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Literature summary for 2.3.2.24 extracted from

  • Cook, B.W.; Barber, K.R.; Shilton, B.H.; Shaw, G.S.
    The HIP2-ubiquitin conjugate forms a non-compact monomeric thioester during di-ubiquitin synthesis (2015), PLoS ONE, 10, e0120318.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.24

Organism

Organism UniProt Comment Textmining
Homo sapiens P61086
-
-
Saccharomyces cerevisiae P21734
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 N6-monoubiquitinyl-[Ubc1]-L-lysine
-
 Saccharomyces cerevisiae N6-diubiquitinyl-[Ubc1]-L-lysine + [Ube2K]-L-lysine
-
 ?
2 N6-monoubiquitinyl-[Ube2K]-L-lysine
-
 Homo sapiens N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine
-
 ?

Synonyms

Synonyms Comment Organism
HIP2
-
 Homo sapiens
Ubc1
-
 Saccharomyces cerevisiae
UBE2K
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function E2 enzyme HIP2-ubiquitin thioester complexes remain predominantly monomeric in solution Saccharomyces cerevisiae
physiological function E2 enzyme HIP2-ubiquitin thioester complexes remain predominantly monomeric in solution. Models of the HIP2-ubiquitin complex show an open or backbent conformation similar to UbcH5b-ubiquitin where the ubiquitin-associated UBA domain and covalently attached ubiquitin reside on opposite ends of the catalytic domain. Full length HIP2 exhibits a fivefold increase in the formation rate of diubiquitin compared to a HIP2 lacking the UBA domain Homo sapiens