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        "title": "Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation.",
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        "date": "2001",
        "authors": "Masson N, Willam C, Maxwell PH, Pugh CW, Ratcliffe PJ",
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                "start_pos": 397,
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                "comment": "Abolishes in VHLE3-dependent ubiquitination, abolishes oxygen-dependent regulation of VP16, partially reduced VHLE target site ubiquitination and no interaction with VHL. No VHLE target site ubiquitination; when associated with G-564. Increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation; when associated with A-564.",
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    {
        "title": "SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation.",
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        "date": "2001",
        "authors": "Wu G, Lyapina S, Das I, Li J, Gurney M, Pauley A, Chui I, Deshaies RJ, Kitajewski J",
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                "protein_name": "Nuclear receptor corepressor 2",
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                "protein_name": "Recombining binding protein suppressor of hairless",
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        "title": "FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor.",
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        "date": "2002",
        "authors": "Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, Bruick RK",
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                    {
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                    {
                        "field": "o_linked_glycans",
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                ],
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        ]
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    {
        "title": "Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity.",
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        "date": "2004",
        "authors": "Lancaster DE, McNeill LA, McDonough MA, Aplin RT, Hewitson KS, Pugh CW, Ratcliffe PJ, Schofield CJ",
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                "uniprot_canonical_ac": "Q9NWT6-1",
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                "tax_name": "Human"
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            {
                "uniprot_canonical_ac": "Q99814-1",
                "protein_name": "Endothelial PAS domain-containing protein 1",
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                "tax_name": "Human"
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        ],
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                "name": "Homo sapiens",
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                ],
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                "glygen_name": "Human",
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        ],
        "mutagenesis": [
            {
                "start_pos": 340,
                "end_pos": 340,
                "sequence_org": "L",
                "sequence_mut": "R",
                "comment": "Impairs dimer formation, leading to loss of HIF1AAsn hydroxylation activity. No stimulation of 2-oxoglutarate turnover; when associated with A-201.",
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                    {
                        "database": "UniProtKB",
                        "id": "Q9NWT6",
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                        "database": "PubMed",
                        "id": "18611856",
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                ],
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            {
                "start_pos": 344,
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                "sequence_mut": "R",
                "comment": "No effect on dimer formation and HIF1AAsn hydroxylation activity.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q9NWT6",
                        "url": "https://www.uniprot.org/uniprotkb/Q9NWT6"
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                    {
                        "field": "n_linked_glycans",
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                    {
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                    },
                    {
                        "field": "n_linked_glycan_sites",
                        "count": 0
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                    {
                        "field": "o_linked_glycan_sites",
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                        "field": "n_linked_glycans",
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                    {
                        "field": "o_linked_sites",
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                    {
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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": "n_linked_glycans",
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                    {
                        "field": "o_linked_glycans",
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    {
        "title": "Sumoylation increases HIF-1alpha stability and its transcriptional activity.",
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        "date": "2004",
        "authors": "Bae SH, Jeong JW, Park JA, Kim SH, Bae MK, Choi SJ, Kim KW",
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                ],
                "common_name": "Human",
                "glygen_name": "Human",
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        ],
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                "start_pos": 389,
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                    {
                        "database": "UniProtKB",
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                    {
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                        "id": "15465032",
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                ],
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            {
                "start_pos": 391,
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                "sequence_org": "K",
                "sequence_mut": "R",
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                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q16665",
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                    {
                        "database": "PubMed",
                        "id": "17610843",
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                ],
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            },
            {
                "start_pos": 392,
                "end_pos": 392,
                "sequence_org": "K",
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                "comment": "No change in sumoylation.",
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                    {
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                    {
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            },
            {
                "start_pos": 442,
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                "comment": "No change in sumoylation.",
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                ],
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            },
            {
                "start_pos": 460,
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                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "No change in sumoylation nor in ARD1-mediated acetylation.",
                "evidence": [
                    {
                        "database": "UniProtKB",
                        "id": "Q16665",
