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Details on Person The PHD domain of TRIM28 (KAP1) is a SUMO E3 ligase that cat...
| Class:Id | Summation:9851226 |
|---|---|
| _displayName | The PHD domain of TRIM28 (KAP1) is a SUMO E3 ligase that cat... |
| _timestamp | 2023-12-23 01:48:46 |
| created | [InstanceEdit:9851229] May, Bruce, 2023-10-15 |
| literatureReference | [LiteratureReference:9843931] KAP1 is an antiparallel dimer with a functional asymmetry [LiteratureReference:9851228] A Dissection of Oligomerization by the TRIM28 Tripartite Motif and the Interaction with Members of the Krab-ZFP Family |
| modified | [InstanceEdit:9851264] May, Bruce, 2023-10-15 [InstanceEdit:9851319] May, Bruce, 2023-10-22 [InstanceEdit:9856776] May, Bruce, 2023-12-23 |
| text | The PHD domain of TRIM28 (KAP1) is a SUMO E3 ligase that catalyzes the autoSUMOylation of lysines 554, 575, 676, 750, 779, and 804 in the bromodomain of TRIM28 (Ivanov et al. 2007, Yang et al. 2015). SUMOylated TRIM28 recruits SETDB1 and the NuRD repressor complex and stimulates the lysine methylation activity of SETDB1 (Ivanov et al. 2007). TRIM28 is a dimer (Fobti et al. 2019) that can form oligomers (inferred from the mouse homolog in Sun et al. 2019). |
| (summation) | [Reaction:9842868] TRIM28 in TRIM28:KRAB-ZFP:retroelement chromatin autoSUMOylates with SUMO2 [Homo sapiens] |
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No pathways have been reviewed or authored by The PHD domain of TRIM28 (KAP1) is a SUMO E3 ligase that cat... (9851226)
