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Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase.", "journal": "The Journal of biological chemistry", "date": "2002", "authors": "Verbsky JW, Wilson MP, Kisseleva MV, Majerus PW, Wente SR", "reference": { "type": "PubMed", "id": "12084730", "url": "https://pubmed.ncbi.nlm.nih.gov/12084730" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9H8X2-1", "protein_name": "Inositol-pentakisphosphate 2-kinase", "gene_name": "IPPK", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UHH9-1", "protein_name": "Inositol hexakisphosphate kinase 2", "gene_name": "IP6K2", "tax_name": "Human" }, { "uniprot_canonical_ac": "O95989-1", "protein_name": "Diphosphoinositol polyphosphate phosphohydrolase 1", "gene_name": "NUDT3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96G61-1", "protein_name": "Diphosphoinositol polyphosphate phosphohydrolase 3-beta", "gene_name": "NUDT11", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96PC2-1", 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"protein_name": "Inositol-tetrakisphosphate 1-kinase", "gene_name": "ITPK1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q6PFW1-1", "protein_name": "Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1", "gene_name": "PPIP5K1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9H8X2", "url": "https://www.uniprot.org/uniprotkb/Q9H8X2" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.12105228", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 10 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { 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"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": "Inositol polyphosphate multikinase regulates inositol 1,4,5,6-tetrakisphosphate.", "journal": "Biochemical and biophysical research communications", "date": "2006", "authors": "Chang SC, Majerus PW", "reference": { "type": "PubMed", "id": "16293229", "url": "https://pubmed.ncbi.nlm.nih.gov/16293229" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9H8X2-1", "protein_name": "Inositol-pentakisphosphate 2-kinase", "gene_name": "IPPK", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UHH9-1", "protein_name": "Inositol hexakisphosphate kinase 2", "gene_name": "IP6K2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q92551-1", "protein_name": "Inositol hexakisphosphate kinase 1", "gene_name": "IP6K1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8NFU5-1", "protein_name": "Inositol polyphosphate multikinase", "gene_name": "IPMK", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9H8X2", "url": 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"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": "Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress.", "journal": "The Journal of biological chemistry", "date": "2007", "authors": "Choi JH, Williams J, Cho J, Falck JR, Shears SB", "reference": { "type": "PubMed", "id": "17702752", "url": "https://pubmed.ncbi.nlm.nih.gov/17702752" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9H8X2-1", "protein_name": "Inositol-pentakisphosphate 2-kinase", "gene_name": "IPPK", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UHH9-1", "protein_name": "Inositol hexakisphosphate kinase 2", "gene_name": "IP6K2", "tax_name": "Human" }, { "uniprot_canonical_ac": "O95989-1", "protein_name": "Diphosphoinositol polyphosphate phosphohydrolase 1", "gene_name": "NUDT3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96G61-1", "protein_name": "Diphosphoinositol polyphosphate phosphohydrolase 3-beta", "gene_name": "NUDT11", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96PC2-1", "protein_name": "Inositol hexakisphosphate kinase 3", "gene_name": "IP6K3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NZJ9-1", "protein_name": "Diphosphoinositol polyphosphate phosphohydrolase 2", "gene_name": "NUDT4", "tax_name": "Human" }, { "uniprot_canonical_ac": "O43314-1", "protein_name": "Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2", "gene_name": "PPIP5K2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q92551-1", "protein_name": "Inositol hexakisphosphate kinase 1", "gene_name": "IP6K1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8NFU5-1", "protein_name": "Inositol polyphosphate multikinase", "gene_name": "IPMK", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8NFP7-1", "protein_name": "Diphosphoinositol polyphosphate phosphohydrolase 3-alpha", "gene_name": "NUDT10", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q13572-1", "protein_name": "Inositol-tetrakisphosphate 1-kinase", 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"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": "Inositol hexakisphosphate kinase products contain diphosphate and triphosphate groups.", "journal": "Chemistry & biology", "date": "2008", "authors": "Draskovic P, Saiardi A, Bhandari R, Burton A, Ilc G, Kovacevic M, Snyder SH, Podobnik M", "reference": { "type": "PubMed", "id": "18355727", "url": "https://pubmed.ncbi.nlm.nih.gov/18355727" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9H8X2-1", "protein_name": "Inositol-pentakisphosphate 2-kinase", "gene_name": "IPPK", "tax_name": "Human" }, { 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Renal physiology", "date": "2018", "authors": "Looker HC, Merchant ML, Rane MJ, Nelson RG, Kimmel PL, Rovin BH, Klein JB, Mauer M", "reference": { "type": "PubMed", "id": "30132343", "url": "https://pubmed.ncbi.nlm.nih.gov/30132343" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9H8X2-1", "protein_name": "Inositol-pentakisphosphate 2-kinase", "gene_name": "IPPK", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9H8X2", "url": "https://www.uniprot.org/uniprotkb/Q9H8X2" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.30132343", "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": "THIK-1 and THIK-2, a novel subfamily of tandem pore domain K+ channels.", "journal": "J. 