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        "title": "Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin.",
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        "authors": "Liu Zhi-Ping, Wang Zhigao, Yanagisawa Hiromi, Olson Eric N",
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    {
        "title": "Novel repressor regulates insulin sensitivity through interaction with Foxo1.",
        "journal": "EMBO J.",
        "date": "2012",
        "authors": "Nakae J, Cao Y, Hakuno F, Takemori H, Kawano Y, Sekioka R, Abe T, Kiyonari H, Tanaka T, Sakai J, Takahashi S, Itoh H",
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                ],
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                "end_pos": 262,
                "sequence_org": "K",
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                "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9R1E0",
                        "url": "https://www.uniprot.org/uniprotkb/Q9R1E0"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                    {
                        "database": "PubMed",
                        "id": "15220471",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15220471"
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                    {
                        "database": "PubMed",
                        "id": "16076959",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/16076959"
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                    {
                        "database": "PubMed",
                        "id": "17090532",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/17090532"
                    },
                    {
                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
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                ],
                "uniprot_canonical_ac": "Q9R1E0-1"
            },
            {
                "start_pos": 262,
                "end_pos": 262,
                "sequence_org": "K",
                "sequence_mut": "Q",
                "comment": "Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9R1E0",
                        "url": "https://www.uniprot.org/uniprotkb/Q9R1E0"
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                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
                    },
                    {
                        "database": "PubMed",
                        "id": "15220471",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/15220471"
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                    {
                        "database": "PubMed",
                        "id": "16076959",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/16076959"
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                    {
                        "database": "PubMed",
                        "id": "17090532",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/17090532"
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                    {
                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
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                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Significant reduction in acetylation and transcriptional activity increased by about 2.0 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-245. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-271 and R-291.",
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                    {
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                        "database": "PubMed",
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                        "database": "PubMed",
                        "id": "17090532",
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                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
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                "uniprot_canonical_ac": "Q9R1E0-1"
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                "start_pos": 271,
                "end_pos": 271,
                "sequence_org": "K",
                "sequence_mut": "Q",
                "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9R1E0",
                        "url": "https://www.uniprot.org/uniprotkb/Q9R1E0"
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                    {
                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
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                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                ],
                "uniprot_canonical_ac": "Q9R1E0-1"
            },
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                "start_pos": 271,
                "end_pos": 271,
                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-291.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9R1E0",
                        "url": "https://www.uniprot.org/uniprotkb/Q9R1E0"
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                    {
                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
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                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                ],
                "uniprot_canonical_ac": "Q9R1E0-1"
            },
            {
                "start_pos": 291,
                "end_pos": 291,
                "sequence_org": "K",
                "sequence_mut": "Q",
                "comment": "Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24: Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9R1E0",
                        "url": "https://www.uniprot.org/uniprotkb/Q9R1E0"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                    {
                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
                    }
                ],
                "uniprot_canonical_ac": "Q9R1E0-1"
            },
            {
                "start_pos": 291,
                "end_pos": 291,
                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-271. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-271. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-271.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9R1E0",
                        "url": "https://www.uniprot.org/uniprotkb/Q9R1E0"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
                    },
                    {
                        "database": "PubMed",
                        "id": "20519497",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/20519497"
                    }
                ],
                "uniprot_canonical_ac": "Q9R1E0-1"
            },
            {
                "start_pos": 78,
                "end_pos": 78,
                "sequence_org": "I",
                "sequence_mut": "A",
                "comment": "Abolishes inhibition of FOXO1 transcriptional activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P0DJI6",
                        "url": "https://www.uniprot.org/uniprotkb/P0DJI6"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
                    }
                ],
                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 80,
                "end_pos": 80,
                "sequence_org": "T",
                "sequence_mut": "A",
                "comment": "Abolishes inhibition of FOXO1 transcriptional activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P0DJI6",
                        "url": "https://www.uniprot.org/uniprotkb/P0DJI6"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
                    }
                ],
                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 81,
                "end_pos": 81,
                "sequence_org": "L",
                "sequence_mut": "A",
                "comment": "Enhances FOXO1 nuclear translocation but does not abolish inhibition of FOXO1 transcriptional activity in the absence of forskolin.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P0DJI6",
                        "url": "https://www.uniprot.org/uniprotkb/P0DJI6"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                ],
                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 85,
                "end_pos": 85,
                "sequence_org": "L",
                "sequence_mut": "A",
                "comment": "Abolishes inhibition of FOXO1 transcriptional activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P0DJI6",
                        "url": "https://www.uniprot.org/uniprotkb/P0DJI6"
                    },
                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                ],
                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 87,
                "end_pos": 87,
                "sequence_org": "L",
                "sequence_mut": "A",
                "comment": "Abolishes inhibition of FOXO1 transcriptional activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P0DJI6",
                        "url": "https://www.uniprot.org/uniprotkb/P0DJI6"
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                    {
                        "database": "PubMed",
                        "id": "22510882",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/22510882"
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                ],
                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 92,
                "end_pos": 92,
                "sequence_org": "S",
                "sequence_mut": "A",
                "comment": "Does not inhibit subcellular localization. Does not affect phosphorylation in response to forskolin.",
                "evidence": [
                    {
                        "database": "UniProtKB",
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                        "url": "https://www.uniprot.org/uniprotkb/P0DJI6"
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                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 93,
                "end_pos": 93,
                "sequence_org": "T",
                "sequence_mut": "A",
                "comment": "Abolishes phosphorylation in response to forskolin. Localizes mainly to the cytosol. Weakly enhances FOXO1 acetylation. Weakly abolishes inhibition of FOXO1 transcriptional activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
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                "uniprot_canonical_ac": "P0DJI6-1"
            },
            {
                "start_pos": 93,
                "end_pos": 93,
                "sequence_org": "T",
                "sequence_mut": "D",
                "comment": "Mimicks phosphorylation state, localizes mainly to the nucleus. Strongly enhances FOXO1 acetylation. Strongly abolishes inhibition of FOXO1 transcriptional activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "P0DJI6",
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                "kinase_uniprot_canonical_ac": "",
                "kinase_gene_name": "",
                "residue": "Thr",
                "comment": "Phosphothreonine; by PKA",
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                        "id": "P0DJI6",
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                "site_lbl": "Thr93",
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        "record_id": "pubmed.22510882",
        "abstract": "",
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    {
        "title": "WNK1 regulates skeletal muscle cell hypertrophy by modulating the nuclear localization and transcriptional activity of FOXO4.",
        "journal": "Scientific reports",
        "date": "2018",
        "authors": "Mandai S, Mori T, Nomura N, Furusho T, Arai Y, Kikuchi H, Sasaki E, Sohara E, Rai T, Uchida S",
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        ],
        "species": [
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                        "id": "Q9WVH3",
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                ],
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                "glygen_name": "Mouse",
                "reference_species": "Mus musculus [10090]"
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                "start_pos": 197,
                "end_pos": 197,
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                "kinase_gene_name": "",
                "residue": "Ser",
                "comment": "Phosphoserine; by PKB/AKT1",
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                        "database": "iPTMnet",
                        "id": "Q9WVH3",
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                    {
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                        "id": "29904119",
                        "url": "https://pubmed.ncbi.nlm.nih.gov/29904119"
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                ],
                "site_lbl": "Ser197",
                "uniprot_canonical_ac": "Q9WVH3-1"
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