| UniProt ID | TSA1_YEAST | |
|---|---|---|
| UniProt AC | P34760 | |
| Protein Name | Peroxiredoxin TSA1 {ECO:0000305} | |
| Gene Name | TSA1 {ECO:0000303|PubMed:8344960} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 196 | |
| Subcellular Localization | Cytoplasm . Associates with ribosomes (PubMed:18271751). Colocalizes with sites of protein aggregation adjacent to active mitochondria (PubMed:24424024). | |
| Protein Description | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. [PubMed: 2895105] | |
| Protein Sequence | MVAQVQKQAPTFKKTAVVDGVFDEVSLDKYKGKYVVLAFIPLAFTFVCPTEIIAFSEAAKKFEEQGAQVLFASTDSEYSLLAWTNIPRKEGGLGPINIPLLADTNHSLSRDYGVLIEEEGVALRGLFIIDPKGVIRHITINDLPVGRNVDEALRLVEAFQWTDKNGTVLPCNWTPGAATIKPTVEDSKEYFEAANK | |
| 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 |
|---|---|---|---|---|---|
| 7 | Succinylation | -MVAQVQKQAPTFKK -CCCCCCCCCCCCCC | 49.96 | 23954790 | |
| 7 | 2-Hydroxyisobutyrylation | -MVAQVQKQAPTFKK -CCCCCCCCCCCCCC | 49.96 | - | |
| 13 | Succinylation | QKQAPTFKKTAVVDG CCCCCCCCCEEEEEC | 52.25 | 23954790 | |
| 13 | 2-Hydroxyisobutyrylation | QKQAPTFKKTAVVDG CCCCCCCCCEEEEEC | 52.25 | - | |
| 13 | Ubiquitination | QKQAPTFKKTAVVDG CCCCCCCCCEEEEEC | 52.25 | 23749301 | |
| 14 | Ubiquitination | KQAPTFKKTAVVDGV CCCCCCCCEEEEECC | 37.21 | 23749301 | |
| 26 | Phosphorylation | DGVFDEVSLDKYKGK ECCCEEECHHHCCCC | 28.89 | 22369663 | |
| 29 | Acetylation | FDEVSLDKYKGKYVV CEEECHHHCCCCEEE | 54.90 | 24489116 | |
| 29 | Ubiquitination | FDEVSLDKYKGKYVV CEEECHHHCCCCEEE | 54.90 | 22106047 | |
| 31 | Acetylation | EVSLDKYKGKYVVLA EECHHHCCCCEEEEE | 55.45 | 24489116 | |
| 89 | Acetylation | AWTNIPRKEGGLGPI EEECCCCCCCCCCCC | 56.19 | 24489116 | |
| 89 | Ubiquitination | AWTNIPRKEGGLGPI EEECCCCCCCCCCCC | 56.19 | 23749301 | |
| 104 | Phosphorylation | NIPLLADTNHSLSRD CCCEEECCCCCCCCC | 29.26 | 22369663 | |
| 107 | Phosphorylation | LLADTNHSLSRDYGV EEECCCCCCCCCEEE | 30.06 | 22369663 | |
| 109 | Phosphorylation | ADTNHSLSRDYGVLI ECCCCCCCCCEEEEE | 26.56 | 22369663 | |
| 112 | Phosphorylation | NHSLSRDYGVLIEEE CCCCCCCEEEEEEEC | 14.18 | 21126336 | |
| 132 | Succinylation | GLFIIDPKGVIRHIT EEEEECCCCEEEEEE | 63.16 | 23954790 | |
| 132 | Ubiquitination | GLFIIDPKGVIRHIT EEEEECCCCEEEEEE | 63.16 | 23749301 | |
| 132 | Acetylation | GLFIIDPKGVIRHIT EEEEECCCCEEEEEE | 63.16 | 24489116 | |
| 132 | 2-Hydroxyisobutyrylation | GLFIIDPKGVIRHIT EEEEECCCCEEEEEE | 63.16 | - | |
| 139 | Phosphorylation | KGVIRHITINDLPVG CCEEEEEEECCCCCC | 13.96 | 22369663 | |
| 164 | Succinylation | EAFQWTDKNGTVLPC HHHEEECCCCCEEEC | 50.32 | 23954790 | |
| 164 | Ubiquitination | EAFQWTDKNGTVLPC HHHEEECCCCCEEEC | 50.32 | 22817900 | |
| 167 | Phosphorylation | QWTDKNGTVLPCNWT EEECCCCCEEECCCC | 28.41 | 22369663 | |
| 174 | Phosphorylation | TVLPCNWTPGAATIK CEEECCCCCCCCEEC | 9.61 | 22369663 | |
| 179 | Phosphorylation | NWTPGAATIKPTVED CCCCCCCEECCCCHH | 29.06 | 22369663 | |
| 181 | Acetylation | TPGAATIKPTVEDSK CCCCCEECCCCHHHH | 30.22 | 24489116 | |
| 181 | Ubiquitination | TPGAATIKPTVEDSK CCCCCEECCCCHHHH | 30.22 | 23749301 | |
| 183 | Phosphorylation | GAATIKPTVEDSKEY CCCEECCCCHHHHHH | 31.37 | 22369663 | |
| 187 | Phosphorylation | IKPTVEDSKEYFEAA ECCCCHHHHHHHHHH | 17.55 | 22369663 | |
| 188 | Succinylation | KPTVEDSKEYFEAAN CCCCHHHHHHHHHHC | 69.61 | 23954790 | |
| 188 | Acetylation | KPTVEDSKEYFEAAN CCCCHHHHHHHHHHC | 69.61 | 24489116 | |
| 188 | Ubiquitination | KPTVEDSKEYFEAAN CCCCHHHHHHHHHHC | 69.61 | 17644757 | |
| 190 | Phosphorylation | TVEDSKEYFEAANK- CCHHHHHHHHHHCC- | 15.51 | 26447709 | |
| 196 | Ubiquitination | EYFEAANK------- HHHHHHCC------- | 57.92 | 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 TSA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TSA1_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 TSA1_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-174, AND MASSSPECTROMETRY. | |