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Chem.", "date": "2001", "authors": "Rajan S, Wischmeyer E, Karschin C, Preisig-Muller R, Grzeschik KH, Daut J, Karschin A, Derst C", "reference": { "type": "PubMed", "id": "11060316", "url": "https://pubmed.ncbi.nlm.nih.gov/11060316" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB14-1", "protein_name": "Potassium channel subfamily K member 13", "gene_name": "KCNK13", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9HB15-1", "protein_name": "Potassium channel subfamily K member 12", "gene_name": "KCNK12", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9ERS0-1", "protein_name": "Potassium channel subfamily K member 13", "gene_name": "Kcnk13", "tax_name": "Rat" }, { "uniprot_canonical_ac": "Q9ERS1-1", "protein_name": "Potassium channel subfamily K member 12", "gene_name": "Kcnk12", "tax_name": "Rat" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9HB14", "url": 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Pharmacol.", "date": "2008", "authors": "Gierten J, Ficker E, Bloehs R, Schlomer K, Kathofer S, Scholz E, Zitron E, Kiesecker C, Bauer A, Becker R, Katus HA, Karle CA, Thomas D", "reference": { "type": "PubMed", "id": "18516069", "url": "https://pubmed.ncbi.nlm.nih.gov/18516069" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB14-1", "protein_name": "Potassium channel subfamily K member 13", "gene_name": "KCNK13", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96T55-1", "protein_name": "Potassium channel subfamily K member 16", "gene_name": "KCNK16", "tax_name": "Human" }, { "uniprot_canonical_ac": "O95279-1", "protein_name": "Potassium channel subfamily K member 5", "gene_name": "KCNK5", "tax_name": "Human" }, { "uniprot_canonical_ac": "P57789-1", "protein_name": "Potassium channel subfamily K member 10", "gene_name": "KCNK10", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", 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"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": "Silencing of the tandem pore domain halothane-inhibited K+ channel 2 (THIK2) relies on combined intracellular retention and low intrinsic activity at the plasma membrane.", "journal": "The Journal of biological chemistry", "date": "2013", "authors": "Chatelain FC, Bichet D, Feliciangeli S, Larroque MM, Braud VM, Douguet D, Lesage F", "reference": { "type": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB14-1", "protein_name": "Potassium channel subfamily K member 13", "gene_name": "KCNK13", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9HB15-1", "protein_name": "Potassium channel subfamily K member 12", "gene_name": "KCNK12", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9HB14", "url": "https://www.uniprot.org/uniprotkb/Q9HB14" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 136, "end_pos": 136, "sequence_org": "S", "sequence_mut": "P", "comment": "Increases channel basal activity. Increases the current amplitude. Confers nonlinear I-V relationship, with currents that saturate upon strong membrane depolarization; when associated with D-139. Does not affect channel ion selectivity, pH sensitivity nor inhibition by halothane.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB14", "url": "https://www.uniprot.org/uniprotkb/Q9HB14" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "40307591", "url": "https://pubmed.ncbi.nlm.nih.gov/40307591" } ], "uniprot_canonical_ac": "Q9HB14-1" }, { "start_pos": 139, "end_pos": 139, "sequence_org": "I", "sequence_mut": "D", "comment": "Increases channel basal activity. Increases the current amplitude. Confers nonlinear I-V relationship, with currents that saturate upon strong membrane depolarization; when associated with P-136.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB14", "url": "https://www.uniprot.org/uniprotkb/Q9HB14" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" } ], "uniprot_canonical_ac": "Q9HB14-1" }, { "start_pos": 11, "end_pos": 11, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-12; A-14; A-15 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-12; A-14; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 12, "end_pos": 12, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-14; A-15 and A-16. Results in 174 -fold increase in current amplitude; when associated with P-155; D-158; A-11; A-14; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 131, "end_pos": 131, "sequence_org": "G", "sequence_mut": "E", "comment": "Acts as a dominant negative when it assembles with wild-type subunit, abolishing K(+) flux.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 13, "end_pos": 13, "sequence_org": "S", "sequence_mut": "A", "comment": "Mimics the dephosphorylated state which decreases trafficking from the ER to the plasma membrane.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 13, "end_pos": 13, "sequence_org": "S", "sequence_mut": "D", "comment": "Mimics the phosphorylated state which increases trafficking from the ER to the plasma membrane and leads to increased K(+) currents.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 14, "end_pos": 14, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-15 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 155, "end_pos": 155, "sequence_org": "A", "sequence_mut": "P", "comment": "Increases channel basal activity. Results in 7-fold increase in current amplitude. Displays additive gating effects and results in a 19-fold increase in current amplitude; when associated with D-158. Results in 174-fold increase in current amplitude; when associated with D-158; A-11; A-12; A-14; A-15 and A-16. Does not affect channel ion selectivity, pH sensitivity nor inhibition by halothane.