| UniProt ID | PRS6A_YEAST | |
|---|---|---|
| UniProt AC | P33297 | |
| Protein Name | 26S proteasome regulatory subunit 6A | |
| Gene Name | RPT5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 434 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).. | |
| Protein Sequence | MATLEELDAQTLPGDDELDQEILNLSTQELQTRAKLLDNEIRIFRSELQRLSHENNVMLEKIKDNKEKIKNNRQLPYLVANVVEVMDMNEIEDKENSESTTQGGNVNLDNTAVGKAAVVKTSSRQTVFLPMVGLVDPDKLKPNDLVGVNKDSYLILDTLPSEFDSRVKAMEVDEKPTETYSDVGGLDKQIEELVEAIVLPMKRADKFKDMGIRAPKGALMYGPPGTGKTLLARACAAQTNATFLKLAAPQLVQMYIGEGAKLVRDAFALAKEKAPTIIFIDELDAIGTKRFDSEKSGDREVQRTMLELLNQLDGFSSDDRVKVLAATNRVDVLDPALLRSGRLDRKIEFPLPSEDSRAQILQIHSRKMTTDDDINWQELARSTDEFNGAQLKAVTVEAGMIALRNGQSSVKHEDFVEGISEVQARKSKSVSFYA | |
| 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 | Acetylation | ------MATLEELDA ------CCCHHHHHH | 22.38 | 22814378 | |
| 3 | Phosphorylation | -----MATLEELDAQ -----CCCHHHHHHC | 33.14 | 23607784 | |
| 11 | Phosphorylation | LEELDAQTLPGDDEL HHHHHHCCCCCCHHH | 36.32 | 20486117 | |
| 26 | Phosphorylation | DQEILNLSTQELQTR HHHHHHCCHHHHHHH | 27.29 | 23607784 | |
| 27 | Phosphorylation | QEILNLSTQELQTRA HHHHHCCHHHHHHHH | 29.27 | 23607784 | |
| 32 | Phosphorylation | LSTQELQTRAKLLDN CCHHHHHHHHHHHHH | 45.26 | 24909858 | |
| 35 | Acetylation | QELQTRAKLLDNEIR HHHHHHHHHHHHHHH | 46.41 | 25381059 | |
| 35 | Ubiquitination | QELQTRAKLLDNEIR HHHHHHHHHHHHHHH | 46.41 | 23749301 | |
| 52 | Phosphorylation | RSELQRLSHENNVML HHHHHHHHHHCCCCH | 30.83 | 24909858 | |
| 61 | Ubiquitination | ENNVMLEKIKDNKEK HCCCCHHHHHCCHHH | 51.61 | 17644757 | |
| 61 | Acetylation | ENNVMLEKIKDNKEK HCCCCHHHHHCCHHH | 51.61 | 24489116 | |
| 97 | Phosphorylation | EIEDKENSESTTQGG HHCCCCCCCCCCCCC | 33.73 | 28889911 | |
| 121 | Phosphorylation | GKAAVVKTSSRQTVF CCEEEEECCCCCEEE | 21.96 | 22369663 | |
| 122 | Phosphorylation | KAAVVKTSSRQTVFL CEEEEECCCCCEEEE | 20.15 | 21440633 | |
| 123 | Phosphorylation | AAVVKTSSRQTVFLP EEEEECCCCCEEEEE | 33.37 | 21440633 | |
| 126 | Phosphorylation | VKTSSRQTVFLPMVG EECCCCCEEEEEECC | 16.47 | 22369663 | |
| 139 | Ubiquitination | VGLVDPDKLKPNDLV CCCCCHHHCCCCCCC | 64.89 | 17644757 | |
| 141 | Ubiquitination | LVDPDKLKPNDLVGV CCCHHHCCCCCCCCC | 47.73 | 23749301 | |
| 150 | Ubiquitination | NDLVGVNKDSYLILD CCCCCCCCCCEEEEE | 45.72 | 17644757 | |
| 152 | Phosphorylation | LVGVNKDSYLILDTL CCCCCCCCEEEEECC | 24.37 | 21440633 | |
| 153 | Phosphorylation | VGVNKDSYLILDTLP CCCCCCCEEEEECCC | 14.11 | 21440633 | |
