Literature summary for 2.3.2.23 extracted from

Tatham, M.; Kim, S.; Yu, B.; Jaffray, E.; Song, J.; Zheng, J.; Rodriguez, M.; Hay, R.; Chen, Y.
Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation (2003), Biochemistry, 42, 9959-9969.

Search for more literature for 2.3.2.23

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
R13A/K14A	mutations in Ubc9 disrupt the interaction with SUMO-1 but do not completely abolish the interaction with E1 enzyme. Mutant displays a significantly reduced efficiency in the transfer of SUMO-1 from E1 to Ubc9, its ability to recognize substrate and transfer SUMO-1 from Ubc9 to the target protein is unaffected	Homo sapiens
R17A/K18A	mutations in Ubc9 disrupt the interaction with SUMO-1 but do not completely abolish the interaction with E1 enzyme. Mutant displays a significantly reduced efficiency in the transfer of SUMO-1 from E1 to Ubc9, its ability to recognize substrate and transfer SUMO-1 from Ubc9 to the target protein is unaffected	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P63279	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-SUMOyl-[E1 SUMO-activating enzyme]-L-cysteine + [Ubc9]-L-cysteine	-	Homo sapiens	[E1 SUMO-activating enzyme]-L-cysteine + S-SUMOyl-[Ubc9]-L-cysteine	isoform Ubc9 is involved as E2 enzyme both in the ubiquitin and the ubiquitin-like SUMO pathway. Ubiquitin-like proteins SUMO-1, -2, and -3 interact with the same N-terminal region of the E2 conjugating enzyme Ubc9 with similar affinities	?

Synonyms

Synonyms	Comment	Organism
SUMO-conjugating enzyme UBC9	-	Homo sapiens
Ube2I	-	Homo sapiens

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Release 2023.1 (January 2023)