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Releases Human HSF1 from HSP70 Latency Control.", "journal": "Journal of molecular biology", "date": "2024-10-15", "authors": "Ciccarelli Michela, Andr\u00e9asson Claes", "reference": { "type": "PubMed", "id": "39122169", "url": "https://pubmed.ncbi.nlm.nih.gov/39122169" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q00613-1", "protein_name": "Heat shock factor protein 1", "gene_name": "HSF1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.39122169", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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Cell. Biol.", "date": "1994", "authors": "Rabindran S K, Wisniewski J, Li L, Li G C, Wu C", "reference": { "type": "PubMed", "id": "7935376", "url": "https://pubmed.ncbi.nlm.nih.gov/7935376" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q00613-1", "protein_name": "Heat shock factor protein 1", "gene_name": "HSF1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P0DMV8-1", "protein_name": "Heat shock 70 kDa protein 1A", "gene_name": "HSPA1A", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.7935376", "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": "Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure.", "journal": "Molecular and cellular biology", "date": "1994", "authors": "Zuo J, Baler R, Dahl G, Voellmy R", "reference": { "type": "PubMed", "id": "7935471", "url": "https://pubmed.ncbi.nlm.nih.gov/7935471" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q00613-1", "protein_name": "Heat shock factor protein 1", "gene_name": "HSF1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 140, "end_pos": 140, "sequence_org": "L", "sequence_mut": "K", "comment": "Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Does not lead to constitutive transactivation activity at 20 degrees Celsius. Decreased DNA-binding activity at 37 degrees Celsius.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "7623826", "url": "https://pubmed.ncbi.nlm.nih.gov/7623826" }, { "database": "PubMed", "id": "7935471", "url": "https://pubmed.ncbi.nlm.nih.gov/7935471" } ], "uniprot_canonical_ac": "Q00613-1" }, { "start_pos": 147, "end_pos": 147, "sequence_org": "M", "sequence_mut": "A", "comment": "Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Does not lead to constitutive transactivation activity at 20 degrees Celsius. No effect on DNA-binding activity at 37 degrees Celsius.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "7623826", "url": "https://pubmed.ncbi.nlm.nih.gov/7623826" }, { "database": "PubMed", "id": "7935471", "url": "https://pubmed.ncbi.nlm.nih.gov/7935471" } ], "uniprot_canonical_ac": "Q00613-1" }, { "start_pos": 147, "end_pos": 147, "sequence_org": "M", "sequence_mut": "E", "comment": "Does not lead to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. 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No effect on DNA-binding activity at 37 degrees Celsius.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "7935471", "url": "https://pubmed.ncbi.nlm.nih.gov/7935471" } ], "uniprot_canonical_ac": "Q00613-1" } ], "record_id": "pubmed.7935471", "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": "Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1.", "journal": "The Journal of biological chemistry", "date": "1996", "authors": "Chu B, Soncin F, Price BD, Stevenson MA, Calderwood SK", "reference": { "type": "PubMed", "id": "8940068", "url": "https://pubmed.ncbi.nlm.nih.gov/8940068" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q00613-1", "protein_name": "Heat shock factor protein 1", "gene_name": "HSF1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 275, "end_pos": 275, "sequence_org": "S", "sequence_mut": "G", "comment": "Leads to weak constitutive transactivation activity at room temperature.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "8940068", "url": "https://pubmed.ncbi.nlm.nih.gov/8940068" } ], "uniprot_canonical_ac": "Q00613-1" }, { "start_pos": 303, "end_pos": 303, "sequence_org": "S", "sequence_mut": "G", "comment": "Leads to constitutive transactivation activity at room temperature. 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"abstract": "", "glycosylation": [], "snv": [], "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": 6 }, { "field": "total_sites", "count": 3 } ], "sort_fields": [ "start_pos", "end_pos", "kinase_uniprot_canonical_ac", "kinase_gene_name", "residue", "comment", "site_lbl", "uniprot_canonical_ac" ] }, { "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": "Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation.", "journal": "Molecular and cellular biology", "date": "1997", "authors": "Kline MP, Morimoto RI", "reference": { "type": "PubMed", "id": "9121459", "url": "https://pubmed.ncbi.nlm.nih.gov/9121459" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q00613-1", "protein_name": "Heat shock factor protein 1", "gene_name": "HSF1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 303, "end_pos": 303, "sequence_org": "S", "sequence_mut": "A", "comment": "No phosphorylation nor sumoylation. No change in nuclear stress granules subcellular location upon heat shock. Loss of colocalization with SUMO1 to nuclear stress granules upon heat shock. Slight decrease in transcriptional activity on heat treatment. No change in PLK1-induced phosphorylation in mitosis, induces derepression of transcription activation at control temperature, abolishes sumoylation and induces 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-307.