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        "title": "Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors.",
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    {
        "title": "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation.",
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        "authors": "Ebisawa T, Fukuchi M, Murakami G, Chiba T, Tanaka K, Imamura T, Miyazono K",
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        "abstract": "",
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    {
        "title": "Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-beta signaling by Smad7.",
        "journal": "The Journal of biological chemistry",
        "date": "2003",
        "authors": "Tajima Y, Goto K, Yoshida M, Shinomiya K, Sekimoto T, Yoneda Y, Miyazono K, Imamura T",
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                    {
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                ],
                "sort_fields": []
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            {
                "table_id": "phosphorylation",
                "table_stats": [
                    {
                        "field": "total",
                        "count": 12
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                    {
                        "field": "total_sites",
                        "count": 6
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                ],
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            },
            {
                "table_id": "glycosylation_reported",
                "table_stats": [
                    {
                        "field": "total",
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                    {
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                        "field": "n_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "o_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "n_linked_glycans",
                        "count": 0
                    },
                    {
                        "field": "o_linked_glycans",
                        "count": 0
                    }
                ],
                "sort_fields": []
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            {
                "table_id": "glycosylation_reported_with_glycan",
                "table_stats": [
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                        "field": "total",
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                    {
                        "field": "total_sites",
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                    {
                        "field": "n_linked_sites",
                        "count": 0
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                    {
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                    {
                        "field": "n_linked_glycan_sites",
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                    {
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                    {
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                    {
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                ],
                "sort_fields": []
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            {
                "table_id": "glycosylation_predicted",
                "table_stats": [
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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",
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                    {
                        "field": "total_sites",
                        "count": 0
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                    {
                        "field": "n_linked_sites",
                        "count": 0
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                    {
                        "field": "o_linked_sites",
                        "count": 0
                    },
                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "o_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "n_linked_glycans",
                        "count": 0
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                    {
                        "field": "o_linked_glycans",
                        "count": 0
                    }
                ],
                "sort_fields": []
            }
        ]
    },
    {
        "title": "Cell cycle-dependent expression of centrosomal ninein-like protein in human cells is regulated by the anaphase-promoting complex.",
        "journal": "J. Biol. Chem.",
        "date": "2007",
        "authors": "Wang Y, Zhan Q",
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            "id": "17403670",
            "url": "https://pubmed.ncbi.nlm.nih.gov/17403670"
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            {
                "uniprot_canonical_ac": "Q12834-1",
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                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9Y2I6-1",
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                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9UM11-1",
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                "gene_name": "FZR1",
                "tax_name": "Human"
            }
        ],
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            {
                "name": "Homo sapiens",
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                    {
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                ],
                "common_name": "Human",
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                "reference_species": "Homo sapiens [9606]"
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        ],
        "mutagenesis": [
            {
                "start_pos": 495,
                "end_pos": 497,
                "sequence_org": "KEN",
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                "comment": "Disrupts binding to CDC20 and FZR1 and prevents ubiquitination and subsequent degradation of NINL; when associated with 633-A--A-636.",
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                    {
                        "database": "UniProtKB",
                        "id": "Q9Y2I6",
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                    {
                        "database": "PubMed",
                        "id": "17403670",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/17403670"
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                ],
                "uniprot_canonical_ac": "Q9Y2I6-1"
            },
            {
                "start_pos": 633,
                "end_pos": 636,
                "sequence_org": "RTQL",
                "sequence_mut": "AAAA",
                "comment": "Disrupts binding to CDC20 and FZR1 and prevents ubiquitination and subsequent degradation of NINL; when associated with 495-A--A-497.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9Y2I6",
                        "url": "https://www.uniprot.org/uniprotkb/Q9Y2I6"
                    },
                    {
                        "database": "PubMed",
                        "id": "17403670",
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                ],
                "uniprot_canonical_ac": "Q9Y2I6-1"
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        ],
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        "abstract": "",
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        "phosphorylation": [],
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        "section_stats": [
            {
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                    {
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                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation",
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                        "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": [
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                        "field": "total",
                        "count": 0
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                    {
                        "field": "total_sites",
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                ],
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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
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                ],
                "sort_fields": []
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            {
                "table_id": "glycosylation_reported_with_glycan",
                "table_stats": [
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                    {
                        "field": "o_linked_sites",
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                        "field": "n_linked_glycan_sites",
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                    {
                        "field": "o_linked_glycan_sites",
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                        "field": "o_linked_glycan_sites",
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                        "field": "o_linked_glycans",
                        "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
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                    {
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                        "count": 0
                    },
                    {
                        "field": "o_linked_glycans",
                        "count": 0
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                ],
                "sort_fields": []
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        ]
    },
    {
        "title": "HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is essential for mitotic progression.",
        "journal": "Cancer Res.",
        "date": "2008",
        "authors": "Lee YJ, Kim EH, Lee JS, Jeoung D, Bae S, Kwon SH, Lee YS",
        "reference": {
            "type": "PubMed",
            "id": "18794143",
            "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
        },
        "referenced_glycans": [],
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            {
                "uniprot_canonical_ac": "Q12834-1",
