| UniProt ID | PSA2_YEAST | |
|---|---|---|
| UniProt AC | P23639 | |
| Protein Name | Proteasome subunit alpha type-2 | |
| Gene Name | PRE8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 250 | |
| 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 | MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETLSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWNDELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTSQEINDRLEAL | |
| 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 | ------MTDRYSFSL ------CCCCCEEEE | 29.23 | 30377154 | |
| 6 | Phosphorylation | --MTDRYSFSLTTFS --CCCCCEEEEEEEC | 14.84 | 28889911 | |
| 10 | Phosphorylation | DRYSFSLTTFSPSGK CCCEEEEEEECCCCC | 25.29 | 28132839 | |
| 11 | Phosphorylation | RYSFSLTTFSPSGKL CCEEEEEEECCCCCH | 27.66 | 28132839 | |
| 13 | Phosphorylation | SFSLTTFSPSGKLGQ EEEEEEECCCCCHHH | 18.96 | 21082442 | |
| 15 | Phosphorylation | SLTTFSPSGKLGQID EEEEECCCCCHHHHH | 47.57 | 24961812 | |
| 17 | Ubiquitination | TTFSPSGKLGQIDYA EEECCCCCHHHHHHH | 54.50 | 24961812 | |
| 29 | Ubiquitination | DYALTAVKQGVTSLG HHHHHHHHHCCCCEE | 38.58 | 23749301 | |
| 49 | Ubiquitination | GVVIATEKKSSSPLA CEEEEECCCCCCCCC | 54.31 | 17644757 | |
| 50 | Ubiquitination | VVIATEKKSSSPLAM EEEEECCCCCCCCCC | 49.71 | 17644757 | |
| 51 | Phosphorylation | VIATEKKSSSPLAMS EEEECCCCCCCCCCH | 47.30 | 22369663 | |
| 52 | Phosphorylation | IATEKKSSSPLAMSE EEECCCCCCCCCCHH | 44.87 | 21440633 | |
| 53 | Phosphorylation | ATEKKSSSPLAMSET EECCCCCCCCCCHHH | 30.90 | 22369663 | |
| 58 | Phosphorylation | SSSPLAMSETLSKVS CCCCCCCHHHHHHHH | 23.09 | 25371407 | |
| 60 | Phosphorylation | SPLAMSETLSKVSLL CCCCCHHHHHHHHHC | 29.08 | 22369663 | |
| 62 | Phosphorylation | LAMSETLSKVSLLTP CCCHHHHHHHHHCCC | 38.13 | 22369663 | |
| 63 | Ubiquitination | AMSETLSKVSLLTPD CCHHHHHHHHHCCCC | 38.67 | 17644757 | |
| 88 | Ubiquitination | DYRVLVDKSRKVAHT CEEEEEECCCCEECC | 44.68 | 23749301 | |
| 88 | 2-Hydroxyisobutyrylation | DYRVLVDKSRKVAHT CEEEEEECCCCEECC | 44.68 | - | |
| 98 | Acetylation | KVAHTSYKRIYGEYP CEECCCHHHHHCCCC | 31.89 | 25381059 | |
| 101 | Phosphorylation | HTSYKRIYGEYPPTK CCCHHHHHCCCCCHH | 14.13 | 19823750 | |
| 104 | Phosphorylation | YKRIYGEYPPTKLLV HHHHHCCCCCHHHHH | 15.34 | 19823750 | |
| 107 | Phosphorylation | IYGEYPPTKLLVSEV HHCCCCCHHHHHHHH | 29.80 | 19823750 | |
| 108 | Ubiquitination | YGEYPPTKLLVSEVA HCCCCCHHHHHHHHH | 45.67 | 23749301 | |
| 108 | Acetylation | YGEYPPTKLLVSEVA HCCCCCHHHHHHHHH | 45.67 | 24489116 | |
| 112 | Phosphorylation | PPTKLLVSEVAKIMQ CCHHHHHHHHHHHHH | 26.73 | 19823750 | |
| 166 | Ubiquitination | WKATAIGKGSVAAKT EEEEEECCCCHHHHH | 41.73 | 23749301 | |
| 168 | Phosphorylation | ATAIGKGSVAAKTFL EEEECCCCHHHHHHH | 16.45 | 23749301 | |
| 172 | Ubiquitination | GKGSVAAKTFLEKRW CCCCHHHHHHHHHHC | 30.03 | 23749301 | |
| 172 | Acetylation | GKGSVAAKTFLEKRW CCCCHHHHHHHHHHC | 30.03 | 24489116 | |
| 177 | 2-Hydroxyisobutyrylation | AAKTFLEKRWNDELE HHHHHHHHHCCCCCC | 65.93 | - | |
| 237 | Ubiquitination | DKGPRFRKLTSQEIN CCCHHHHHCCHHHHH | 54.10 | 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 PSA2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA2_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 PSA2_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-13 AND SER-53, AND MASSSPECTROMETRY. | |
