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"journal": "Bioengineered", "date": "2021", "authors": "Zheng Y, Zeng J, Xia H, Wang X, Chen H, Huang L, Zeng C", "reference": { "type": "PubMed", "id": "34511033", "url": "https://pubmed.ncbi.nlm.nih.gov/34511033" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q6IMN6-1", "protein_name": "Caprin-2", "gene_name": "CAPRIN2", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q6IMN6", "url": "https://www.uniprot.org/uniprotkb/Q6IMN6" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.34511033", "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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Allows FBXO5 degradation in the absence of CDK4 inhibitor.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "16921029", "url": "https://pubmed.ncbi.nlm.nih.gov/16921029" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" }, { "database": "PubMed", "id": "29875408", "url": "https://pubmed.ncbi.nlm.nih.gov/29875408" } ], "uniprot_canonical_ac": "Q9UKT4-1" } ], "record_id": "pubmed.16921029", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "DNA damage triggers p21WAF1-dependent Emi1 down-regulation that maintains G2 arrest.", "journal": "Mol. Biol. Cell", "date": "2009", "authors": "Lee Jinho, Kim Jin Ah, Barbier Valerie, Fotedar Arun, Fotedar Rati", "reference": { "type": "PubMed", "id": "19211842", "url": "https://pubmed.ncbi.nlm.nih.gov/19211842" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UKT4-1", "protein_name": "F-box only protein 5", "gene_name": "FBXO5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.19211842", "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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"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": "Bcr-Abl-induced tyrosine phosphorylation of Emi1 to stabilize Skp2 protein via inhibition of ubiquitination in chronic myeloid leukemia cells.", "journal": "Journal of cellular physiology", "date": "2011", "authors": "Chen JY, Wang MC, Hung WC", "reference": { "type": "PubMed", "id": "20717963", "url": "https://pubmed.ncbi.nlm.nih.gov/20717963" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UKT4-1", "protein_name": "F-box only protein 5", "gene_name": "FBXO5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "phosphorylation": [ { "start_pos": 142, "end_pos": 142, "kinase_uniprot_canonical_ac": "P12931-1", "kinase_gene_name": "SRC", "residue": "Tyr", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "Q9UKT4", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q9UKT4" }, { "database": "PubMed", "id": "20717963", "url": "https://pubmed.ncbi.nlm.nih.gov/20717963" } ], "site_lbl": "Tyr142", "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 142, "end_pos": 142, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Tyr", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "Q9UKT4", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q9UKT4" }, { "database": "PubMed", "id": "20717963", "url": 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"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": "Emi1 preferentially inhibits ubiquitin chain elongation by the anaphase-promoting complex.", "journal": "Nature cell biology", "date": "2013", "authors": "Wang W, Kirschner MW", "reference": { "type": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UKT4-1", "protein_name": "F-box only protein 5", "gene_name": "FBXO5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 322, "end_pos": 325, "sequence_org": "RTPL", "sequence_mut": "ATPA", "comment": "Does not affect inhibition of UBE2S-catalyzed chain elongation. Efficiently inhibits the degradation of PTTG1 at relatively high concentration. Reduces the competitive ability of FBXO5 to inhibit the association of PTTG1 to APC. Cannot compete with the APC substrate for APC binding. Decreases inhibition of CCNB1 ubiquitination by UBE2C.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 401, "end_pos": 401, "sequence_org": "C", "sequence_mut": "S", "comment": "Reduced inhibition of APC. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly; when associated with S-401. Does not affect inhibition of UBE2S-catalyzed chain elongation. Reduces the competitive ability of FBXO5 to inhibit the association of securin to APC. Can still compete with the APC substrate for APC binding. Fails to inhibit ubiquitin chain assembly by UBE2C or mono-ubiquitination by UBE2D1. Largely abolishes the inhibitory activity against protein degradation. Fails to inactivate APC-FZR1 complex. Allows FBXO5 degradation in the absence of CDK4 inhibitor.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "16921029", "url": "https://pubmed.ncbi.nlm.nih.gov/16921029" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" }, { "database": "PubMed", "id": "29875408", "url": "https://pubmed.ncbi.nlm.nih.gov/29875408" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 406, "end_pos": 406, "sequence_org": "C", "sequence_mut": "S", "comment": "Does not affect the inhibitory activity against chain assembly; when associated with S-401.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 444, "end_pos": 445, "sequence_org": "LR", "sequence_mut": "AA", "comment": "Loses inhibitory activity on UBE2S-catalyzed chain elongation.