ELM - instance LIG_SUMO_SIM_par_1 in sequence Q9UER7 at position 732

Instance

Accession	Acc. Gene-, Name	Start	End	Subsequence	Logic	PDB	Organism	Length
ELMI002794	Q9UER7 DAXX DAXX_HUMAN	732	740	KTSVATQCDPEEIIVLSDSD	TP	2KQS	Homo sapiens (Human)	740

Instance evidence

Evidence class	PSI-MI	Method	BioSource	PubMed	Logic	Reliability	Notes
experimental	MI:0096	pull down	in vivo/in vitro		support	certain	InteractionDetection
experimental	MI:0519	glutathione s tranferase tag	in vitro	Lin,2006	support	certain
experimental	MI:0077	nuclear magnetic resonance	in vitro	Chang,2011	support	certain	InteractionDetection FeatureDetection
experimental	MI:0113	western blot	in vitro	Lin,2006	support	certain	ParticipantIdentification FeatureDetection
experimental	MI:0573	mutation disrupting interaction	in vivo/in vitro	Lin,2006	support	certain
experimental	MI:0074	mutation analysis	in vivo/in vitro	Lin,2006	support	certain	FeatureDetection

Switches

This ELM instance is part of the following 5 switching mechanisms annotated at the switches.ELM resource:

SWTI000458:

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).
SWTI000666:

Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Death domain-associated protein 6 (DAXX) to PML nuclear bodies.
SWTI000667:

Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Death domain-associated protein 6 (DAXX) to PML nuclear bodies.
SWTI000705:

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.
SWTI000706:

Acetylation of K37 in the SUMO1 inhibits binding to the Small ubiquitin-related modifier 1 (SUMO1) protein see switch details. SUMO-modified forms of Protein PML (PML) are essential for the recruitment of DAXX to PML nuclear bodies. The acetylated versions of SUMO1/2 failed to trigger recruitment of DAXX into the nuclear bodies. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.

Pathways

KEGG: The sequence Q9UER7 is implicated in the following 6 Pathways: (color codes: This sequence=red, interacting sequence=orange)

Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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