| UniProt ID | RPN5_YEAST | |
|---|---|---|
| UniProt AC | Q12250 | |
| Protein Name | 26S proteasome regulatory subunit RPN5 | |
| Gene Name | RPN5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 445 | |
| Subcellular Localization | ||
| Protein Description | Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.. | |
| Protein Sequence | MSRDAPIKADKDYSQILKEEFPKIDSLAQNDCNSALDQLLVLEKKTRQASDLASSKEVLAKIVDLLASRNKWDDLNEQLTLLSKKHGQLKLSIQYMIQKVMEYLKSSKSLDLNTRISVIETIRVVTENKIFVEVERARVTKDLVEIKKEEGKIDEAADILCELQVETYGSMEMSEKIQFILEQMELSILKGDYSQATVLSRKILKKTFKNPKYESLKLEYYNLLVKISLHKREYLEVAQYLQEIYQTDAIKSDEAKWKPVLSHIVYFLVLSPYGNLQNDLIHKIQNDNNLKKLESQESLVKLFTTNELMRWPIVQKTYEPVLNEDDLAFGGEANKHHWEDLQKRVIEHNLRVISEYYSRITLLRLNELLDLTESQTETYISDLVNQGIIYAKVNRPAKIVNFEKPKNSSQLLNEWSHNVDELLEHIETIGHLITKEEIMHGLQAK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSRDAPIKA ------CCCCCCCCC | 38.58 | 27717283 | |
| 2 | Acetylation | ------MSRDAPIKA ------CCCCCCCCC | 38.58 | 12504901 | |
| 11 | Acetylation | DAPIKADKDYSQILK CCCCCCCCCHHHHHH | 64.52 | 24489116 | |
| 18 | Acetylation | KDYSQILKEEFPKID CCHHHHHHHHCCHHH | 57.75 | 24489116 | |
| 26 | Phosphorylation | EEFPKIDSLAQNDCN HHCCHHHHHCCCCHH | 29.13 | 20486117 | |
| 44 | Acetylation | DQLLVLEKKTRQASD HHHHHHHHHHCCHHH | 56.11 | 24489116 | |
| 56 | Acetylation | ASDLASSKEVLAKIV HHHHHCCHHHHHHHH | 49.71 | 24489116 | |
| 71 | Acetylation | DLLASRNKWDDLNEQ HHHHHCCCHHHHHHH | 51.38 | 24489116 | |
| 71 | Ubiquitination | DLLASRNKWDDLNEQ HHHHHCCCHHHHHHH | 51.38 | 17644757 | |
| 84 | Acetylation | EQLTLLSKKHGQLKL HHHHHHHHHHCCHHH | 49.08 | 24489116 | |
| 84 | Ubiquitination | EQLTLLSKKHGQLKL HHHHHHHHHHCCHHH | 49.08 | 17644757 | |
| 85 | Ubiquitination | QLTLLSKKHGQLKLS HHHHHHHHHCCHHHH | 49.98 | 17644757 | |
| 92 | Phosphorylation | KHGQLKLSIQYMIQK HHCCHHHHHHHHHHH | 13.17 | 19823750 | |
| 95 | Phosphorylation | QLKLSIQYMIQKVME CHHHHHHHHHHHHHH | 8.43 | 19795423 | |
| 194 | Phosphorylation | SILKGDYSQATVLSR HHHCCCHHHHHHHHH | 20.34 | 28889911 | |
| 200 | Phosphorylation | YSQATVLSRKILKKT HHHHHHHHHHHHHHH | 27.47 | 28889911 | |
| 231 | 2-Hydroxyisobutyrylation | LVKISLHKREYLEVA HHHHCCCCHHHHHHH | 52.82 | - | |
| 295 | Phosphorylation | NNLKKLESQESLVKL CCHHHHHHHHHHHHH | 50.08 | 27214570 | |
| 298 | Phosphorylation | KKLESQESLVKLFTT HHHHHHHHHHHHHHH | 30.72 | 28889911 | |
| 301 | Acetylation | ESQESLVKLFTTNEL HHHHHHHHHHHHHHH | 43.08 | 24489116 | |
| 316 | Ubiquitination | MRWPIVQKTYEPVLN HCCCCCCCCCCCCCC | 42.03 | 17644757 | |
| 335 | Ubiquitination | AFGGEANKHHWEDLQ CCCCCCCHHCHHHHH | 43.84 | 17644757 |
| 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 RPN5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN5_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 RPN5_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "N-terminal modifications of the 19S regulatory particle subunits ofthe yeast proteasome."; Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.; Arch. Biochem. Biophys. 409:341-348(2003). Cited for: PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT SER-2. | |
