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mouse cardiac neural crest cells condensation and outflow tract septation.", "journal": "eLife", "date": "2020", "authors": "Darrigrand JF, Valente M, Comai G, Martinez P, Petit M, Nishinakamura R, Osorio DS, Renault G, Marchiol C, Ribes V, Cadot B", "reference": { "type": "PubMed", "id": "32105214", "url": "https://pubmed.ncbi.nlm.nih.gov/32105214" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q3TP92-1", "protein_name": "CTD nuclear envelope phosphatase 1", "gene_name": "Ctdnep1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q3TP92", "url": "https://www.uniprot.org/uniprotkb/Q3TP92" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.32105214", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": 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Sci.", "date": "1983", "authors": "Fey G H, Wiebauer K, Domdey H", "reference": { "type": "PubMed", "id": "6609661", "url": "https://pubmed.ncbi.nlm.nih.gov/6609661" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P01027-1", "protein_name": "Complement C3", "gene_name": "C3", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "P01027", "url": "https://www.uniprot.org/uniprotkb/P01027" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.6609661", "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": "Characterization of the mRNA and cloned cDNA specifying the third component of mouse complement.", "journal": "Proc. 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Chem.", "date": "1994", "authors": "Kawano T, Kozutsumi Y, Kawasaki T, Suzuki A", "reference": { "type": "PubMed", "id": "8132639", "url": "https://pubmed.ncbi.nlm.nih.gov/8132639" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q61419-1", "protein_name": "Cytidine monophosphate-N-acetylneuraminic acid hydroxylase", "gene_name": "Cmah", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q61419", "url": "https://www.uniprot.org/uniprotkb/Q61419" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.8132639", "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": "A naturally occurring 46-amino acid deletion of cytidine monophospho-N-acetylneuraminic acid hydroxylase leads to a change in the intracellular distribution of the protein.", "journal": "Glycoconj. 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"journal": "The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society", "date": "2008", "authors": "Bothe MK, Braun J, Mundhenk L, Gruber AD", "reference": { "type": "PubMed", "id": "18285349", "url": "https://pubmed.ncbi.nlm.nih.gov/18285349" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q6Q473-1", "protein_name": "Calcium-activated chloride channel regulator 4A", "gene_name": "Clca4a", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q6Q473", "url": "https://www.uniprot.org/uniprotkb/Q6Q473" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.18285349", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } 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Neurosci.", "date": "2006", "authors": "Lepicard Eve M, Mizuno Keiko, Antunes-Martins Ana, von Hertzen Laura S J, Giese K Peter", "reference": { "type": "PubMed", "id": "16819996", "url": "https://pubmed.ncbi.nlm.nih.gov/16819996" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q6QWF9-1", "protein_name": "Calcium/calmodulin-dependent protein kinase II inhibitor 1", "gene_name": "Camk2n1", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q6QWF9", "url": "https://www.uniprot.org/uniprotkb/Q6QWF9" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.16819996", "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": "Regulation of Ca2+/calmodulin kinase II inhibitor alpha (CaMKIINalpha) in virus-infected mouse brain.", "journal": "Biochem. 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"o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "CHST2-mediated sulfation of MECA79 antigens is critical for breast cancer cell migration and metastasis.", "journal": "Cell death & disease", "date": "2023-04-24", "authors": "Zhang Dan, Zhang Yihong, Zou Xiuqun, Li Mengying, Zhang Hui, Du Yaning, Wang Jiamin, Peng Chicheng, Dong Chunyan, Hou Zhaoyuan", "reference": { "type": "PubMed", "id": "37095090", "url": "https://pubmed.ncbi.nlm.nih.gov/37095090" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q80WV3-1", "protein_name": "Carbohydrate sulfotransferase 2", "gene_name": "Chst2", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q80WV3", "url": "https://www.uniprot.org/uniprotkb/Q80WV3" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.37095090", "abstract": "", "glycosylation": 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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 }, { 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Mol. Life