UniProt ID | UBC12_YEAST | |
---|---|---|
UniProt AC | P52491 | |
Protein Name | NEDD8-conjugating enzyme UBC12 | |
Gene Name | UBC12 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 188 | |
Subcellular Localization | ||
Protein Description | Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins. The major substrate is CDC53/Cullin.. | |
Protein Sequence | MLKLRQLQKKKQKENENSSSIQPNLSAARIRLKRDLDSLDLPPTVTLNVITSPDSADRSQSPKLEVIVRPDEGYYNYGSINFNLDFNEVYPIEPPKVVCLKKIFHPNIDLKGNVCLNILREDWSPALDLQSIITGLLFLFLEPNPNDPLNKDAAKLLCEGEKEFAEAVRLTMSGGSIEHVKYDNIVSP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MLKLRQLQ -------CCHHHHHH | 7.22 | 21940857 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of UBC12_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
1 | M | Acetylation |
| 21940857 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of UBC12_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"N-terminal acetylation acts as an avidity enhancer within aninterconnected multiprotein complex."; Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.; Science 334:674-678(2011). Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-24 IN COMPLEX WITH DCN1,AND ACETYLATION AT MET-1. |