Literature summary for 2.3.2.31 extracted from

Kelsall, I.R.; Kristariyanto, Y.A.; Knebel, A.; Wood, N.T.; Kulathu, Y.; Alpi, A.F.
Coupled monoubiquitylation of the co-E3 ligase DCNL1 by Ariadne-RBR E3 ubiquitin ligases promotes cullin-RING ligase complex remodeling (2019), J. Biol. Chem., 294, 2651-2664 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293 cell	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O95376	isoform ARIH2	-
Homo sapiens	Q9Y4X5	isoform ARIH1	-

Synonyms

Synonyms	Comment	Organism
ARIH2	-	Homo sapiens
Triad1	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the ubiquitin-associated domain-containing DCNL1 is monoubiquitylated when bound to cullin-RING E3 ubiquitin ligases.This monoubiquitylation depends on the cullin-RING E3 ubiquitin ligases-associated Ariadne RBR ligases TRIAD1 (ARIH2) andHHARI (ARIH1) and strictly requires the DCNL1's ubiquitin-associated domain	Homo sapiens
physiological function	the ubiquitin-associated domain-containing DCNL1 is monoubiquitylated when bound to cullin-RING E3 ubiquitin ligases.This monoubiquitylation depends on the cullin-RING E3 ubiquitin ligases-associated Ariadne RBR ligases TRIAD1 (ARIH2) andHHARI (ARIH1) and strictly requires the DCNL1's ubiquitin-associated domain. Autoubiquitylated TRIAD1 mediates binding to the ubiquitin-associated domain and subsequently promotes a single ubiquitin attachment to DCNL1. DCNL1 monoubiquitylation is required for efficient cullin-RING E3 ubiquitin ligase activity	Homo sapiens

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Release 2023.1 (January 2023)