Switches.ELM

Switch #:

SWTI000613

Switch type:
Binary

Switch subtype:
Physicochemical compatibility

Description:
Phosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).

Participants:
(1) E3 SUMO-protein ligase PIAS1 (PIAS1)
(2) Small ubiquitin-related modifier 1 (SUMO1)

Interactions

Interaction #1 PIAS1 - SUMO1

Interfaces
(1) LIG_SUMO_SBM_1 motif (₄₅₇VEVID₄₆₁) in E3 SUMO-protein ligase PIAS1 (PIAS1)
(2) Ubiquitin-2 like Rad60 SUMO-like_(22-92) in Small ubiquitin-related modifier 1 (SUMO1)

Interaction Regulation
PTM-dependent Enhancement (Phosphorylation of S₄₆₆, S₄₆₇ and S₄₆₈ on E3 SUMO-protein ligase PIAS1 (PIAS1)) of the E3 SUMO-protein ligase PIAS1 (PIAS1) LIG_SUMO_SBM_1 motif - Small ubiquitin-related modifier 1 (SUMO1) Ubiquitin-2 like Rad60 SUMO-like interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: S₄₆₆: CK2 subfamily; S₄₆₇: CK2 subfamily; S₄₆₈: CK2 subfamily

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: S₄₆₆ : Casein kinase II subunit alpha (CSNK2A1). S₄₆₇ : Casein kinase II subunit alpha (CSNK2A1). S₄₆₈ : Casein kinase II subunit alpha (CSNK2A1).

Additional Information
Switch_Notes: Since three serine residues are involved, this might be a rheostatic regulation of SIM binding, however experiments were only performed with triple S to A and triple S to D mutants.

Context

Switch localisation

Inferred: nuclear speck, nucleoplasm

References

(1) Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling.
Stehmeier et al. Mol. Cell (2009)