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                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-170. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-187 and/or E-220.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 170,
                "end_pos": 170,
                "sequence_org": "K",
                "sequence_mut": "E",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-161.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 182,
                "end_pos": 182,
                "sequence_org": "C",
                "sequence_mut": "A",
                "comment": "Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 187,
                "end_pos": 187,
                "sequence_org": "K",
                "sequence_mut": "E",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-191. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-220.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 191,
                "end_pos": 191,
                "sequence_org": "R",
                "sequence_mut": "E",
                "comment": "Mildly reduces binding to KPNB1 and nuclear import. Does not affect binding to KPNA2, IPO7 or TNPO1. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-193. Loss of binding to KPNB1 and nuclear import; when associated with A-193 and A-196.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    },
                    {
                        "database": "PubMed",
                        "id": "24699649",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/24699649"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 210,
                "end_pos": 210,
                "sequence_org": "C",
                "sequence_mut": "A",
                "comment": "Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 215,
                "end_pos": 215,
                "sequence_org": "R",
                "sequence_mut": "E",
                "comment": "Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1. No change in subcellular localization.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 220,
                "end_pos": 220,
                "sequence_org": "R",
                "sequence_mut": "E",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-222 and E-224. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-224. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-187.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 222,
                "end_pos": 222,
                "sequence_org": "N",
                "sequence_mut": "E",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-224.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 224,
                "end_pos": 224,
                "sequence_org": "R",
                "sequence_mut": "E",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-222. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-220. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-228.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    },
                    {
                        "database": "PubMed",
                        "id": "24699649",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/24699649"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 232,
                "end_pos": 235,
                "sequence_org": "DVKK",
                "sequence_mut": "KVEE",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 238,
                "end_pos": 238,
                "sequence_org": "C",
                "sequence_mut": "A",
                "comment": "Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 239,
                "end_pos": 239,
                "sequence_org": "Q",
                "sequence_mut": "E",
                "comment": "Does not affect binding to KPNB1, KPNA2, IPO7, TNPO1 or DNA.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19386897",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19386897"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            }
        ],
        "record_id": "pubmed.19386897",
        "abstract": "",
        "glycosylation": [],
        "snv": [],
        "phosphorylation": [],
        "glycation": [],
        "section_stats": [
            {
                "table_id": "referenced_proteins",
                "table_stats": [
                    {
                        "field": "total",
                        "count": 6
                    }
                ],
                "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
                    },
                    {
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                        "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",
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                    },
                    {
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                        "count": 0
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                    {
                        "field": "o_linked_sites",
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                    {
                        "field": "n_linked_glycan_sites",
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                    }
                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation_predicted",
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                        "count": 0
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                        "field": "total_sites",
                        "count": 0
                    },
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                        "count": 0
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                        "field": "o_linked_sites",
                        "count": 0
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                        "field": "n_linked_glycan_sites",
                        "count": 0
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                        "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": "Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function: potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A.",
        "journal": "Mol. Biol. Cell",
        "date": "2010",
        "authors": "MacPherson MR, Molina P, Souchelnytskyi S, Wernstedt C, Martin-Perez J, Portillo F, Cano A",
        "reference": {
            "type": "PubMed",
            "id": "19923321",
            "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "Q02085-1",
                "protein_name": "Zinc finger protein SNAI1",
                "gene_name": "Snai1",
                "tax_name": "Mouse"
            },
            {
                "uniprot_canonical_ac": "O95863-1",
                "protein_name": "Zinc finger protein SNAI1",
                "gene_name": "SNAI1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P68400-1",
                "protein_name": "Casein kinase II subunit alpha",
                "gene_name": "CSNK2A1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q60737-1",
                "protein_name": "Casein kinase II subunit alpha",
                "gene_name": "Csnk2a1",
                "tax_name": "Mouse"
            }
        ],
        "species": [
            {
                "name": "Mus musculus",
                "taxid": 10090,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q02085",
                        "url": "https://www.uniprot.org/uniprotkb/Q02085"
                    }
                ],
                "common_name": "Mouse",
                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
            }
        ],
        "mutagenesis": [
            {
                "start_pos": 104,
                "end_pos": 104,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Increases protein stability, does not affect repressor activity on E-cadherin/CDH1 promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-107. Impairs phosphorylation in the serine-rich domain/region; when associated with A-92 and A-107. Abolishes phosphorylation at S-96.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "20305697",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20305697"
                    },
                    {
                        "database": "PubMed",
                        "id": "15647282",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15647282"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 107,
                "end_pos": 107,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-111; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-111; A-115 and A-119. Increases protein stability, does not affect repressor activity on E-cadherin promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-104. Impairs phosphorylation in the serine-rich region; when associated with A-92 and A-104. Abolishes phosphorylation at S-96.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "15448698",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15448698"
                    },
                    {
                        "database": "PubMed",
                        "id": "20305697",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20305697"
                    },
                    {
                        "database": "PubMed",
                        "id": "15647282",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15647282"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
                    },
                    {
                        "database": "PubMed",
                        "id": "29059170",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/29059170"
                    },
                    {
                        "database": "PubMed",
                        "id": "25827072",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/25827072"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 107,
                "end_pos": 107,
                "sequence_org": "S",
                "sequence_mut": "E",
                "comment": "Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "15448698",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15448698"
                    },
                    {
                        "database": "PubMed",
                        "id": "20305697",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20305697"
                    },
                    {
                        "database": "PubMed",
                        "id": "15647282",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15647282"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 11,
                "end_pos": 11,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 92,
                "end_pos": 92,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Abolishes CK2 phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in cell survival. Abolishes phosphorylation in the serine-rich region; when associated with A-104 and A-107.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            },
            {
                "start_pos": 92,
                "end_pos": 92,
                "sequence_org": "S",
                "sequence_mut": "E",
                "comment": "Does not affect repressor activity on E-cadherin/CDH1 promoter.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
                    }
                ],
                "uniprot_canonical_ac": "O95863-1"
            }
        ],
        "phosphorylation": [
            {
                "start_pos": 104,
                "end_pos": 104,
                "kinase_uniprot_canonical_ac": "",
                "kinase_gene_name": "",
                "residue": "Ser",
                "comment": "Phosphoserine",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "O95863",
                        "url": "https://www.uniprot.org/uniprotkb/O95863"
                    },
                    {
                        "database": "PubMed",
                        "id": "19923321",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19923321"
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        "title": "Increase of SUMO-1 expression in response to hypoxia: direct interaction with HIF-1alpha in adult mouse brain and heart in vivo.",
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    {
        "title": "Ikaros SUMOylation: switching out of repression.",
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        "authors": "Gomez-del Arco P, Koipally J, Georgopoulos K",
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    {
        "title": "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body.",
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        "authors": "Kuwata T, Nakamura T",
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]
