| UniProt ID | PSA5_YEAST | |
|---|---|---|
| UniProt AC | P32379 | |
| Protein Name | Proteasome subunit alpha type-5 | |
| Gene Name | PUP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 260 | |
| 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 | MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELIKELKEKEAAESPEEADVEMS | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MFLTRSEYDRG ----CCCCHHHCCCC | 22.38 | 22369663 | |
| 6 | Phosphorylation | --MFLTRSEYDRGVS --CCCCHHHCCCCCC | 34.96 | 22369663 | |
| 8 | Phosphorylation | MFLTRSEYDRGVSTF CCCCHHHCCCCCCCC | 16.52 | 22369663 | |
| 13 | Phosphorylation | SEYDRGVSTFSPEGR HHCCCCCCCCCCCCC | 26.93 | 22369663 | |
| 14 | Phosphorylation | EYDRGVSTFSPEGRL HCCCCCCCCCCCCCE | 26.23 | 28132839 | |
| 16 | Phosphorylation | DRGVSTFSPEGRLFQ CCCCCCCCCCCCEEE | 23.33 | 22369663 | |
| 27 | Phosphorylation | RLFQVEYSLEAIKLG CEEEEEEEEEEHHHC | 13.26 | 30377154 | |
| 35 | Phosphorylation | LEAIKLGSTAIGIAT EEEHHHCCCEEEEEE | 25.71 | 21440633 | |
| 43 | Ubiquitination | TAIGIATKEGVVLGV CEEEEEECCCEEEEE | 43.37 | 24961812 | |
| 55 | Phosphorylation | LGVEKRATSPLLESD EEEECCCCCCCCCCC | 34.60 | 22369663 | |
| 56 | Phosphorylation | GVEKRATSPLLESDS EEECCCCCCCCCCCC | 16.74 | 25521595 | |
| 61 | Phosphorylation | ATSPLLESDSIEKIV CCCCCCCCCCHHHHH | 36.31 | 22369663 | |
| 63 | Phosphorylation | SPLLESDSIEKIVEI CCCCCCCCHHHHHHH | 41.76 | 22369663 | |
| 87 | Phosphorylation | GLTADARSMIEHART CCCHHHHHHHHHHHH | 26.32 | 25752575 | |
| 128 | Phosphorylation | LRFGEGASGEERLMS HHHCCCCCHHHHHHC | 58.56 | 22369663 | |
| 170 | Ubiquitination | TFYRYNAKAIGSGSE CEEEEEEEEECCCCH | 36.58 | 23749301 | |
| 202 | Ubiquitination | EAELLVLKILKQVME HHHHHHHHHHHHHHH | 38.21 | 23749301 | |
| 205 | Acetylation | LLVLKILKQVMEEKL HHHHHHHHHHHHHHC | 44.30 | 22865919 | |
| 205 | Ubiquitination | LLVLKILKQVMEEKL HHHHHHHHHHHHHHC | 44.30 | 23749301 | |
| 211 | Acetylation | LKQVMEEKLDENNAQ HHHHHHHHCCCCCCC | 48.18 | 24489116 | |
| 211 | Ubiquitination | LKQVMEEKLDENNAQ HHHHHHHHCCCCCCC | 48.18 | 23749301 | |
| 224 | Ubiquitination | AQLSCITKQDGFKIY CCCEEEECCCCCEEE | 26.87 | 23749301 | |
| 229 | Acetylation | ITKQDGFKIYDNEKT EECCCCCEEECCHHH | 45.98 | 24489116 | |
| 235 | Acetylation | FKIYDNEKTAELIKE CEEECCHHHHHHHHH | 60.33 | 24489116 | |
| 235 | Ubiquitination | FKIYDNEKTAELIKE CEEECCHHHHHHHHH | 60.33 | 23749301 | |
| 246 | Ubiquitination | LIKELKEKEAAESPE HHHHHHHHHHHCCHH | 51.57 | 23749301 | |
| 251 | Phosphorylation | KEKEAAESPEEADVE HHHHHHCCHHHHCCC | 32.65 | 22369663 | |
| 260 | Phosphorylation | EEADVEMS------- HHHCCCCC------- | 24.46 | 22890988 |
| 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 PSA5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA5_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 PSA5_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-35; SER-56; SER-87;SER-251 AND SER-260, AND MASS SPECTROMETRY. | |
| "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 THR-55 AND SER-56, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-56 AND SER-251,AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, AND MASSSPECTROMETRY. | |