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "8946918", "url": "https://pubmed.ncbi.nlm.nih.gov/8946918" }, { "database": "PubMed", "id": "9535852", "url": "https://pubmed.ncbi.nlm.nih.gov/9535852" }, { "database": "PubMed", "id": "12665592", "url": "https://pubmed.ncbi.nlm.nih.gov/12665592" }, { "database": "PubMed", "id": "9121459", "url": "https://pubmed.ncbi.nlm.nih.gov/9121459" }, { "database": "PubMed", "id": "12646186", "url": "https://pubmed.ncbi.nlm.nih.gov/12646186" }, { "database": "PubMed", "id": "18794143", "url": "https://pubmed.ncbi.nlm.nih.gov/18794143" } ], "uniprot_canonical_ac": "Q00613-1" }, { "start_pos": 303, "end_pos": 303, "sequence_org": "S", "sequence_mut": "D", "comment": "Mimics phosphorylation. No effect on in vitro sumoylation. Greatly increased transcriptional activity on heat induction. 5-fold derepression of transcriptional activity at control temperature; when associated with D-307.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "8946918", "url": "https://pubmed.ncbi.nlm.nih.gov/8946918" }, { "database": "PubMed", "id": "9535852", "url": "https://pubmed.ncbi.nlm.nih.gov/9535852" }, { "database": "PubMed", "id": "12665592", "url": "https://pubmed.ncbi.nlm.nih.gov/12665592" }, { "database": "PubMed", "id": "9121459", "url": "https://pubmed.ncbi.nlm.nih.gov/9121459" } ], "uniprot_canonical_ac": "Q00613-1" }, { "start_pos": 307, "end_pos": 307, "sequence_org": "S", "sequence_mut": "A", "comment": "No phosphorylation. Does not reduce Ser-303 phosphorylation. 1.5% increase in transcriptional activity on heat-treatment. No change in PLK1-induced phosphorylation in mitosis, induces derepression of transcription activation at control temperature, abolishes sumoylation and induces 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303.", "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" }, { "database": "PubMed", "id": "8946918", "url": "https://pubmed.ncbi.nlm.nih.gov/8946918" }, { "database": "PubMed", "id": "9535852", "url": "https://pubmed.ncbi.nlm.nih.gov/9535852" }, { "database": "PubMed", "id": "12665592", "url": "https://pubmed.ncbi.nlm.nih.gov/12665592" }, { "database": "PubMed", "id": "9121459", "url": "https://pubmed.ncbi.nlm.nih.gov/9121459" }, { "database": "PubMed", "id": "12646186", "url": "https://pubmed.ncbi.nlm.nih.gov/12646186" }, { "database": "PubMed", "id": "18794143", "url": "https://pubmed.ncbi.nlm.nih.gov/18794143" } ], "uniprot_canonical_ac": "Q00613-1" }, { "start_pos": 307, "end_pos": 307, "sequence_org": "S", "sequence_mut": "D", "comment": "5-fold derepression of transcriptional activity at control temperature; when associated with D-303. 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[] } ] }, { "title": "Heat shock factor 1 represses Ras-induced transcriptional activation of the c-fos gene.", "journal": "The Journal of biological chemistry", "date": "1997", "authors": "Chen C, Xie Y, Stevenson MA, Auron PE, Calderwood SK", "reference": { "type": "PubMed", "id": "9341107", "url": "https://pubmed.ncbi.nlm.nih.gov/9341107" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q00613-1", "protein_name": "Heat shock factor protein 1", "gene_name": "HSF1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q00613", "url": "https://www.uniprot.org/uniprotkb/Q00613" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 22, "end_pos": 22, "sequence_org": "L", "sequence_mut": "A", "comment": "Inhibits HSEDNA-binding activity and transcriptional activation.", "evidence": [ { "database": 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Chem.", "date": "2011", "authors": "Hong Jaewoo, Bae Suyoung, Jhun Hyunjhung, Lee Siyoung, Choi Jida, Kang Taebong, Kwak Areum, Hong Kwangwon, Kim Eunsom, Jo Seunghyun, Kim Soohyun", "reference": { "type": "PubMed", "id": "21454686", "url": "https://pubmed.ncbi.nlm.nih.gov/21454686" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O95760-1", "protein_name": "Interleukin-33", "gene_name": "IL33", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O95760", "url": "https://www.uniprot.org/uniprotkb/O95760" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.21454686", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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Int. Genet.", "date": "2010", "authors": "Mengel-From Jonas, B\u00f8rsting Claus, Sanchez Juan J, Eiberg Hans, Morling Niels", "reference": { "type": "PubMed", "id": "20457063", "url": "https://pubmed.ncbi.nlm.nih.gov/20457063" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O95714-1", "protein_name": "E3 ubiquitin-protein ligase HERC2", "gene_name": "HERC2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O95714", "url": "https://www.uniprot.org/uniprotkb/O95714" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.20457063", "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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plasma membrane uncouples triggering from amplifying Ca2+ signals.", "journal": "The Journal of biological chemistry", "date": "2010", "authors": "Brailoiu E, Rahman T, Churamani D, Prole DL, Brailoiu GC, Hooper R, Taylor CW, Patel S", "reference": { "type": "PubMed", "id": "20880839", "url": "https://pubmed.ncbi.nlm.nih.gov/20880839" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9ULQ1-1", "protein_name": "Two pore channel protein 1", "gene_name": "TPCN1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8NHX9-1", "protein_name": "Two pore channel protein 2", "gene_name": "TPCN2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9ULQ1", "url": "https://www.uniprot.org/uniprotkb/Q9ULQ1" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 740, "end_pos": 741, "sequence_org": "LL", 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Loss of NAADP-sensitive calcium-release channel activity. 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