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"field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Focal Irradiation and Systemic TGF\u03b2 Blockade in Metastatic Breast Cancer.", "journal": "Clinical cancer research : an official journal of the American Association for Cancer Research", "date": "2018-06-01", "authors": "Formenti Silvia C, Lee Percy, Adams Sylvia, Goldberg Judith D, Li Xiaochun, Xie Mike W, Ratikan Josephine A, Felix Carol, Hwang Lin, Faull Kym F, Sayre James W, Hurvitz Sara, Glaspy John A, Comin-Anduix Bego\u00f1a, Demaria Sandra, Schaue D\u00f6rthe, McBride William H", "reference": { "type": "PubMed", "id": "29476019", "url": "https://pubmed.ncbi.nlm.nih.gov/29476019" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UGL1-1", "protein_name": "Lysine-specific demethylase 5B", "gene_name": "KDM5B", "tax_name": "Human" }, { "uniprot_canonical_ac": "P04626-1", "protein_name": "Receptor tyrosine-protein kinase 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"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": "Quantifying the contribution of recessive coding variation to developmental disorders.", "journal": "Science", "date": "2018", "authors": "Martin HC, Jones WD, McIntyre R, Sanchez-Andrade G, Sanderson M, Stephenson JD, Jones CP, Handsaker J, Gallone G, Bruntraeger M, McRae JF, Prigmore E, Short P, Niemi M, Kaplanis J, Radford EJ, Akawi N, Balasubramanian M, Dean J, Horton R, Hulbert A, Johnson DS, Johnson K, Kumar D, Lynch SA, Mehta SG, Morton J, Parker MJ, Splitt M, Turnpenny PD, Vasudevan PC, Wright M, Bassett A, Gerety SS, Wright CF, FitzPatrick DR, Firth HV, Hurles ME, Barrett JC", "reference": { "type": "PubMed", "id": "30409806", "url": "https://pubmed.ncbi.nlm.nih.gov/30409806" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UGL1-1", "protein_name": "Lysine-specific demethylase 5B", "gene_name": "KDM5B", "tax_name": 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"o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "PIDD mediates NF-kappaB activation in response to DNA damage.", "journal": "Cell", "date": "2005", "authors": "Janssens S, Tinel A, Lippens S, Tschopp J", "reference": { "type": "PubMed", "id": "16360037", "url": "https://pubmed.ncbi.nlm.nih.gov/16360037" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB75-1", "protein_name": "p53-induced death domain-containing protein 1", "gene_name": "PIDD1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9Y6K9-1", "protein_name": "NF-kappa-B essential modulator", "gene_name": "IKBKG", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.16360037", "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": "Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway.", "journal": "The EMBO journal", "date": "2007", "authors": "Tinel A, Janssens S, Lippens S, Cuenin S, Logette E, Jaccard B, Quadroni M, Tschopp J", "reference": { "type": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB75-1", "protein_name": "p53-induced death domain-containing protein 1", "gene_name": "PIDD1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P78560-1", "protein_name": "Death domain-containing protein CRADD", "gene_name": "CRADD", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 444, "end_pos": 444, "sequence_org": "H", "sequence_mut": "Q", "comment": "Loss of the proteolytic cleavage producing PIDD-C.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 445, "end_pos": 445, "sequence_org": "F", "sequence_mut": "H", "comment": "Loss of the proteolytic cleavage producing PIDD-C.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 445, "end_pos": 445, "sequence_org": "F", "sequence_mut": "W", "comment": "Loss of the proteolytic cleavage producing PIDD-C.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 446, "end_pos": 446, "sequence_org": "S", "sequence_mut": "A", "comment": "Loss of the proteolytic cleavage producing PIDD-C. Unable to translocate to the nucleus upon DNA damage. No effect on the ability to activate CASP2. Complete loss of proteolytic cleavage; when associated with A-588.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 446, "end_pos": 446, "sequence_org": "S", "sequence_mut": "C", "comment": "No effect on the proteolytic cleavage producing PIDD-C.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 582, "end_pos": 582, "sequence_org": "F", "sequence_mut": "A", "comment": "Loss of the proteolytic cleavage producing PIDD-CC.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 587, "end_pos": 587, "sequence_org": "F", "sequence_mut": "H", "comment": "Loss of the proteolytic cleavage producing PIDD-CC.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 588, "end_pos": 588, "sequence_org": "S", "sequence_mut": "A", "comment": "Loss of the proteolytic cleavage producing PIDD-CC. Loss of interaction with CRADD and of the ability to activate CASP2. No effect on translocation to the nucleus upon DNA damage. Complete loss of proteolytic cleavage; when associated with A-446.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 588, "end_pos": 588, "sequence_org": "S", "sequence_mut": "C", "comment": "No effect on the proteolytic cleavage producing PIDD-CC.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17159900", "url": "https://pubmed.ncbi.nlm.nih.gov/17159900" } ], "uniprot_canonical_ac": "Q9HB75-1" } ], "record_id": "pubmed.17159900", "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": "Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex.", "journal": "Cell", "date": "2007", "authors": "Park HH, Logette E, Raunser S, Cuenin S, Walz T, Tschopp J, Wu H", "reference": { "type": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9HB75-1", "protein_name": "p53-induced death domain-containing protein 1", "gene_name": "PIDD1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P78560-1", "protein_name": "Death domain-containing protein CRADD", "gene_name": "CRADD", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 801, "end_pos": 801, "sequence_org": "L", "sequence_mut": "A", "comment": "No effect on complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 814, "end_pos": 814, "sequence_org": "Y", "sequence_mut": "A", "comment": "Loss of complex assembly with CRADD. Loss of PIDDosome assembly. Loss of CASP2 activation.