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Ubc9
From Proteopedia
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== Function == | == Function == | ||
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== Disease == | == Disease == | ||
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== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
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== References == | == References == | ||
1. Reverter, D., & Lima, C. D. (2005). Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature, 435(June), 687–692. doi:10.1038/nature03588 | 1. Reverter, D., & Lima, C. D. (2005). Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature, 435(June), 687–692. doi:10.1038/nature03588 | ||
<references/> | <references/> | ||
Revision as of 05:09, 22 February 2015
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Contents |
Structure
Ubc9 exhibits a single domain structure consisting of both alpha helices and beta-pleated sheets. C93 has been identified as the active residue and is located on a non-secondary structured loop of amino acids (78-108) between beta sheet four and alpha helix two ^1^ .
Function
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Disease
-
Relevance
-
Structural highlights
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References
1. Reverter, D., & Lima, C. D. (2005). Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature, 435(June), 687–692. doi:10.1038/nature03588
