| UniProt ID | PSA3_YEAST | |
|---|---|---|
| UniProt AC | P23638 | |
| Protein Name | Proteasome subunit alpha type-3 | |
| Gene Name | PRE9 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 258 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.. | |
| Protein Sequence | MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDYKDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILVKTGITKKDEDEEADEDMK | |
| 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 |
|---|---|---|---|---|---|
| 14 | Phosphorylation | DSRTTIFSPEGRLYQ CCCCEEECCCCCEEE | 6.87 | 28152593 | |
| 51 | Acetylation | IVLAAERKVTSTLLE EEEEEECHHHHHHHC | 38.42 | 24489116 | |
| 51 | Ubiquitination | IVLAAERKVTSTLLE EEEEEECHHHHHHHC | 38.42 | 23749301 | |
| 53 | Phosphorylation | LAAERKVTSTLLEQD EEEECHHHHHHHCCC | 3.06 | 21126336 | |
| 62 | Phosphorylation | TLLEQDTSTEKLYKL HHHCCCCCHHHHHHH | 42.34 | 29734811 | |
| 65 | Acetylation | EQDTSTEKLYKLNDK CCCCCHHHHHHHCHH | 8.12 | 24489116 | |
| 65 | Ubiquitination | EQDTSTEKLYKLNDK CCCCCHHHHHHHCHH | 8.12 | 23749301 | |
| 68 | Ubiquitination | TSTEKLYKLNDKIAV CCHHHHHHHCHHHHH | 24.38 | 22817900 | |
| 68 | Acetylation | TSTEKLYKLNDKIAV CCHHHHHHHCHHHHH | 24.38 | 25381059 | |
| 100 | Ubiquitination | IHAQNYLKTYNEDIP HHHHHHHHHCCCCCC | 39.10 | 23749301 | |
| 100 | Acetylation | IHAQNYLKTYNEDIP HHHHHHHHHCCCCCC | 39.10 | 24489116 | |
| 116 | Phosphorylation | EILVRRLSDIKQGYT HHHHHHHHHHCCCCC | 5.29 | 21440633 | |
| 195 | Ubiquitination | DAIELALKTLSKTTD HHHHHHHHHHCCCCC | 39.70 | 22817900 | |
| 199 | Ubiquitination | LALKTLSKTTDSSAL HHHHHHCCCCCCCCC | 1.83 | 23749301 | |
| 218 | Ubiquitination | LEFATIRKGANDGEV EEEEEEECCCCCCHH | 4.95 | 24961812 | |
| 228 | Ubiquitination | NDGEVYQKIFKPQEI CCCHHHHHHCCHHHH | 23.94 | 22817900 | |
| 231 | Ubiquitination | EVYQKIFKPQEIKDI HHHHHHCCHHHHHHH | 8.92 | 23749301 | |
| 236 | Succinylation | IFKPQEIKDILVKTG HCCHHHHHHHHHHHC | 5.28 | 23954790 | |
| 236 | Ubiquitination | IFKPQEIKDILVKTG HCCHHHHHHHHHHHC | 5.28 | 23749301 | |
| 236 | Acetylation | IFKPQEIKDILVKTG HCCHHHHHHHHHHHC | 5.28 | 24489116 | |
| 241 | Ubiquitination | EIKDILVKTGITKKD HHHHHHHHHCCCCCC | 39.62 | 22817900 | |
| 246 | Ubiquitination | LVKTGITKKDEDEEA HHHHCCCCCCCCHHH | 29.61 | 23749301 | |
| 247 | Ubiquitination | VKTGITKKDEDEEAD HHHCCCCCCCCHHHH | 10.08 | 23749301 | |
| 258 | Ubiquitination | EEADEDMK------- HHHHHHCC------- | 43.32 | 15699485 |
| 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 PSA3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA3_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 PSA3_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 THR-278 AND THR-279, ANDMASS SPECTROMETRY. | |
