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Switch #:
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Physicochemical compatibility

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).

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

Interaction #1 PIAS1 - SUMO1

(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

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.
Switch localisation

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

See also

Other switches involving participants
Small ubiquitin-related modifier 1 (SUMO1) - 6 more (view)
E3 SUMO-protein ligase PIAS1 (PIAS1) - 2 more (view)

Other switches involving interfaces
LIG_SUMO_SBM_1 - 10 more (view)
Ubiquitin-2 like Rad60 SUMO-like - 10 more (view)

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