                        "url": "https://www.uniprot.org/uniprotkb/Q16665"
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                "start_pos": 477,
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                "comment": "Abolishes 1 sumoylation. Abolishes 2 sumoylations; when associated with R-391. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-532.",
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                "comment": "Reduced ubiquitination. No change in sumoylation nor on interaction with NAA10. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-477. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-538 and K-547.",
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    {
        "title": "Hypoxia requires notch signaling to maintain the undifferentiated cell state.",
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        "date": "2005",
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    {
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    {
        "title": "HIF-1alpha and EPAS ubiquitination mediated by the VHL tumour suppressor involves flexibility in the ubiquitination mechanism, similar to other RING E3 ligases.",
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        "date": "2007",
        "authors": "Paltoglou S, Roberts BJ",
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                "comment": "No change in VHL-dependent ubiquitination. Partially reduced VHLE target site ubiquitination. No VHLE target site ubiquitination; when associated with A-402.",
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        "title": "Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1alpha.",
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        "date": "2006",
        "authors": "Mylonis I, Chachami G, Samiotaki M, Panayotou G, Paraskeva E, Kalousi A, Georgatsou E, Bonanou S, Simos G",
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    {
        "title": "Clioquinol, a Cu(II)/Zn(II) chelator, inhibits both ubiquitination and asparagine hydroxylation of hypoxia-inducible factor-1alpha, leading to expression of vascular endothelial growth factor and erythropoietin in normoxic cells.",
        "journal": "The Journal of biological chemistry",
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    {
        "title": "NOTCH1 directly regulates c-MYC and activates a feed-forward-loop transcriptional network promoting leukemic cell growth.",
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        "authors": "Palomero T, Lim WK, Odom DT, Sulis ML, Real PJ, Margolin A, Barnes KC, O'Neil J, Neuberg D, Weng AP, Aster JC, Sigaux F, Soulier J, Look AT, Young RA, Califano A, Ferrando AA",
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    {
        "title": "RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha.",
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        "date": "2007",
        "authors": "Liu Ye V, Baek Jin H, Zhang Huafeng, Diez Roberto, Cole Robert N, Semenza Gregg L",
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                "uniprot_canonical_ac": "P63244-1",
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        ],
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                ],
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        ],
        "record_id": "pubmed.17244529",
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                ],
                "sort_fields": []
            },
            {
                "table_id": "glycosylation",
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                        "field": "n_linked_glycan_sites",
                        "count": 0
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                        "count": 0
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                    {
                        "field": "o_linked_glycans",
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                ],
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        ]
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    {
        "title": "Modulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1alpha.",
        "journal": "FEBS letters",
        "date": "2007",
        "authors": "Cho H, Ahn DR, Park H, Yang EG",
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        ],
        "phosphorylation": [
            {
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                ],
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                        "field": "o_linked_glycan_sites",
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            {
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                ],
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        ]
    },
    {
        "title": "SUMOylation of hypoxia-inducible factor-1alpha reduces its transcriptional activity.",
        "journal": "Biochemical and biophysical research communications",
        "date": "2007",
        "authors": "Berta MA, Mazure N, Hattab M, Pouyssegur J, Brahimi-Horn MC",
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            "id": "17610843",
            "url": "https://pubmed.ncbi.nlm.nih.gov/17610843"
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                ],
                "common_name": "Human",
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        ],
        "mutagenesis": [
            {
                "start_pos": 377,
                "end_pos": 377,
                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-391; R-477 and R-532.",
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                    {
                        "database": "UniProtKB",
                        "id": "Q16665",
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            {
                "start_pos": 391,
                "end_pos": 391,
                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Abolishes 1 sumoylation. Abolishes 1 sumoylation; when associated with R-532. Abolishes 2 sumoylations; when associated with R-477. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-477 and R-532.",
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                "start_pos": 477,
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                "comment": "Abolishes 1 sumoylation. Abolishes 2 sumoylations; when associated with R-391. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-532.",
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                ],
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            },
            {
                "start_pos": 532,
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                "sequence_org": "K",
                "sequence_mut": "R",
                "comment": "Reduced ubiquitination. No change in sumoylation nor on interaction with NAA10. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-477. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-538 and K-547.",
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    {
        "title": "Hypoxia-inducible factor-1alpha (HIF-1alpha) gene polymorphisms, circulating insulin-like growth factor binding protein (IGFBP)-3 levels and prostate cancer.",
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        "authors": "Li H, Bubley GJ, Balk SP, Gaziano JM, Pollak M, Stampfer MJ, Ma J",
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    {
        "title": "The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha.",
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        "date": "2007",
        "authors": "Hu CJ, Sataur A, Wang L, Chen H, Simon MC",
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                "uniprot_canonical_ac": "P01588-1",
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        "title": "RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia.",
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                "start_pos": 21,
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                "start_pos": 61,
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