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 158, "end_pos": 158, "sequence_org": "I", "sequence_mut": "D", "comment": "Increases channel basal activity. Results in 6-fold increase in current amplitude. Confers nonlinear I-V relationship, with currents that saturate upon strong membrane depolarization around 0 mV. Displays additive gating effects and results in a 19-fold increase in current amplitude; when associated with P-155. Results in 174-fold increase in current amplitude; when associated with P-155; A-11; A-12; A-14; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 158, "end_pos": 158, "sequence_org": "I", "sequence_mut": "G", "comment": "Does not affect channel basal activity.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 15, "end_pos": 15, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-14 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-14 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 163, "end_pos": 163, "sequence_org": "L", "sequence_mut": "G", "comment": "Does not affect channel basal activity.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 165, "end_pos": 165, "sequence_org": "L", "sequence_mut": "G", "comment": "Does not affect channel basal activity.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 16, "end_pos": 16, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-14 and A-15. Results in 174 -fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-14 and A-15.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" } ], "record_id": "pubmed.24163367", "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": "Tandem pore domain halothane-inhibited K+ channel subunits THIK1 and THIK2 assemble and form active channels.", "journal": "The Journal of biological chemistry", "date": "2014", "authors": "Blin S, Chatelain FC, Feliciangeli S, Kang D, Lesage F, Bichet D", "reference": { "type": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB14-1", "protein_name": "Potassium channel subfamily K member 13", "gene_name": "KCNK13", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9HB15-1", "protein_name": "Potassium channel subfamily K member 12", "gene_name": "KCNK12", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9HB14", "url": "https://www.uniprot.org/uniprotkb/Q9HB14" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 112, "end_pos": 112, "sequence_org": "G", "sequence_mut": "E", "comment": "Acts as a dominant negative when it assembles with wild-type KCNK13 or KCNK12 subunits, abolishing K(+) flux.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB14", "url": "https://www.uniprot.org/uniprotkb/Q9HB14" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB14-1" }, { "start_pos": 11, "end_pos": 11, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-12; A-14; A-15 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-12; A-14; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 12, "end_pos": 12, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-14; A-15 and A-16. Results in 174 -fold increase in current amplitude; when associated with P-155; D-158; A-11; A-14; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 131, "end_pos": 131, "sequence_org": "G", "sequence_mut": "E", "comment": "Acts as a dominant negative when it assembles with wild-type subunit, abolishing K(+) flux.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 14, "end_pos": 14, "sequence_org": "R", "sequence_mut": "A", "comment": "Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-15 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-15 and A-16.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 155, "end_pos": 155, "sequence_org": "A", "sequence_mut": "P", "comment": "Increases channel basal activity. Results in 7-fold increase in current amplitude. Displays additive gating effects and results in a 19-fold increase in current amplitude; when associated with D-158. Results in 174-fold increase in current amplitude; when associated with D-158; A-11; A-12; A-14; A-15 and A-16. Does not affect channel ion selectivity, pH sensitivity nor inhibition by halothane.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB15", "url": "https://www.uniprot.org/uniprotkb/Q9HB15" }, { "database": "PubMed", "id": "24163367", "url": "https://pubmed.ncbi.nlm.nih.gov/24163367" }, { "database": "PubMed", "id": "25148687", "url": "https://pubmed.ncbi.nlm.nih.gov/25148687" } ], "uniprot_canonical_ac": "Q9HB15-1" }, { "start_pos": 158, "end_pos": 158, "sequence_org": "I", "sequence_mut": "D", "comment": "Increases channel basal activity. Results in 6-fold increase in current amplitude. Confers nonlinear I-V relationship, with currents that saturate upon strong membrane depolarization around 0 mV. Displays additive gating effects and results in a 19-fold increase in current amplitude; when associated with P-155. 