| UniProt ID | RPN10_YEAST | |
|---|---|---|
| UniProt AC | P38886 | |
| Protein Name | 26S proteasome regulatory subunit RPN10 | |
| Gene Name | RPN10 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 268 | |
| Subcellular Localization | ||
| Protein Description | Multiubiquitin binding protein.. | |
| Protein Sequence | MVLEATVLVIDNSEYSRNGDFPRTRFEAQIDSVEFIFQAKRNSNPENTVGLISGAGANPRVLSTFTAEFGKILAGLHDTQIEGKLHMATALQIAQLTLKHRQNKVQHQRIVAFVCSPISDSRDELIRLAKTLKKNNVAVDIINFGEIEQNTELLDEFIAAVNNPQEETSHLLTVTPGPRLLYENIASSPIILEEGSSGMGAFGGSGGDSDANGTFMDFGVDPSMDPELAMALRLSMEEEQQRQERLRQQQQQQDQPEQSEQPEQHQDK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 15 | Phosphorylation | LVIDNSEYSRNGDFP EEECCCCCCCCCCCC | 16.86 | 28132839 | |
| 43 | Phosphorylation | IFQAKRNSNPENTVG EEEHHHCCCCCCCEE | 58.77 | 23749301 | |
| 71 | Ubiquitination | TFTAEFGKILAGLHD EEEHHHHHHHHCCCC | 39.61 | 23749301 | |
| 84 | Ubiquitination | HDTQIEGKLHMATAL CCCCCCCCHHHHHHH | 23.56 | 23749301 | |
| 116 | Phosphorylation | RIVAFVCSPISDSRD EEEEEEECCCCCCHH | 21.70 | 23749301 | |
| 235 | Phosphorylation | LAMALRLSMEEEQQR HHHHHHHCHHHHHHH | 20.08 | 28889911 | |
| 259 | Phosphorylation | QQDQPEQSEQPEQHQ HHHCHHHHCCHHHHC | 36.22 | 22369663 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN10_YEAST !! | ||||||
* 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 RPN10_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY. | |