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 815, "end_pos": 815, "sequence_org": "R", "sequence_mut": "A", "comment": "Partial loss of complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 815, "end_pos": 815, "sequence_org": "R", "sequence_mut": "E", "comment": "Loss of complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 825, "end_pos": 825, "sequence_org": "R", "sequence_mut": "A", "comment": "Partial loss of complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 825, "end_pos": 825, "sequence_org": "R", "sequence_mut": "E", "comment": "Partial loss of complex assembly with CRADD. Decreased PIDDosome assembly. Decreased CASP2 activation.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 826, "end_pos": 826, "sequence_org": "D", "sequence_mut": "K", "comment": "Partial loss of complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 828, "end_pos": 828, "sequence_org": "L", "sequence_mut": "E", "comment": "Loss of complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 830, "end_pos": 830, "sequence_org": "E", "sequence_mut": "K", "comment": "No effect on complex assembly with CRADD.", "evidence": [ { "database": "UniProtKB", "id": "Q9HB75", "url": "https://www.uniprot.org/uniprotkb/Q9HB75" }, { "database": "PubMed", "id": "17289572", "url": "https://pubmed.ncbi.nlm.nih.gov/17289572" } ], "uniprot_canonical_ac": "Q9HB75-1" }, { "start_pos": 837, "end_pos": 837, "sequence_org": "F", "sequence_mut": "D", "comment": "Loss of complex assembly with CRADD. 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controls responsiveness and adaptation to cellular stress.", "journal": "Cell reports", "date": "2024-04-23", "authors": "Magg Vera, Manetto Alessandro, Kopp Katja, Wu Chia Ching, Naghizadeh Mohsen, Lindner Doris, Eke Lucy, Welsch Julia, Kallenberger Stefan M, Schott Johanna, Haucke Volker, Locker Nicolas, Stoecklin Georg, Ruggieri Alessia", "reference": { "type": "PubMed", "id": "38602876", "url": "https://pubmed.ncbi.nlm.nih.gov/38602876" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O75807-1", "protein_name": "Protein phosphatase 1 regulatory subunit 15A", "gene_name": "PPP1R15A", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O75807", "url": "https://www.uniprot.org/uniprotkb/O75807" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.38602876", "abstract": "", "glycosylation": [], "mutagenesis": [], 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"PubMed", "id": "10413516", "url": "https://pubmed.ncbi.nlm.nih.gov/10413516" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P62937-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase A", "gene_name": "PPIA", "tax_name": "Human" }, { "uniprot_canonical_ac": "P51681-1", "protein_name": "C-C chemokine receptor type 5", "gene_name": "CCR5", "tax_name": "Human" }, { "uniprot_canonical_ac": "P61073-1", "protein_name": "C-X-C chemokine receptor type 4", "gene_name": "CXCR4", "tax_name": "Human" }, { "uniprot_canonical_ac": "P01730-1", "protein_name": "T-cell surface glycoprotein CD4", "gene_name": "CD4", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P62937", "url": "https://www.uniprot.org/uniprotkb/P62937" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.10413516", "abstract": "", "glycosylation": [], 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"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": "CCR5 HIV-1 coreceptor activity. Role of cooperativity between residues in N-terminal extracellular and intracellular domains.", "journal": "The Journal of biological chemistry", "date": "1999", "authors": "Wang Z, Lee B, Murray JL, Bonneau F, Sun Y, Schweickart V, Zhang T, Peiper SC", "reference": { "type": "PubMed", "id": "10497202", "url": "https://pubmed.ncbi.nlm.nih.gov/10497202" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P62937-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase A", "gene_name": "PPIA", "tax_name": "Human" }, { "uniprot_canonical_ac": "P51681-1", "protein_name": "C-C chemokine receptor type 5", "gene_name": "CCR5", "tax_name": "Human" }, { "uniprot_canonical_ac": "P61073-1", "protein_name": "C-X-C chemokine receptor type 4", "gene_name": "CXCR4", "tax_name": "Human" }, { "uniprot_canonical_ac": "P01730-1", "protein_name": "T-cell surface glycoprotein CD4", "gene_name": "CD4", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P62937", "url": "https://www.uniprot.org/uniprotkb/P62937" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.10497202", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 4 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 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J. Biochem.", "date": "1990", "authors": "Haendler B, Hofer E", "reference": { "type": "PubMed", "id": "2197089", "url": "https://pubmed.ncbi.nlm.nih.gov/2197089" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P62937-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase A", "gene_name": "PPIA", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P62937", "url": "https://www.uniprot.org/uniprotkb/P62937" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.2197089", "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": 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"table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Cyclophilin A restricts influenza A virus replication through degradation of the M1 protein.", "journal": "PloS one", "date": "2012", "authors": "Liu Xiaoling, Zhao Zhendong, Xu Chongfeng, Sun Lei, Chen Jilong, Zhang Lianfeng, Liu Wenjun", "reference": { "type": "PubMed", "id": "22347431", "url": "https://pubmed.ncbi.nlm.nih.gov/22347431" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P62937-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase A", "gene_name": "PPIA", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, 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Women's health", "date": "2014", "authors": "McConville C, Boyd P, Major I", "reference": { "type": "PubMed", "id": "24741339", "url": "https://pubmed.ncbi.nlm.nih.gov/24741339" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P62937-1", "protein_name": "Peptidyl-prolyl cis-trans isomerase A", "gene_name": "PPIA", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P62937", "url": "https://www.uniprot.org/uniprotkb/P62937" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.24741339", "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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No loss of its interaction with BSG/CD147 or its ability to induce leukocyte chemotaxis. No effect on its interaction with MAP3K5/ASK1. Loss of its ability to negatively regulate oxidative stress-induced apoptosis mediated by MAP3K5/ASK1. Reduced interaction with TARDBP. 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