| 175 | Ubiquitination | KAMEVDEKPTETYSD CEEECCCCCCCCCCC | 53.42 | 23749301 | |
| 175 | Acetylation | KAMEVDEKPTETYSD CEEECCCCCCCCCCC | 53.42 | 24489116 | |
| 177 | Phosphorylation | MEVDEKPTETYSDVG EECCCCCCCCCCCCC | 52.61 | 22369663 | |
| 179 | Phosphorylation | VDEKPTETYSDVGGL CCCCCCCCCCCCCCH | 30.70 | 22369663 | |
| 180 | Phosphorylation | DEKPTETYSDVGGLD CCCCCCCCCCCCCHH | 9.17 | 22369663 | |
| 181 | Phosphorylation | EKPTETYSDVGGLDK CCCCCCCCCCCCHHH | 32.99 | 22369663 | |
| 202 | Ubiquitination | EAIVLPMKRADKFKD HHHHHCCCCHHHHHH | 42.36 | 24961812 | |
| 208 | Ubiquitination | MKRADKFKDMGIRAP CCCHHHHHHCCCCCC | 53.17 | 23749301 | |
| 221 | Phosphorylation | APKGALMYGPPGTGK CCCCCEEECCCCCCH | 27.59 | 27017623 | |
| 226 | Phosphorylation | LMYGPPGTGKTLLAR EEECCCCCCHHHHHH | 41.08 | 27017623 | |
| 228 | Ubiquitination | YGPPGTGKTLLARAC ECCCCCCHHHHHHHH | 35.52 | 22817900 | |
| 229 | Phosphorylation | GPPGTGKTLLARACA CCCCCCHHHHHHHHH | 28.48 | 27017623 | |
| 245 | Ubiquitination | QTNATFLKLAAPQLV HCCCHHHHHHHHHHH | 31.71 | 17644757 | |
| 261 | Ubiquitination | MYIGEGAKLVRDAFA HHHHCHHHHHHHHHH | 59.37 | 17644757 | |
| 273 | Ubiquitination | AFALAKEKAPTIIFI HHHHHHCCCCEEEEE | 59.98 | 17644757 | |
| 289 | Ubiquitination | ELDAIGTKRFDSEKS CCCCCCCCCCCCCCC | 45.94 | 17644757 | |
| 322 | Ubiquitination | FSSDDRVKVLAATNR CCCHHHHHHHHCCCC | 32.21 | 17644757 | |
| 346 | Ubiquitination | RSGRLDRKIEFPLPS HCCCCCCEEECCCCC | 46.37 | 17644757 | |
| 367 | Ubiquitination | ILQIHSRKMTTDDDI HHHHHHCCCCCCCCC | 43.54 | 17644757 | |
| 369 | Phosphorylation | QIHSRKMTTDDDINW HHHHCCCCCCCCCCH | 30.06 | 20486117 | |
| 370 | Phosphorylation | IHSRKMTTDDDINWQ HHHCCCCCCCCCCHH | 33.65 | 20486117 | |
| 411 | Acetylation | RNGQSSVKHEDFVEG CCCCCCCCHHHHCCC | 43.13 | 24489116 | |
| 420 | Phosphorylation | EDFVEGISEVQARKS HHHCCCHHHHHHHHC | 42.44 | 27017623 | |
| 426 | Ubiquitination | ISEVQARKSKSVSFY HHHHHHHHCCCCCCC | 66.31 | 22817900 | |
| 428 | Ubiquitination | EVQARKSKSVSFYA- HHHHHHCCCCCCCC- | 58.89 | 23749301 |
| 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 PRS6A_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRS6A_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 PRS6A_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 2-9, AND ACETYLATION AT ALA-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 THR-27 AND SER-181, AND MASSSPECTROMETRY. | |
| "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-181, AND MASSSPECTROMETRY. | |
