| UniProt ID | PSB5_YEAST | |
|---|---|---|
| UniProt AC | P30656 | |
| Protein Name | Proteasome subunit beta type-5 | |
| Gene Name | PRE2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 287 | |
| 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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.; This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins.. | |
| Protein Sequence | MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHTDDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG | |
| 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 |
|---|---|---|---|---|---|
| 51 | Phosphorylation | LTVPPIASPQQFLRA CCCCCCCCHHHHHHH | 24.78 | 28152593 | |
| 107 | Ubiquitination | WVASQTVKKVIEINP HHHHHHHHHHHCCCH | 44.72 | 23749301 | |
| 108 | Ubiquitination | VASQTVKKVIEINPF HHHHHHHHHHCCCHH | 44.07 | 22817900 | |
| 156 | Ubiquitination | ISVAAASKILSNLVY HHHHHHHHHHHHHHH | 42.83 | 23749301 | |
| 165 | Phosphorylation | LSNLVYQYKGAGLSM HHHHHHHCCCCCCCC | 8.16 | 28889911 | |
| 174 | Phosphorylation | GAGLSMGTMICGYTR CCCCCCCCEECCCCC | 8.50 | 27017623 | |
| 179 | Phosphorylation | MGTMICGYTRKEGPT CCCEECCCCCCCCCE | 10.04 | 27017623 | |
| 180 | Phosphorylation | GTMICGYTRKEGPTI CCEECCCCCCCCCEE | 22.13 | 27017623 | |
| 182 | Ubiquitination | MICGYTRKEGPTIYY EECCCCCCCCCEEEE | 60.26 | 23749301 | |
| 235 | Phosphorylation | ALYLGKRSILAAAHR HHHHCHHHHHHHHHC | 25.99 | 21440633 | |
| 274 | Ubiquitination | DVGELFWKVKEEEGS CHHHHEEEEECCCCC | 35.77 | 17644757 | |
| 276 | Ubiquitination | GELFWKVKEEEGSFN HHHEEEEECCCCCCC | 56.53 | 23749301 | |
| 281 | Phosphorylation | KVKEEEGSFNNVIG- EEECCCCCCCCCCC- | 28.25 | 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 PSB5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSB5_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 PSB5_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-51, AND MASSSPECTROMETRY. | |
