Switch #:
Switch type:
Switch subtype:
Altered binding specificity

Acetylation of K33 in the SUMO2 inhibits binding to the Death domain-associated protein 6 (DAXX) protein see switch details. SUMO-modified forms of Protein PML (PML) are essential for the recruitment of Small ubiquitin-related modifier 2 (SUMO2) to PML nuclear bodies. The acetylated versions of SUMO1/2 failed to trigger recruitment of Small ubiquitin-related modifier 2 (SUMO2) into the nuclear bodies. An additional interaction is also possible upon acetylation with the Bromodomain of Histone acetyltransferase p300 (EP300) shown to bind the acetylated version of SUMO2. This does not occur with acetylated SUMO1. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.

(1) Death domain-associated protein 6 (DAXX)
(2) Small ubiquitin-related modifier 2 (SUMO2)
(3) Histone acetyltransferase p300 (EP300)

Interaction #2 SUMO2 - EP300

(3) ELM:LIG_BROMO motif (33K33) in Small ubiquitin-related modifier 2 (SUMO2)
(4) Bromodomain (1058-1144) in Histone acetyltransferase p300 (EP300)

Interaction Regulation
PTM-dependent Induction (Acetylation of K33 on Small ubiquitin-related modifier 2 (SUMO2)) of the Small ubiquitin-related modifier 2 (SUMO2) LIG_BROMO motif - Histone acetyltransferase p300 (EP300) Bromodomain interaction


(1) An Acetylation Switch Regulates SUMO-Dependent Protein Interaction Networks.
Ullmann et al. Mol. Cell (2012)

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