate phosphatidylserine.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "31371510", "url": "https://pubmed.ncbi.nlm.nih.gov/31371510" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 388, "end_pos": 388, "sequence_org": "D", "sequence_mut": "N", "comment": "Abolishes ATPAse activity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 837, "end_pos": 837, "sequence_org": "K", "sequence_mut": "A", "comment": "No effect on flipping of PS and ATPase activity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 845, "end_pos": 845, "sequence_org": "K", "sequence_mut": "A", "comment": "Greatly reduces flipping of PS; reduces affinity PS by 7- and 8-fold; for reduces ATPase activity by 30- and 70-fold; reduces PS-activated dephosphorylation of intermediate; reduces affinity to vanadate.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 845, "end_pos": 845, "sequence_org": "K", "sequence_mut": "E", "comment": "Greatly reduces flipping of PS; reduces affinity PS by 7- and 8-fold; for reduces ATPase activity by 30- and 70-fold.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 845, "end_pos": 845, "sequence_org": "K", "sequence_mut": "R", "comment": "Reduces flipping of PS; reduces affinity PS by 4-fold; reduces ATPase activity by 10-fold.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 846, "end_pos": 846, "sequence_org": "N", "sequence_mut": "A", "comment": "Reduces flipping of PS; reduces affinity PS by 3-fold; reduces ATPase activity by 10-fold.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "22307598", "url": "https://pubmed.ncbi.nlm.nih.gov/22307598" } ], "uniprot_canonical_ac": "C7EXK4-1" } ], "record_id": "pubmed.22307598", "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": "Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2014-04-08", "authors": "Vestergaard Anna L, Coleman Jonathan A, Lemmin Thomas, Mikkelsen Stine A, Molday Laurie L, Vilsen Bente, Molday Robert S, Dal Peraro Matteo, Andersen Jens Peter", "reference": { "type": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "C7EXK4-1", "protein_name": "Phospholipid-transporting ATPase IB", "gene_name": "ATP8A2", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "mutagenesis": [ { "start_pos": 326, "end_pos": 326, "sequence_org": "F", "sequence_mut": "A", "comment": "Does not affect affinity for PS.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 330, "end_pos": 330, "sequence_org": "Y", "sequence_mut": "A", "comment": "Does not affect affinity for PS.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 331, "end_pos": 331, "sequence_org": "N", "sequence_mut": "A", "comment": "Dramatically reduces the maximal velocity (Vmax) to 11% that of the wild type (WT) for PS and 9% for PE. Reduces approximately sixfold the apparent affinity for PS and PE. Strongly reduces ATPase activity. Loss of the PS flipping. Enhances approximately threefold the phosphorylation rate. Reduces highly the apparent affinity for vanadate.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 332, "end_pos": 332, "sequence_org": "N", "sequence_mut": "A", "comment": "Increases the apparent affinity for PS. Reduces approximately twofold the PS flipping rate relative to the WT. Does not affect the phosphorylation rate.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 333, "end_pos": 333, "sequence_org": "L", "sequence_mut": "A", "comment": "Does not affect affinity for PS. Decreases TMEM30A glycosylation. Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. Reduces markedly the flipping activity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" }, { "database": "PubMed", "id": "26592152", "url": "https://pubmed.ncbi.nlm.nih.gov/26592152" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 334, "end_pos": 334, "sequence_org": "I", "sequence_mut": "A", "comment": "Increases the apparent affinity for PS.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 336, "end_pos": 336, "sequence_org": "I", "sequence_mut": "E", "comment": "Loss of flipping activity. PS- and PE-stimulated activity is very low. Does not affect the phosphorylation rates. Substantially reduces the apparent affinity for PS. Only slightly reduced vanadate affinity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 336, "end_pos": 336, "sequence_org": "I", "sequence_mut": "F", "comment": "Loss of flipping activity. PS- and PE-stimulated activity is very low. The phosphorylation rates is fourfold reduced. Substantially reduces the apparent affinity for PS. Does not affect vanadate affinity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 336, "end_pos": 336, "sequence_org": "I", "sequence_mut": "M", "comment": "Loss of flipping activity. PS- and PE-stimulated activity is very low. The phosphorylation rates is twofold reduced. Substantially reduces the apparent affinity for PS. Markedly reduced vanadate affinity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 336, "end_pos": 336, "sequence_org": "I", "sequence_mut": "Q", "comment": "Decreases flipping activity of about 90%. PS- and PE-stimulated activity is very low. The phosphorylation rates is twofold reduced. Reduces markedly reduced vanadate affinity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 336, "end_pos": 336, "sequence_org": "I", "sequence_mut": "S", "comment": "Decreases flipping activity of 70%. Phosphatidylserine (PS) stimulates the ATPase activity to maximum levels of 43% of the wild type level. Phosphatityletanolamine (PE)-stimulated maximum activity is only 22% of wild type. The phosphorylation rates is fourfold reduced. Enhances approximately twofold the apparent affinity for PS. Increases significantly apparent vanadate affinity.