| UniProt ID | PSA4_YEAST | |
|---|---|---|
| UniProt AC | P40303 | |
| Protein Name | Proteasome subunit alpha type-4 | |
| Gene Name | PRE6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 254 | |
| 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 | MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQQEQDKKKKSNH | |
| 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 |
|---|---|---|---|---|---|
| 28 | Ubiquitination | EYALEAVKRGTCAVG HHHHHHHHHCCCEEE | 30.18 | 17644757 | |
| 31 | Phosphorylation | LEAVKRGTCAVGVKG HHHHHHCCCEEECCC | 26.89 | 23749301 | |
| 37 | Ubiquitination | GTCAVGVKGKNCVVL CCCEEECCCCCEEEE | 10.93 | 23749301 | |
| 39 | Ubiquitination | CAVGVKGKNCVVLGC CEEECCCCCEEEEEC | 2.17 | 23749301 | |
| 50 | Phosphorylation | VLGCERRSTLKLQDT EEECCCCCCEEEECC | 33.74 | 21440633 | |
| 53 | Acetylation | CERRSTLKLQDTRIT CCCCCCEEEECCEEC | 21.01 | 25381059 | |
| 53 | Ubiquitination | CERRSTLKLQDTRIT CCCCCCEEEECCEEC | 21.01 | 23749301 | |
| 60 | Phosphorylation | KLQDTRITPSKVSKI EEECCEECHHHHHCC | 33.00 | 20486117 | |
| 62 | Phosphorylation | QDTRITPSKVSKIDS ECCEECHHHHHCCCC | 42.74 | 27017623 | |
| 63 | Ubiquitination | DTRITPSKVSKIDSH CCEECHHHHHCCCCE | 38.95 | 22817900 | |
| 66 | Ubiquitination | ITPSKVSKIDSHVVL ECHHHHHCCCCEEEE | 3.57 | 22817900 | |
| 69 | Phosphorylation | SKVSKIDSHVVLSFS HHHHCCCCEEEEEEC | 6.73 | 20486117 | |
| 74 | Phosphorylation | IDSHVVLSFSGLNAD CCCEEEEEECCCCCC | 6.75 | 22369663 | |
| 88 | Ubiquitination | DSRILIEKARVEAQS CCEEEEEHHHHHHHH | 5.45 | 22817900 | |
| 88 | Acetylation | DSRILIEKARVEAQS CCEEEEEHHHHHHHH | 5.45 | 24489116 | |
| 146 | Ubiquitination | DPRDDEPKLYQTEPS CCCCCCCCCEECCCC | 6.09 | 17644757 | |
| 169 | Ubiquitination | QTIGRNSKTVREFLE CCCCCCCHHHHHHHH | 21.14 | 22817900 | |
| 177 | Acetylation | TVREFLEKNYDRKEP HHHHHHHHCCCCCCC | 26.30 | 24489116 | |
| 177 | Succinylation | TVREFLEKNYDRKEP HHHHHHHHCCCCCCC | 26.30 | 23954790 | |
| 187 | Phosphorylation | DRKEPPATVEECVKL CCCCCCCCHHHHHHH | 33.82 | 28889911 |
| 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 PSA4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA4_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 PSA4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Ubiquitylation | |
| Reference | PubMed |
| "A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery."; Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-199, AND MASSSPECTROMETRY. | |
