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                    {
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                    {
                        "field": "o_linked_glycans",
                        "count": 0
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                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation_automatic_literature_mining",
                "table_stats": [
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        ]
    },
    {
        "title": "Candidate tumor suppressor DDX3 RNA helicase specifically represses cap-dependent translation by acting as an eIF4E inhibitory protein.",
        "journal": "Oncogene",
        "date": "2008",
        "authors": "Shih JW, Tsai TY, Chao CH, Wu Lee YH",
        "reference": {
            "type": "PubMed",
            "id": "17667941",
            "url": "https://pubmed.ncbi.nlm.nih.gov/17667941"
        },
        "referenced_glycans": [],
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            {
                "uniprot_canonical_ac": "P06730-1",
                "protein_name": "Eukaryotic translation initiation factor 4E",
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                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "O00571-1",
                "protein_name": "ATP-dependent RNA helicase DDX3X",
                "gene_name": "DDX3X",
                "tax_name": "Human"
            }
        ],
        "species": [
            {
                "name": "Homo sapiens",
                "taxid": 9606,
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                        "id": "P06730",
                        "url": "https://www.uniprot.org/uniprotkb/P06730"
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
                "reference_species": "Homo sapiens [9606]"
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        ],
        "mutagenesis": [
            {
                "start_pos": 73,
                "end_pos": 73,
                "sequence_org": "W",
                "sequence_mut": "A",
                "comment": "Abolishes binding to EIF4EBP1. Impairs interaction with DDX3X. Does not impair mRNA nuclear export. Does not affect affinity for ribavirin.",
                "evidence": [
                    {
                        "database": "UniProtKB",
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                    {
                        "database": "PubMed",
                        "id": "22578813",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22578813"
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                    {
                        "database": "PubMed",
                        "id": "17667941",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/17667941"
                    },
                    {
                        "database": "PubMed",
                        "id": "15601771",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15601771"
                    },
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                        "database": "PubMed",
                        "id": "22684010",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22684010"
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            {
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                        "id": "23413191",
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                    {
                        "database": "PubMed",
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                        "url": "https://pubmed.ncbi.nlm.nih.gov/21883093"
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                ],
                "uniprot_canonical_ac": "O00571-1"
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            {
                "start_pos": 382,
                "end_pos": 384,
                "sequence_org": "SAT",
                "sequence_mut": "AAA",
                "comment": "Loss of RNA helicase, but not ATPase activity; no effect on the repression of cap- and IRES-dependent translation, WNT/beta catenin signaling, up-regulation of CDKN1A promoter activity, HNF4A-mediated MTTP transcriptional activation, nor on stress granule assembly.",
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                "start_pos": 38,
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                "sequence_org": "Y",
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                "comment": "Impaired interaction with EIF4E; impaired stress granule formation, decreased repression of cap-dependent translation and decreased ability to enhance IRES-mediated translation. No effect on translation of HIV-1 RNA; when associated with A-43.",
                "evidence": [
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                "start_pos": 43,
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                "sequence_org": "L",
                "sequence_mut": "A",
                "comment": "Impaired interaction with EIF4E; decreased repression of cap-dependent translation. Fails to induce stress granule assembly and to rescue cell viability after stress. No effect on translation of HIV-1 RNA; when associated with A-38.",
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                    {
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                "table_id": "glycosylation_reported",
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    {
        "title": "Inhibition of mammalian target of rapamycin induces phosphatidylinositol 3-kinase-dependent and Mnk-mediated eukaryotic translation initiation factor 4E phosphorylation.",
        "journal": "Molecular and cellular biology",
        "date": "2007",
        "authors": "Wang X, Yue P, Chan CB, Ye K, Ueda T, Watanabe-Fukunaga R, Fukunaga R, Fu H, Khuri FR, Sun SY",
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