Sci.", "date": "2012", "authors": "Krug SM, Gunzel D, Conrad MP, Rosenthal R, Fromm A, Amasheh S, Schulzke JD, Fromm M", "reference": { "type": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q8BXA6-1", "protein_name": "Claudin-17", "gene_name": "Cldn17", "tax_name": "Mouse" }, { "uniprot_canonical_ac": "P56750-1", "protein_name": "Claudin-17", "gene_name": "CLDN17", "tax_name": "Human" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8BXA6", "url": "https://www.uniprot.org/uniprotkb/Q8BXA6" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "mutagenesis": [ { "start_pos": 149, "end_pos": 149, "sequence_org": "Y", "sequence_mut": "A", "comment": "Increased transepithelial resistance. No effect on localization to cell-cell junctions.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 154, "end_pos": 154, "sequence_org": "H", "sequence_mut": "A", "comment": "Loss of anion selectivity. Strongly increased permeabilities not only for chloride, but also for sodium and the larger anions, including pyruvate, nitrate and thiocyanate. No effect on localization to cell-cell junctions.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 31, "end_pos": 31, "sequence_org": "R", "sequence_mut": "E", "comment": "Decreased transepithelial resistance and anion selectivity. 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No effect on transepithelial resistance.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 59, "end_pos": 59, "sequence_org": "R", "sequence_mut": "A", "comment": "No effect on transepithelial resistance, nor on anion selectivity. Increased permeability for thiocyanate.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 61, "end_pos": 61, "sequence_org": "R", "sequence_mut": "A", "comment": "Decreased anion selectivity. No effect on transepithelial resistance.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 65, "end_pos": 65, "sequence_org": "K", "sequence_mut": "A", "comment": "Reduced channel formation ability. Increased transepithelial resistance. Loss of anion selectivity in favor of cation selectivity.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 65, "end_pos": 65, "sequence_org": "K", "sequence_mut": "E", "comment": "No effect on channel formation ability. Loss of anion selectivity in favor of cation selectivity. No effect on transepithelial resistance.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 65, "end_pos": 65, "sequence_org": "K", "sequence_mut": "R", "comment": "Strongly reduced channel formation ability. Increased transepithelial resistance. Loss of anion selectivity in favor of cation selectivity.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" }, { "start_pos": 68, "end_pos": 68, "sequence_org": "S", "sequence_mut": "E", "comment": "Increased transepithelial resistance. Loss of anion selectivity in favor of cation (sodium) selectivity.", "evidence": [ { "database": "UniProtKB", "id": "P56750", "url": "https://www.uniprot.org/uniprotkb/P56750" }, { "database": "PubMed", "id": "22402829", "url": "https://pubmed.ncbi.nlm.nih.gov/22402829" } ], "uniprot_canonical_ac": "P56750-1" } ], "record_id": "pubmed.22402829", "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 }, { 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"count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "CHD1L Regulated PARP1-Driven Pluripotency and Chromatin Remodeling During the Early-Stage Cell Reprogramming.", "journal": "Stem cells (Dayton, Ohio)", "date": "2015", "authors": "Jiang BH, Chen WY, Li HY, Chien Y, Chang WC, Hsieh PC, Wu P, Chen CY, Song HY, Chien CS, Sung YJ, Chiou SH", "reference": { "type": "PubMed", "id": "26201266", "url": "https://pubmed.ncbi.nlm.nih.gov/26201266" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9CXF7-1", "protein_name": "ATP-dependent chromatin remodeler CHD1L", "gene_name": "Chd1l", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9CXF7", "url": "https://www.uniprot.org/uniprotkb/Q9CXF7" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], 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M, Chen L, Ma NF, Chow RK, Li Y, Song Y, Chan TH, Fang S, Yang X, Xi S, Jiang L, Li Y, Zeng TT, Li Y, Yuan YF, Guan XY", "reference": { "type": "PubMed", "id": "27100146", "url": "https://pubmed.ncbi.nlm.nih.gov/27100146" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9CXF7-1", "protein_name": "ATP-dependent chromatin remodeler CHD1L", "gene_name": "Chd1l", "tax_name": "Mouse" } ], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q9CXF7", "url": "https://www.uniprot.org/uniprotkb/Q9CXF7" } ], "common_name": "Mouse", "glygen_name": "Mouse", "reference_species": "Mus musculus [10090]" } ], "record_id": "pubmed.27100146", "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", 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