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" } ], "uniprot_canonical_ac": "Q9UKT4-1" } ], "record_id": "pubmed.23708001", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", 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"count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown.", "journal": "Nature structural & molecular biology", "date": "2013", "authors": "Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA", "reference": { "type": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UKT4-1", "protein_name": "F-box only protein 5", "gene_name": "FBXO5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "mutagenesis": [ { "start_pos": 322, "end_pos": 325, "sequence_org": "RTPL", "sequence_mut": "ATPA", "comment": "Does not affect inhibition of UBE2S-catalyzed chain elongation. Efficiently inhibits the degradation of PTTG1 at relatively high concentration. Reduces the competitive ability of FBXO5 to inhibit the association of PTTG1 to APC. Cannot compete with the APC substrate for APC binding. Decreases inhibition of CCNB1 ubiquitination by UBE2C.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 339, "end_pos": 345, "sequence_org": "KDAQTKL", "sequence_mut": "", "comment": "Impairs CCNB1 ubiquitination by UBE2C; when associated with 356-Y--R-358 del.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 345, "end_pos": 345, "sequence_org": "L", "sequence_mut": "A", "comment": "Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 346, "end_pos": 355, "sequence_org": "SNQGDQKGST", "sequence_mut": "", "comment": "Inhibits CCNB1 ubiquitination by UBE2C. Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with A-345; A-356 and A-358.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 356, "end_pos": 356, "sequence_org": "Y", "sequence_mut": "A", "comment": "Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 356, "end_pos": 358, "sequence_org": "YSR", "sequence_mut": "", "comment": "Impairs CCNB1 ubiquitination by UBE2C; when associated with 339-K--L-345 del.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 358, "end_pos": 358, "sequence_org": "R", "sequence_mut": "A", "comment": "Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 375, "end_pos": 375, "sequence_org": "L", "sequence_mut": "A", "comment": "Decreases UBE2C-mediated ubiquitination.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 376, "end_pos": 376, "sequence_org": "K", "sequence_mut": "A", "comment": "Decreases UBE2C-mediated ubiquitination.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 393, "end_pos": 393, "sequence_org": "R", "sequence_mut": "A", "comment": "Decreases UBE2C-mediated ubiquitination.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "23708605", "url": "https://pubmed.ncbi.nlm.nih.gov/23708605" } ], "uniprot_canonical_ac": "Q9UKT4-1" }, { "start_pos": 409, "end_pos": 409, "sequence_org": "C", "sequence_mut": "A", "comment": "Decreases UBE2C-mediated ubiquitination.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": 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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": 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Osteogenic Differentiation of Human Periodontal Ligament Mesenchymal Stem Cells.", "journal": "BioMed research international", "date": "2018", "authors": "Liu L, Liu K, Yan Y, Chu Z, Tang Y, Tang C", "reference": { "type": "PubMed", "id": "29850565", "url": "https://pubmed.ncbi.nlm.nih.gov/29850565" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UKT4-1", "protein_name": "F-box only protein 5", "gene_name": "FBXO5", "tax_name": "Human" } ], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" } ], "common_name": "Human", "glygen_name": "Human", "reference_species": "Homo sapiens [9606]" } ], "record_id": "pubmed.29850565", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], 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"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": "EMI1 switches from being a substrate to an inhibitor of APC/C(CDH1) to start the cell cycle.", "journal": "Nature", "date": "2018", "authors": "Cappell SD, Mark KG, Garbett D, Pack LR, Rape M, Meyer T", "reference": { "type": "PubMed", "id": "29875408", "url": "https://pubmed.ncbi.nlm.nih.gov/29875408" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q9UKT4-1", "protein_name": "F-box only protein 5", "gene_name": 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Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly; when associated with S-401. Does not affect inhibition of UBE2S-catalyzed chain elongation. Reduces the competitive ability of FBXO5 to inhibit the association of securin to APC. Can still compete with the APC substrate for APC binding. Fails to inhibit ubiquitin chain assembly by UBE2C or mono-ubiquitination by UBE2D1. Largely abolishes the inhibitory activity against protein degradation. Fails to inactivate APC-FZR1 complex. Allows FBXO5 degradation in the absence of CDK4 inhibitor.", "evidence": [ { "database": "UniProtKB", "id": "Q9UKT4", "url": "https://www.uniprot.org/uniprotkb/Q9UKT4" }, { "database": "PubMed", "id": "16921029", "url": "https://pubmed.ncbi.nlm.nih.gov/16921029" }, { "database": "PubMed", "id": "23708001", "url": "https://pubmed.ncbi.nlm.nih.gov/23708001" }, { "database": "PubMed", "id": "29875408", "url": "https://pubmed.ncbi.nlm.nih.gov/29875408" } ], "uniprot_canonical_ac": "Q9UKT4-1" } ], "record_id": "pubmed.29875408", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 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