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D", "date": "2014", "authors": "Rosenberg I., Brynda J., Fabry M., Rezacova P., Pachl P., Simak O.", "reference": { "type": "PubMed", "id": "24531480", "url": "https://pubmed.ncbi.nlm.nih.gov/24531480" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8TCD5-1", "protein_name": "5'(3')-deoxyribonucleotidase, cytosolic type", "gene_name": "NT5C", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8TCD5", "url": "https://www.uniprot.org/uniprotkb/Q8TCD5" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.24531480", "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" ] }, 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[] } ] }, { "title": "Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast ECO1 that is essential for the establishment of sister chromatid cohesion.", "journal": "Nature genetics", "date": "2005", "authors": "Vega H, Waisfisz Q, Gordillo M, Sakai N, Yanagihara I, Yamada M, van Gosliga D, Kayserili H, Xu C, Ozono K, Jabs EW, Inui K, Joenje H", "reference": { "type": "PubMed", "id": "15821733", "url": "https://pubmed.ncbi.nlm.nih.gov/15821733" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3U4-1", "protein_name": "Cohesin subunit SA-2", "gene_name": "STAG2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q7Z5K2-1", "protein_name": "Wings apart-like protein homolog", "gene_name": "WAPL", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8WVM7-1", "protein_name": "Cohesin subunit SA-1", "gene_name": "STAG1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q14683-1", "protein_name": "Structural maintenance of chromosomes 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"The molecular mechanism underlying Roberts syndrome involves loss of ESCO2 acetyltransferase activity.", "journal": "Human molecular genetics", "date": "2008", "authors": "Gordillo M, Vega H, Trainer AH, Hou F, Sakai N, Luque R, Kayserili H, Basaran S, Skovby F, Hennekam RC, Uzielli ML, Schnur RE, Manouvrier S, Chang S, Blair E, Hurst JA, Forzano F, Meins M, Simola KO, Raas-Rothschild A, Schultz RA, McDaniel LD, Ozono K, Inui K, Zou H, Jabs EW", "reference": { "type": "PubMed", "id": "18411254", "url": "https://pubmed.ncbi.nlm.nih.gov/18411254" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3U4-1", "protein_name": "Cohesin subunit SA-2", "gene_name": "STAG2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q7Z5K2-1", "protein_name": "Wings apart-like protein homolog", "gene_name": "WAPL", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8WVM7-1", "protein_name": "Cohesin subunit SA-1", "gene_name": "STAG1", "tax_name": "Human" }, { 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"Q9UQE7-1", "protein_name": "Structural maintenance of chromosomes protein 3", "gene_name": "SMC3", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8N3U4", "url": "https://www.uniprot.org/uniprotkb/Q8N3U4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.18411254", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 11 } ], "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": "Cohesin acetyltransferase Esco2 is a cell viability factor and is required for cohesion in pericentric heterochromatin.", "journal": "The EMBO journal", "date": "2012", "authors": "Whelan G, Kreidl E, Wutz G, Egner A, Peters JM, Eichele G", "reference": { "type": "PubMed", "id": "22101327", "url": "https://pubmed.ncbi.nlm.nih.gov/22101327" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3U4-1", "protein_name": "Cohesin subunit SA-2", "gene_name": "STAG2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q7Z5K2-1", "protein_name": "Wings apart-like protein homolog", "gene_name": "WAPL", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8WVM7-1", "protein_name": "Cohesin subunit SA-1", "gene_name": "STAG1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q14683-1", "protein_name": "Structural maintenance of chromosomes protein 1A", "gene_name": "SMC1A", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q29RF7-1", "protein_name": "Sister chromatid cohesion protein PDS5 homolog A", "gene_name": "PDS5A", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q96FF9-1", "protein_name": "Sororin", "gene_name": "CDCA5", "tax_name": "Human" }, { "uniprot_canonical_ac": "O60216-1", "protein_name": "Double-strand-break repair protein rad21 homolog", "gene_name": "RAD21", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9NTI5-1", "protein_name": "Sister chromatid cohesion protein PDS5 homolog B", "gene_name": "PDS5B", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q56NI9-1", "protein_name": "N-acetyltransferase ESCO2", "gene_name": "ESCO2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q5FWF5-1", "protein_name": "N-acetyltransferase ESCO1", "gene_name": "ESCO1", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q9UQE7-1", "protein_name": "Structural 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{ "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": "De novo loss-of-function variants in STAG2 are associated with developmental delay, microcephaly, and congenital anomalies.", "journal": "American journal of medical genetics. Part A", "date": "2017", "authors": "Mullegama SV, Klein SD, Mulatinho MV, Senaratne TN, Singh K, Nguyen DC, Gallant NM, Strom SP, Ghahremani S, Rao NP, Martinez-Agosto JA", "reference": { "type": "PubMed", "id": "28296084", "url": "https://pubmed.ncbi.nlm.nih.gov/28296084" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3U4-1", "protein_name": "Cohesin subunit SA-2", "gene_name": "STAG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8N3U4", "url": "https://www.uniprot.org/uniprotkb/Q8N3U4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.28296084", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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}, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 } ], "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", 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Hum. Genet.", "date": "2019", "authors": "Aoi H, Lei M, Mizuguchi T, Nishioka N, Goto T, Miyama S, Suzuki T, Iwama K, Uchiyama Y, Mitsuhashi S, Itakura A, Takeda S, Matsumoto N", "reference": { "type": "PubMed", "id": "30765867", "url": "https://pubmed.ncbi.nlm.nih.gov/30765867" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8N3U4-1", "protein_name": "Cohesin subunit SA-2", "gene_name": "STAG2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q8N3U4", "url": "https://www.uniprot.org/uniprotkb/Q8N3U4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.30765867", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ 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Attenuation in Severe COVID-19 Cases: From Hematopoietic Stem Cell Recruitment and Chemotaxis to Thrombo-inflammation.", "journal": "Stem cell reviews and reports", "date": "2021", "authors": "Lintzmaier Petiz L, Glaser T, Scharfstein J, Ratajczak MZ, Ulrich H", "reference": { "type": "PubMed", "id": "33575962", "url": "https://pubmed.ncbi.nlm.nih.gov/33575962" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q15391-1", "protein_name": "P2Y purinoceptor 14", "gene_name": "P2RY14", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q15391", "url": "https://www.uniprot.org/uniprotkb/Q15391" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.33575962", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", 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"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A.", "journal": "Mol. Biol. Cell", "date": "2006", "authors": "Yamasaki A, Tani K, Yamamoto A, Kitamura N, Komada M", "reference": { "type": "PubMed", "id": "16957052", "url": "https://pubmed.ncbi.nlm.nih.gov/16957052" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O94979-1", "protein_name": "Protein transport protein Sec31A", "gene_name": "SEC31A", "tax_name": "Human" }, { "uniprot_canonical_ac": "P55735-1", "protein_name": "Protein SEC13 homolog", "gene_name": "SEC13", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8WUM4-1", "protein_name": "Programmed cell death 6-interacting protein", "gene_name": "PDCD6IP", "tax_name": "Human" }, { "uniprot_canonical_ac": "O75340-1", "protein_name": "Programmed cell death protein 6", "gene_name": "PDCD6", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O94979", "url": "https://www.uniprot.org/uniprotkb/O94979" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 114, "end_pos": 114, "sequence_org": "E", "sequence_mut": "A", "comment": "Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; 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Commun.", "date": "2007", "authors": "Shibata H, Suzuki H, Yoshida H, Maki M", "reference": { "type": "PubMed", "id": "17196169", "url": "https://pubmed.ncbi.nlm.nih.gov/17196169" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O94979-1", "protein_name": "Protein transport protein Sec31A", "gene_name": "SEC31A", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "O94979", "url": "https://www.uniprot.org/uniprotkb/O94979" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.17196169", "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": "Structural analysis of the complex between penta-EF-hand ALG-2 protein and Sec31A peptide reveals a novel target recognition mechanism of ALG-2.", "journal": "Int. 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Genet.", "date": "2014", "authors": "Girolami F, Iascone M, Tomberli B, Bardi S, Benelli M, Marseglia G, Pescucci C, Pezzoli L, Sana ME, Basso C, Marziliano N, Merlini PA, Fornaro A, Cecchi F, Torricelli F, Olivotto I", "reference": { "type": "PubMed", "id": "25173926", "url": "https://pubmed.ncbi.nlm.nih.gov/25173926" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q5VST9-1", "protein_name": "Obscurin", "gene_name": "OBSCN", "tax_name": "Human" }, { "uniprot_canonical_ac": "P35609-1", "protein_name": "Alpha-actinin-2", "gene_name": "ACTN2", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q8WZ42-1", "protein_name": "Titin", "gene_name": "TTN", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q5VST9", "url": "https://www.uniprot.org/uniprotkb/Q5VST9" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": 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Hu J, Li G, Qu L, He Q, Lou Y, Song Q, Ma D, Chen Y", "reference": { "type": "PubMed", "id": "25484098", "url": "https://pubmed.ncbi.nlm.nih.gov/25484098" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9BUL5-1", "protein_name": "PHD finger protein 23", "gene_name": "PHF23", "tax_name": "Human" }, { "uniprot_canonical_ac": "Q6UWE0-1", "protein_name": "E3 ubiquitin-protein ligase LRSAM1", "gene_name": "LRSAM1", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9BUL5", "url": "https://www.uniprot.org/uniprotkb/Q9BUL5" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.25484098", "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 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter.", "journal": "The Journal of biological chemistry", "date": "1999", "authors": "Prefontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Hache RJ", "reference": { "type": "PubMed", "id": "10480874", "url": "https://pubmed.ncbi.nlm.nih.gov/10480874" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P09086-1", "protein_name": "POU domain, class 2, transcription factor 2", "gene_name": "POU2F2", "tax_name": "Human" }, { "uniprot_canonical_ac": "P14859-1", "protein_name": "POU domain, class 2, transcription factor 1", "gene_name": "POU2F1", "tax_name": "Human" }, { "uniprot_canonical_ac": "P06536-1", "protein_name": "Glucocorticoid receptor", "gene_name": "Nr3c1", "tax_name": "Rat" } ], "species": [ { 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