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Details on Person KMT2D (also known as MLL4) binds the WRAD complex, consistin...
| Class:Id | Summation:9676260 |
|---|---|
| _displayName | KMT2D (also known as MLL4) binds the WRAD complex, consistin... |
| _timestamp | 2023-02-10 18:27:51 |
| created | [InstanceEdit:9676262] Orlic-Milacic, Marija, 2020-02-11 |
| modified | [InstanceEdit:9818183] Orlic-Milacic, Marija, 2022-10-12 [InstanceEdit:9818559] Orlic-Milacic, Marija, 2022-10-18 [InstanceEdit:9823555] Orlic-Milacic, Marija, 2023-01-06 [InstanceEdit:9828129] Orlic-Milacic, Marija, 2023-02-10 |
| text | KMT2D (also known as MLL4) binds the WRAD complex, consisting of WDR5, RBBP5, ASH2L and DPY30, to form the MLL4 complex. WDR5 plays an important role in the optimal stimulation of MLL4 methyltransferase activity by the RBBP5:ASH2L heterodimer (Zhang et al. 2012). KMT2C and KMT2D are paralogous histone methyltransferases and mainly responsible for H3K4 mono-methylation (H3K4me1) at enhancers (Lee et al. 2013). KMT2D has a partial functional redundancy with KMT2C in cells, although the phenotypes of KMT2D and KMT2C null mice suggest that MLL4 might be the dominant counterpart (Lee et al. 2013). KMT2C/D are thought to play a role in the recruitment of the acetyltransferase CBP/p300 complex, which facilitates H3K27 acetylation and RNA polymerase II's recruitment to enhancer regions (Jin et al. 2011, Wang et al. 2016, Lai et al. 2017). |
| (summation) | [Reaction:9676268] Formation of the MLL4 complex [Homo sapiens] |
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No pathways have been reviewed or authored by KMT2D (also known as MLL4) binds the WRAD complex, consistin... (9676260)
