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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.
    View publication on PubMed
Search for more literature for 2.3.2.23

Cloned(Commentary)

Cloned (Comment) Organism
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 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
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 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
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 Homo sapiens