| UniProt ID | RPN8_YEAST | |
|---|---|---|
| UniProt AC | Q08723 | |
| Protein Name | 26S proteasome regulatory subunit RPN8 | |
| Gene Name | RPN8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 338 | |
| 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 | MSLQHEKVTIAPLVLLSALDHYERTQTKENKRCVGVILGDANSSTIRVTNSFALPFEEDEKNSDVWFLDHNYIENMNEMCKKINAKEKLIGWYHSGPKLRASDLKINELFKKYTQNNPLLLIVDVKQQGVGLPTDAYVAIEQVKDDGTSTEKTFLHLPCTIEAEEAEEIGVEHLLRDVRDQAAGGLSIRLTNQLKSLKGLQSKLKDVVEYLDKVINKELPINHTILGKLQDVFNLLPNLGTPDDDEIDVENHDRINISNNLQKALTVKTNDELMVIYISNLVRSIIAFDDLIENKIQNKKIQEQRVKDKQSKVSDDSESESGDKEATAPLIQRKNKKN | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSLQHEKVT ------CCCCCCCCC | 36.41 | 12504901 | |
| 7 | Ubiquitination | -MSLQHEKVTIAPLV -CCCCCCCCCHHHHH | 42.42 | 17644757 | |
| 43 | Phosphorylation | VILGDANSSTIRVTN EEEECCCCCEEEEEC | 30.49 | 20486117 | |
| 44 | Phosphorylation | ILGDANSSTIRVTNS EEECCCCCEEEEECE | 27.88 | 20486117 | |
| 45 | Phosphorylation | LGDANSSTIRVTNSF EECCCCCEEEEECEE | 16.78 | 20486117 | |
| 88 | Acetylation | KKINAKEKLIGWYHS HHCCHHHHHHHCHHC | 44.70 | 24489116 | |
| 98 | Acetylation | GWYHSGPKLRASDLK HCHHCCCCCCHHHHH | 54.88 | 24489116 | |
| 102 | Phosphorylation | SGPKLRASDLKINEL CCCCCCHHHHHHHHH | 36.72 | 28889911 | |
| 105 | Acetylation | KLRASDLKINELFKK CCCHHHHHHHHHHHH | 48.77 | 24489116 | |
| 105 | Ubiquitination | KLRASDLKINELFKK CCCHHHHHHHHHHHH | 48.77 | 23749301 | |
| 111 | Ubiquitination | LKINELFKKYTQNNP HHHHHHHHHHHCCCC | 58.45 | 17644757 | |
| 112 | Ubiquitination | KINELFKKYTQNNPL HHHHHHHHHHCCCCE | 46.31 | 23749301 | |
| 126 | Ubiquitination | LLLIVDVKQQGVGLP EEEEEEHHHCCCCCC | 32.23 | 17644757 | |
| 144 | Acetylation | YVAIEQVKDDGTSTE EEEEEEECCCCCCCC | 50.20 | 24489116 | |
| 144 | Ubiquitination | YVAIEQVKDDGTSTE EEEEEEECCCCCCCC | 50.20 | 23749301 | |
| 152 | Ubiquitination | DDGTSTEKTFLHLPC CCCCCCCEEEEEECE | 44.67 | 17644757 | |
| 195 | Ubiquitination | IRLTNQLKSLKGLQS HHHHHHHHHHHHHHH | 43.93 | 23749301 | |
| 198 | Ubiquitination | TNQLKSLKGLQSKLK HHHHHHHHHHHHHHH | 65.74 | 23749301 | |
| 203 | Ubiquitination | SLKGLQSKLKDVVEY HHHHHHHHHHHHHHH | 46.74 | 22817900 | |
| 205 | Ubiquitination | KGLQSKLKDVVEYLD HHHHHHHHHHHHHHH | 52.81 | 23749301 | |
| 213 | Ubiquitination | DVVEYLDKVINKELP HHHHHHHHHHCCCCC | 42.28 | 17644757 | |
| 213 | Acetylation | DVVEYLDKVINKELP HHHHHHHHHHCCCCC | 42.28 | 24489116 | |
| 217 | Ubiquitination | YLDKVINKELPINHT HHHHHHCCCCCCCCC | 49.88 | 17644757 | |
| 217 | Acetylation | YLDKVINKELPINHT HHHHHHCCCCCCCCC | 49.88 | 22865919 | |
| 228 | Ubiquitination | INHTILGKLQDVFNL CCCCHHHHHHHHHHH | 39.26 | 17644757 | |
| 263 | Ubiquitination | NISNNLQKALTVKTN ECCCCHHHHEEECCC | 48.83 | 23749301 | |
| 295 | Ubiquitination | FDDLIENKIQNKKIQ HHHHHHHHHHCHHHH | 32.64 | 23749301 | |
| 295 | Acetylation | FDDLIENKIQNKKIQ HHHHHHHHHHCHHHH | 32.64 | 24489116 | |
| 311 | Phosphorylation | QRVKDKQSKVSDDSE HHHHHCCCCCCCCCC | 40.54 | 20486117 | |
| 314 | Phosphorylation | KDKQSKVSDDSESES HHCCCCCCCCCCCCC | 39.16 | 22369663 | |
| 317 | Phosphorylation | QSKVSDDSESESGDK CCCCCCCCCCCCCCH | 48.27 | 22369663 | |
| 319 | Phosphorylation | KVSDDSESESGDKEA CCCCCCCCCCCCHHH | 40.80 | 22369663 | |
| 321 | Phosphorylation | SDDSESESGDKEATA CCCCCCCCCCHHHHH | 62.66 | 25521595 | |
| 324 | Acetylation | SESESGDKEATAPLI CCCCCCCHHHHHHHH | 53.42 | 24489116 | |
| 324 | Ubiquitination | SESESGDKEATAPLI CCCCCCCHHHHHHHH | 53.42 | 23749301 | |
| 327 | Phosphorylation | ESGDKEATAPLIQRK CCCCHHHHHHHHHHH | 29.87 | 22369663 |
| 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 RPN8_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN8_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 RPN8_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 2-9, AND ACETYLATION AT SER-2. | |
| 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-44; SER-314; SER-317;SER-319; SER-321 AND THR-327, AND MASS SPECTROMETRY. | |
| "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-314; SER-317; SER-319AND SER-321, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-319, ANDMASS SPECTROMETRY. | |
