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Literature summary for 6.2.1.45 extracted from

  • Lao, T.; Chen, S.; Sang, N.
    Two mutations impair the stability and function of ubiquitin-activating enzyme (E1) (2012), J. Cell. Physiol., 227, 1561-1568.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.45

Cloned(Commentary)

Cloned (Comment) Organism
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 Mus musculus

Protein Variants

Protein Variants Comment Organism
A189T improved stability and activity compared to mutant A189T/W714C, but when incubated at 39°C, cells expressing the mutant show increased apoptotic rate ompared to wild-type. Mutant is able to monoubiquitinate histone H2A and to support growth of TS20 cells at 39°C. Compared to mutant A189T/W714C, mutation A189T significantly improves the ubiquitination-dependent disposal of HIF-1alpha Mus musculus
A189T/W714C mutant protein is less stable than its wildtype counterpart, and restrictive temperature of 39°C accelerates its degradation Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
A31N-ts20 cell mouse embryo fibroblast cell, thermosensitive for ubiquitin-activating enzyme E1 Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
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 Mus musculus AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
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