TRIM28 in TRIM28:KRAB-ZFP:retroelement chromatin autoSUMOylates with SUMO2

Stable Identifier
R-HSA-9842868
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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).
Literature References
PubMed ID Title Journal Year
26365490 Systematic identification of factors for provirus silencing in embryonic stem cells

Fang, HT, Tergaonkar, V, Li, Y, Chen, L, Yu, T, Wang, HF, Neo, SP, Li, H, Lorincz, MC, Schlesinger, S, Loh, YH, Yang, BX, Gunaratne, J, Seah, YF, Goff, SP, El Farran, CA, Guo, HC, Bard, FA, Daley, GQ, Goh, GY, Lim, TM, Collins, JJ

Cell 2015
18082607 PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing

Yap, KL, Negorev, DG, Ivanov, AV, Schultz, DC, Peng, H, Fredericks, WJ, Sadofsky, MJ, Psulkowski, E, Rauscher FJ, 3rd, White, DE, Yurchenko, V, Zhou, MM, Maul, GG

Mol Cell 2007
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Catalyst Activity

SUMO ligase activity of TRIM28:KRAB-ZFP:retroelement chromatin [nucleoplasm]

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