                "protein_name": "Cell division cycle protein 20 homolog",
                "gene_name": "CDC20",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q13257-1",
                "protein_name": "Mitotic spindle assembly checkpoint protein MAD2A",
                "gene_name": "MAD2L1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P53350-1",
                "protein_name": "Serine/threonine-protein kinase PLK1",
                "gene_name": "PLK1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9Y297-1",
                "protein_name": "F-box/WD repeat-containing protein 1A",
                "gene_name": "BTRC",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q00613-1",
                "protein_name": "Heat shock factor protein 1",
                "gene_name": "HSF1",
                "tax_name": "Human"
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        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q12834",
                        "url": "https://www.uniprot.org/uniprotkb/Q12834"
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
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        ],
        "mutagenesis": [
            {
                "start_pos": 216,
                "end_pos": 216,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Does not change interaction with XRCC5 and XRCC6. No PLK1-induced phosphorylation in mitosis. Inhibits PLK1-stimulated ubiquitinylation. Increased protein stability.",
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                    {
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                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                        "id": "26359349",
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                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
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            {
                "start_pos": 216,
                "end_pos": 216,
                "sequence_org": "S",
                "sequence_mut": "E",
                "comment": "Does not change interaction with XRCC5 and XRCC6. No change in spindle pole localization. Increases weakly PLK1-stimulated ubiquitinylation. No change in protein stability. Increased interaction with BTRC.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                    {
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                        "id": "26359349",
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                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 216,
                "end_pos": 216,
                "sequence_org": "S",
                "sequence_mut": "N",
                "comment": "Decreased spindle pole localization. Decreased interaction with BTRC. Increased protein stability.",
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                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
                    },
                    {
                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
                    }
                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 230,
                "end_pos": 230,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "No phosphorylation. No change in PLK1-induced phosphorylation in mitosis. No change in DNA-binding activity upon heat shock. Decreased transcriptional activity upon heat shock.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                    {
                        "database": "PubMed",
                        "id": "11447121",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/11447121"
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                    {
                        "database": "PubMed",
                        "id": "12665592",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12665592"
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                    {
                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 303,
                "end_pos": 303,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "No phosphorylation nor sumoylation. No change in nuclear stress granules subcellular location upon heat shock. Loss of colocalization with SUMO1 to nuclear stress granules upon heat shock. Slight decrease in transcriptional activity on heat treatment. No change in PLK1-induced phosphorylation in mitosis, induces derepression of transcription activation at control temperature, abolishes sumoylation and induces 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-307.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                    {
                        "database": "PubMed",
                        "id": "8946918",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/8946918"
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                    {
                        "database": "PubMed",
                        "id": "9535852",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9535852"
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                    {
                        "database": "PubMed",
                        "id": "12665592",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12665592"
                    },
                    {
                        "database": "PubMed",
                        "id": "9121459",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9121459"
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                    {
                        "database": "PubMed",
                        "id": "12646186",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12646186"
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                    {
                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 307,
                "end_pos": 307,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "No phosphorylation. Does not reduce Ser-303 phosphorylation. 1.5% increase in transcriptional activity on heat-treatment. No change in PLK1-induced phosphorylation in mitosis, induces derepression of transcription activation at control temperature, abolishes sumoylation and induces 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                    {
                        "database": "PubMed",
                        "id": "8946918",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/8946918"
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                    {
                        "database": "PubMed",
                        "id": "9535852",
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                        "id": "12665592",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12665592"
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                    {
                        "database": "PubMed",
                        "id": "9121459",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/9121459"
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                    {
                        "database": "PubMed",
                        "id": "12646186",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/12646186"
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                    {
                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
            },
            {
                "start_pos": 419,
                "end_pos": 419,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Does not change interaction with XRCC5 and XRCC6. Decreased nuclear localization upon heat shock. Strongly decreases PLK1-induced phosphorylation. No change in PLK1-induced phosphorylation in mitosis.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
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                    {
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                        "id": "26359349",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/26359349"
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                    {
                        "database": "PubMed",
                        "id": "15661742",
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                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "uniprot_canonical_ac": "Q00613-1"
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                "start_pos": 216,
                "end_pos": 216,
                "kinase_uniprot_canonical_ac": "P53350-1",
                "kinase_gene_name": "PLK1",
                "residue": "Ser",
                "comment": "",
                "evidence": [
                    {
                        "database": "iPTMnet",
                        "id": "Q00613",
                        "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q00613"
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                    {
                        "database": "PubMed",
                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                ],
                "site_lbl": "Ser216",
                "uniprot_canonical_ac": "Q00613-1"
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            {
                "start_pos": 216,
                "end_pos": 216,
                "kinase_uniprot_canonical_ac": "",
                "kinase_gene_name": "",
                "residue": "Ser",
                "comment": "Phosphoserine; by PLK1",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q00613",
                        "url": "https://www.uniprot.org/uniprotkb/Q00613"
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                    {
                        "database": "iPTMnet",
                        "id": "Q00613",
                        "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/Q00613"
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                        "id": "18794143",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/18794143"
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                    {
                        "database": "PubMed",
                        "id": "19934326",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/19934326"
                    },
                    {
                        "database": "PubMed",
                        "id": "32457290",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/32457290"
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                ],
                "site_lbl": "Ser216",
                "uniprot_canonical_ac": "Q00613-1"
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        "record_id": "pubmed.18794143",
        "abstract": "",
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