Ubc9
From Proteopedia
(Difference between revisions)
| Line 7: | Line 7: | ||
== Function == | == Function == | ||
| - | + | - | |
== Disease == | == Disease == | ||
| - | + | - | |
== Relevance == | == Relevance == | ||
| - | + | - | |
== Structural highlights == | == Structural highlights == | ||
| + | - | ||
== 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
|
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
-
Disease
-
Relevance
-
Structural highlights
-
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
