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 | ||
* 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 | ||||||
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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. |