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 337, "end_pos": 337, "sequence_org": "S", "sequence_mut": "A", "comment": "Reduces significantly affinity for PS. Reduces apparent affinity for PE.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 339, "end_pos": 339, "sequence_org": "L", "sequence_mut": "A", "comment": "Reduces significantly affinity for PS. Does not affect apparent affinity for PE.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 341, "end_pos": 341, "sequence_org": "T", "sequence_mut": "A", "comment": "Increases the apparent affinity for PS.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 343, "end_pos": 343, "sequence_org": "E", "sequence_mut": "Q", "comment": "Does not affect affinity for PS.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 346, "end_pos": 346, "sequence_org": "K", "sequence_mut": "A", "comment": "Does not affect affinity for PS.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 60, "end_pos": 60, "sequence_org": "F", "sequence_mut": "A", "comment": "Enhances substrate affinities. Reduces considerably the Vmax.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 84, "end_pos": 84, "sequence_org": "L", "sequence_mut": "A", "comment": "Does not affect Vmax. Does not affect the apparent affinities for the substrates. Does not affect the phosphorylation rate.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" }, { "start_pos": 87, "end_pos": 87, "sequence_org": "I", "sequence_mut": "A", "comment": "Reduces approximately twofold the apparent affinity for PS. Does not affect the apparent affinity for PE.", "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" }, { "database": "PubMed", "id": "24706822", "url": "https://pubmed.ncbi.nlm.nih.gov/24706822" } ], "uniprot_canonical_ac": "C7EXK4-1" } ], "record_id": "pubmed.24706822", "abstract": "", "glycosylation": [], "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": "Phosphatidylserine flipping by the P4-ATPase ATP8A2 is electrogenic.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2019", "authors": "Tadini-Buoninsegni F, Mikkelsen SA, Mogensen LS, Molday RS, Andersen JP", "reference": { "type": "PubMed", "id": "31371510", "url": "https://pubmed.ncbi.nlm.nih.gov/31371510" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "C7EXK4-1", "protein_name": "Phospholipid-transporting ATPase IB", "gene_name": "ATP8A2", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "C7EXK4", "url": "https://www.uniprot.org/uniprotkb/C7EXK4" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "mutagenesis": [ { "start_pos": 170, "end_pos": 170, "sequence_org": "E", "sequence_mut": "Q", "comment": "Slightly reverses flipping of PS, no ATPase activity. 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The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin.", "journal": "The Journal of biological chemistry", "date": "1997", "authors": "Chiba A, Matsumura K, Yamada H, Inazu T, Shimizu T, Kusunoki S, Kanazawa I, Kobata A, Endo T", "reference": { "type": "PubMed", "id": "8999917", "url": "https://pubmed.ncbi.nlm.nih.gov/8999917" }, "referenced_glycans": [ { "glytoucan_ac": "G59126YU" }, { "glytoucan_ac": "G82453SK" }, { "glytoucan_ac": "G44528IE" }, { "glytoucan_ac": "G47256GA" }, { "glytoucan_ac": "G48849EN" }, { "glytoucan_ac": "G49644CL" }, { "glytoucan_ac": "G29931IJ" }, { "glytoucan_ac": "G45349TS" } ], "referenced_proteins": [ { "uniprot_canonical_ac": "O18738-1", "protein_name": "Dystroglycan 1", "gene_name": "DAG1", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "O18738", "url": "https://www.uniprot.org/uniprotkb/O18738" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "glycan_expression": [ { "glytoucan_ac": "G82453SK", "abundance": "", "tissue": { "name": "", "namespace": "UBERON", "id": "0001021", "url": "http://purl.obolibrary.org/obo/UBERON_0001021" }, "species": { "name": "Bos taurus", "taxid": 9913, "reference_species": "Bos taurus [9913]", "common_name": "Bovine", "glygen_name": "Bovine" }, "cell_line": {} }, { "glytoucan_ac": "G45349TS", "abundance": "", "tissue": { "name": "", "namespace": "UBERON", "id": "0001021", "url": "http://purl.obolibrary.org/obo/UBERON_0001021" }, "species": { "name": "Bos taurus", "taxid": 9913, "reference_species": "Bos taurus [9913]", "common_name": "Bovine", "glygen_name": "Bovine" }, "cell_line": {} } ], "record_id": "pubmed.8999917", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 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0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments.", "journal": "Molecular and cellular biology", "date": "1997-07", "authors": "Sakisaka T, Itoh T, Miura K, Takenawa T", "reference": { "type": "PubMed", "id": "9199318", "url": "https://pubmed.ncbi.nlm.nih.gov/9199318" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O18964-1", "protein_name": "Polyphosphatidylinositol phosphatase SYNJ1", "gene_name": "SYNJ1", "tax_name": "Bovine" } ], "species": [ { "name": "Bos taurus", "taxid": 9913, "evidence": [ { "database": "UniProtKB", "id": "O18964", "url": "https://www.uniprot.org/uniprotkb/O18964" } ], "common_name": "Bovine", "glygen_name": "Bovine", "reference_species": "Bos taurus [9913]" } ], "record_id": "pubmed.9199318", 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"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 endogenous phosphorylation sites of bovine medium and low molecular weight neurofilament proteins by tandem mass spectrometry.", "journal": "Biochemistry", "date": "2004-02-24", "authors": "Trimpin Sarah, Mixon April E, Stapels 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