Switch #:
SWTI000664
Switch type:
Binary
Switch subtype:
Physicochemical compatibility

Description:
Acetylation of K33 in Small ubiquitin-related modifier 2 (SUMO2) inhibits binding to E3 SUMO-protein ligase PIAS2 (PIAS2). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. An additional interaction is also possible upon acetylation with the Bromodomain of p300 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.

Participants:
(1) E3 SUMO-protein ligase PIAS2 (PIAS2)
(2) Small ubiquitin-related modifier 2 (SUMO2)

Interactions
Interaction #1 PIAS2 - SUMO2

Interfaces
(1) LIG_SUMO_SBM_1 motif (467VDVID471) in E3 SUMO-protein ligase PIAS2 (PIAS2)
(2) Ubiquitin-2 like Rad60 SUMO-like (18-88) in Small ubiquitin-related modifier 2 (SUMO2)

Interaction Regulation
PTM-dependent Induction (Acetylation of K33 on Small ubiquitin-related modifier 2 (SUMO2)) of the E3 SUMO-protein ligase PIAS2 (PIAS2) LIG_SUMO_SBM_1 motif - Small ubiquitin-related modifier 2 (SUMO2) Ubiquitin-2 like Rad60 SUMO-like interaction

Context
Switch localisation
Inferred: nucleus
References

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




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