Switches.ELM

Switch #:

SWTI000458

Switch type:
Cumulative

Switch subtype:
Rheostatic

Description:
Multisite phosphorylation of S737 and S739 in the SUMO-binding motif of Death domain-associated protein 6 (DAXX) by CK2 subfamily and CK2 subfamily increases the strength of the interaction with Small ubiquitin-related modifier 1 (SUMO1).

Participants:
(1) Death domain-associated protein 6 (DAXX)
(2) Small ubiquitin-related modifier 1 (SUMO1)

Interactions

Interaction #1 DAXX - SUMO1

Interfaces
(1) LIG_SUMO_SBM_1 motif (₇₃₄IVLSDSD₇₄₀) in Death domain-associated protein 6 (DAXX)
(2) Ubiquitin-2 like Rad60 SUMO-like_(22-92) in Small ubiquitin-related modifier 1 (SUMO1)

Interaction Regulation
PTM-dependent Enhancement (Phosphorylation of S₇₃₇ and S₇₃₉ on Death domain-associated protein 6 (DAXX)) of the Death domain-associated protein 6 (DAXX) 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: S₇₃₇: CK2 subfamily; S₇₃₉: CK2 subfamily

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: S₇₃₇ : Casein kinase II subunit alpha (CSNK2A1). S₇₃₉ : Casein kinase II subunit alpha (CSNK2A1).

Additional Information
Affinity : Daxx(721-740): 55.3 (+/-14.2) µM, Daxx(721-740)-pS737: 4.6 (+/-1.2) µM, Daxx(721-740)-pS739: 2.8 (+/-0.3) µM, Daxx(721-740)-pS737-pS739: 1.6 (+/-0.4) µM
Structural information: 2KQS

References

(1) Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation.
Chang et al. Mol. Cell (2011)