| UniProt ID | RPN7_YEAST | |
|---|---|---|
| UniProt AC | Q06103 | |
| Protein Name | 26S proteasome regulatory subunit RPN7 | |
| Gene Name | RPN7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 429 | |
| 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 | MVDVEEKSQEVEYVDPTVNRVPNYEVSEKAFLLTQSKVSIEQRKEAAEFVLAKIKEEEMAPYYKYLCEEYLVNNGQSDLEHDEKSDSLNEWIKFDQELYNELCKKNESKIKELNEKIQKLEEDDEGELEQAQAWINLGEYYAQIGDKDNAEKTLGKSLSKAISTGAKIDVMLTIARLGFFYNDQLYVKEKLEAVNSMIEKGGDWERRNRYKTYYGIHCLAVRNFKEAAKLLVDSLATFTSIELTSYESIATYASVTGLFTLERTDLKSKVIDSPELLSLISTTAALQSISSLTISLYASDYASYFPYLLETYANVLIPCKYLNRHADFFVREMRRKVYAQLLESYKTLSLKSMASAFGVSVAFLDNDLGKFIPNKQLNCVIDRVNGIVETNRPDNKNAQYHLLVKQGDGLLTKLQKYGAAVRLTGSDRV | |
| 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 |
|---|---|---|---|---|---|
| 7 | Acetylation | -MVDVEEKSQEVEYV -CCCHHHHCCEEEEE | 43.89 | 25381059 | |
| 7 | Ubiquitination | -MVDVEEKSQEVEYV -CCCHHHHCCEEEEE | 43.89 | 17644757 | |
| 8 | Phosphorylation | MVDVEEKSQEVEYVD CCCHHHHCCEEEEEC | 34.55 | 22369663 | |
| 13 | Phosphorylation | EKSQEVEYVDPTVNR HHCCEEEEECCCCCC | 18.48 | 28889911 | |
| 17 | Phosphorylation | EVEYVDPTVNRVPNY EEEEECCCCCCCCCC | 26.42 | 26447709 | |
| 24 | Phosphorylation | TVNRVPNYEVSEKAF CCCCCCCCCCCHHHH | 16.19 | 26447709 | |
| 27 | Phosphorylation | RVPNYEVSEKAFLLT CCCCCCCCHHHHHHH | 22.80 | 26447709 | |
| 29 | Ubiquitination | PNYEVSEKAFLLTQS CCCCCCHHHHHHHCC | 36.61 | 23749301 | |
| 34 | Phosphorylation | SEKAFLLTQSKVSIE CHHHHHHHCCCCCHH | 32.70 | 24909858 | |
| 36 | Phosphorylation | KAFLLTQSKVSIEQR HHHHHHCCCCCHHHH | 29.77 | 21440633 | |
| 53 | Ubiquitination | AAEFVLAKIKEEEMA HHHHHHHHCCHHHCH | 50.58 | 17644757 | |
| 55 | Ubiquitination | EFVLAKIKEEEMAPY HHHHHHCCHHHCHHH | 59.37 | 17644757 | |
| 64 | Ubiquitination | EEMAPYYKYLCEEYL HHCHHHHHHHHHHHH | 26.38 | 17644757 | |
| 70 | Phosphorylation | YKYLCEEYLVNNGQS HHHHHHHHHHHCCCC | 8.15 | 19779198 | |
| 77 | Phosphorylation | YLVNNGQSDLEHDEK HHHHCCCCCCCCCCC | 45.63 | 21551504 | |
| 85 | Phosphorylation | DLEHDEKSDSLNEWI CCCCCCCCCCHHHHH | 30.31 | 21440633 | |
| 87 | Phosphorylation | EHDEKSDSLNEWIKF CCCCCCCCHHHHHHH | 39.94 | 21440633 | |
| 104 | Acetylation | ELYNELCKKNESKIK HHHHHHHHHCHHHHH | 71.85 | 24489116 | |
| 190 | Acetylation | DQLYVKEKLEAVNSM CEEHHHHHHHHHHHH | 46.00 | 24489116 | |
| 196 | Phosphorylation | EKLEAVNSMIEKGGD HHHHHHHHHHHCCCC | 17.97 | 27821475 | |
| 200 | Acetylation | AVNSMIEKGGDWERR HHHHHHHCCCCHHHH | 58.21 | 24489116 | |
| 405 | Acetylation | AQYHLLVKQGDGLLT CEEEEEEECCCCHHH | 48.83 | 24489116 | |
| 405 | Ubiquitination | AQYHLLVKQGDGLLT CEEEEEEECCCCHHH | 48.83 | 24961812 | |
| 413 | Acetylation | QGDGLLTKLQKYGAA CCCCHHHHHHHHCCE | 49.22 | 24489116 | |
| 416 | Acetylation | GLLTKLQKYGAAVRL CHHHHHHHHCCEEEE | 56.97 | 24489116 | |
| 416 | Ubiquitination | GLLTKLQKYGAAVRL CHHHHHHHHCCEEEE | 56.97 | 23749301 | |
| 426 | Phosphorylation | AAVRLTGSDRV---- CEEEECCCCCC---- | 19.60 | 21440633 |
| 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 RPN7_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN7_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 RPN7_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-77, AND MASSSPECTROMETRY. | |
