2.3.2.25: N-terminal E2 ubiquitin-conjugating enzyme
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For detailed information about N-terminal E2 ubiquitin-conjugating enzyme, go to the full flat file.
Reaction
Synonyms
E2 Ube2w, E2 ubiquitin-conjugating enzyme, Ubc16, UbcH6, UBE2E1, UBE2O, UBE2W, ubiquitin conjugating enzyme, ubiquitin conjugating enzyme E2, ubiquitin-conjugating enzyme (E2), ubiquitin-conjugating enzyme E2, ubiquitin-protein ligase W
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Engineering
Engineering on EC 2.3.2.25 - N-terminal E2 ubiquitin-conjugating enzyme
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C91A
site-directed mutagenesis of an active site residue, the mutation eliminates the ability of Ube2W to transfer ubiquitin (Ub) to substrates while still allowing Ube2W to bind substrates, it disrupts Ube2W-mediated ubiquitination
W144E
site-directed mutagenesis, the mutation eliminates substrate binding and disrupts Ube2W-mediated ubiquitination
C91A
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site-directed mutagenesis of an active site residue, the mutation eliminates the ability of Ube2W to transfer ubiquitin (Ub) to substrates while still allowing Ube2W to bind substrates, it disrupts Ube2W-mediated ubiquitination
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W144E
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site-directed mutagenesis, the mutation eliminates substrate binding and disrupts Ube2W-mediated ubiquitination
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additional information
to obtain homogenous and pure ubiquitin (Ub)-modified alphasynuclein (alphaS) and tauK18, engineered constructs that expressed fusion proteins with a single Ub moiety immediately before the first residue of alphaS or tauK18 (Ub-alphaS and Ub-tauK18) are genetically engineered. These engineered N-terminal Ub-fusion proteins are protected from deubiquitination by a Gly76Ser substitution of the C-terminal residue of Ub. No filamentous aggregates from Ub-alphaS are detected under TEM, thus, the morphology of filamentous aggregates is affected by N-terminal Ub modification. Meanwhile, oligomers from both tauK18 and Ub-tauK18 are reproducibly detected early in the aggregation process. An apparent reduction of the fraction of soluble oligomers with time is detected in both unmodified and Ub-modified tauK18 beyond 50 and 70 h, respectively. Comparisons of modified and unmodified proteins' aggregation behaviour, overview. Proteasomes are able to target Ub-modified aggregates
additional information
absence of Ube2W increases soluble, monomeric mutant huntingtin (HTT) in a knock-in mouse model of Huntington's disease. The absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species
additional information
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absence of Ube2W increases soluble, monomeric mutant huntingtin (HTT) in a knock-in mouse model of Huntington's disease. The absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species
additional information
generation of E2-knockdown macrophages, siRNA knockdown of Ube2o expression in engineered RAW-RA cells, Ube2o knockdown efficiency is measured by quantitative PCR
additional information
specific downregulation of enzyme UBE2W in spermatogenic cells by murine UBE2W-specific shRNA. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis. UBE2W upregulation is performed by a recombinant lentivirus containing murine UBE2W
additional information
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specific downregulation of enzyme UBE2W in spermatogenic cells by murine UBE2W-specific shRNA. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis. UBE2W upregulation is performed by a recombinant lentivirus containing murine UBE2W
additional information
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specific downregulation of enzyme UBE2W in spermatogenic cells by murine UBE2W-specific shRNA. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis. UBE2W upregulation is performed by a recombinant lentivirus containing murine UBE2W
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additional information
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absence of Ube2W increases soluble, monomeric mutant huntingtin (HTT) in a knock-in mouse model of Huntington's disease. The absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species
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