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The entire C-terminal region of histone-lysine-N-methyltr...
| Class:Id | Summation:9945001 |
|---|---|
| _displayName | The entire C-terminal region of histone-lysine-N-methyltr... |
| _timestamp | 2025-05-26 23:38:39 |
| created | [InstanceEdit:9945007] Orlic-Milacic, Marija, 2025-04-08 |
| literatureReference | [LiteratureReference:9945005] Dissecting KMT2D missense mutations in Kabuki syndrome patients [LiteratureReference:9823216] KMT2C/D COMPASS complex-associated diseases [KCDCOM-ADs]: an emerging class of congenital regulopathies [LiteratureReference:9949919] Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4 [LiteratureReference:9949915] Molecular analysis, pathogenic mechanisms, and readthrough therapy on a large cohort of Kabuki syndrome patients |
| modified | [InstanceEdit:9949669] Orlic-Milacic, Marija, 2025-05-24 [InstanceEdit:9949936] Orlic-Milacic, Marija, 2025-05-26 |
| text | The entire C-terminal region of histone-lysine-N-methyltransferase KMT2D (residues 4507-5537), which includes the ZF, PHD7, FYRN, FYRC, WIN and SET domains, is involved in binding to the WRAD complex (Dhar et al. 2012). Missense mutations in the C-terminal region of KMT2D, identified in Kabuki syndrome patients, affect its binding to the WRAD complex (Cocciadiferro et al. 2018, Lavery et al. 2020), consisting of WDR5, RBBP5, ASH2L and DPY30. While the impact of KMT2D truncating mutations on the WRAD complex binding has not been tested, they were shown to frequently result in KMT2D mRNA degradation through nonsense-mediated mRNA decay and contribute to haploinsufficiency (Micale et al. 2014). |
| (summation) | [Pathway:9944997] Loss of Function of KMT2D in MLL4 Complex Formation in Kabuki Syndrome [Homo sapiens] |
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The entire C-terminal region of histone-lysine-N-methyltr... (9945001)