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Brain Res.", "date": "2002", "authors": "Ozaita Andres, Vega-Saenz de Miera Eleazar", "reference": { "type": "PubMed", "id": "12191490", "url": "https://pubmed.ncbi.nlm.nih.gov/12191490" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9NYG8-1", "protein_name": "Potassium channel subfamily K member 4", "gene_name": "KCNK4", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9NYG8", "url": "https://www.uniprot.org/uniprotkb/Q9NYG8" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.12191490", "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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[] } ] }, { "title": "KIAA1522 potentiates TNFalpha-NFkappaB signaling to antagonize platinum-based chemotherapy in lung adenocarcinoma.", "journal": "Journal of experimental & clinical cancer research : CR", "date": "2020", "authors": "Wang B, Jing T, Jin W, Chen J, Wu C, Wang M, Liu Y", "reference": { "type": "PubMed", "id": "32854746", "url": "https://pubmed.ncbi.nlm.nih.gov/32854746" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9P206-1", "protein_name": "NHS-like protein 3", "gene_name": "NHSL3", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9P206", "url": "https://www.uniprot.org/uniprotkb/Q9P206" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.32854746", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { 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"Asia-Pacific journal of clinical oncology", "date": "2024-06", "authors": "Guo Yuting, Tian She, Li Haiyang, Zuo Shi, Yu Chao, Sun Chengyi", "reference": { "type": "PubMed", "id": "38520660", "url": "https://pubmed.ncbi.nlm.nih.gov/38520660" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9P206-1", "protein_name": "NHS-like protein 3", "gene_name": "NHSL3", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q13886-1", "protein_name": "Krueppel-like factor 9", "gene_name": "KLF9", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9P206", "url": "https://www.uniprot.org/uniprotkb/Q9P206" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.38520660", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", 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"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 Rab11-binding protein RELCH/KIAA1468 controls intracellular cholesterol distribution.", "journal": "The Journal of cell biology", "date": "2018", "authors": "Sobajima T, Yoshimura SI, Maeda T, Miyata H, Miyoshi E, Harada A", "reference": { "type": "PubMed", "id": "29514919", "url": "https://pubmed.ncbi.nlm.nih.gov/29514919" }, "referenced_glycans": [], "referenced_proteins": [ { 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Biophys. Res. Commun.", "date": "1997", "authors": "Zeng Z, Kyaw H, Gakenheimer K R, Augustus M, Fan P, Zhang X, Su K, Carter K C, Li Y", "reference": { "type": "PubMed", "id": "9240447", "url": "https://pubmed.ncbi.nlm.nih.gov/9240447" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9Y4A0-1", "protein_name": "Jerky protein homolog-like", "gene_name": "JRKL", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9Y4A0", "url": "https://www.uniprot.org/uniprotkb/Q9Y4A0" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.9240447", "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": "Human deoxythymidine kinase. I. 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H, Nevo Y, Eriksson S, Elpeleg O", "reference": { "type": "PubMed", "id": "11687801", "url": "https://pubmed.ncbi.nlm.nih.gov/11687801" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O00142-1", "protein_name": "Thymidine kinase 2, mitochondrial", "gene_name": "TK2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q16854-1", "protein_name": "Deoxyguanosine kinase, mitochondrial", "gene_name": "DGUOK", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O00142", "url": "https://www.uniprot.org/uniprotkb/O00142" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.11687801", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 2 } ], "sort_fields": [ 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"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": 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"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": "Identification of residues involved in the substrate specificity of human and murine dCK.", "journal": "Biochemical pharmacology", "date": "2002", "authors": "Usova EV, Eriksson S", "reference": { "type": "PubMed", "id": "12429345", "url": "https://pubmed.ncbi.nlm.nih.gov/12429345" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O00142-1", "protein_name": "Thymidine kinase 2, mitochondrial", "gene_name": "TK2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NWZ5-1", "protein_name": "Uridine-cytidine kinase-like 1", "gene_name": "UCKL1", "tax_name": "Human" }, { "uniprot_canonical_ac": "O95045-1", "protein_name": "Uridine phosphorylase 2", "gene_name": "UPP2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P27707-1", "protein_name": "Deoxycytidine kinase", "gene_name": "DCK", "tax_name": "Human" }, { "uniprot_canonical_ac": "P04183-1", "protein_name": "Thymidine kinase, 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"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": "Molecular insight into mitochondrial DNA depletion syndrome in two patients with novel mutations in the deoxyguanosine kinase and thymidine kinase 2 genes.", "journal": "Molecular genetics and metabolism", "date": "2005", "authors": "Wang L, Limongelli A, Vila MR, Carrara F, Zeviani M, Eriksson S", "reference": { "type": "PubMed", "id": "15639197", "url": "https://pubmed.ncbi.nlm.nih.gov/15639197" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O00142-1", "protein_name": "Thymidine kinase 2, mitochondrial", "gene_name": "TK2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q16854-1", "protein_name": "Deoxyguanosine kinase, mitochondrial", "gene_name": "DGUOK", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O00142", "url": "https://www.uniprot.org/uniprotkb/O00142" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.15639197", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": 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