| UniProt ID | GRE3_YEAST | |
|---|---|---|
| UniProt AC | P38715 | |
| Protein Name | NADPH-dependent aldose reductase GRE3 {ECO:0000305|PubMed:11525399} | |
| Gene Name | GRE3 {ECO:0000303|PubMed:10407268} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 327 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)-lactaldehyde under stress conditions. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. [PubMed: 11525399 In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable)] | |
| Protein Sequence | MSSLVTLNNGLKMPLVGLGCWKIDKKVCANQIYEAIKLGYRLFDGACDYGNEKEVGEGIRKAISEGLVSRKDIFVVSKLWNNFHHPDHVKLALKKTLSDMGLDYLDLYYIHFPIAFKYVPFEEKYPPGFYTGADDEKKGHITEAHVPIIDTYRALEECVDEGLIKSIGVSNFQGSLIQDLLRGCRIKPVALQIEHHPYLTQEHLVEFCKLHDIQVVAYSSFGPQSFIEMDLQLAKTTPTLFENDVIKKVSQNHPGSTTSQVLLRWATQRGIAVIPKSSKKERLLGNLEIEKKFTLTEQELKDISALNANIRFNDPWTWLDGKFPTFA | |
| 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 | ------MSSLVTLNN ------CCCCEECCC | 32.17 | 21126336 | |
| 53 | Acetylation | ACDYGNEKEVGEGIR CCCCCCHHHHHHHHH | 62.79 | 24489116 | |
| 125 | Phosphorylation | YVPFEEKYPPGFYTG CCCHHHCCCCCCCCC | 20.24 | 22369663 | |
| 130 | Phosphorylation | EKYPPGFYTGADDEK HCCCCCCCCCCCCCC | 15.35 | 22369663 | |
| 131 | Phosphorylation | KYPPGFYTGADDEKK CCCCCCCCCCCCCCC | 24.51 | 22369663 | |
| 291 | Acetylation | LGNLEIEKKFTLTEQ HCCCEEEECEECCHH | 59.87 | 24489116 | |
| 294 | Phosphorylation | LEIEKKFTLTEQELK CEEEECEECCHHHHH | 41.47 | 22369663 | |
| 296 | Phosphorylation | IEKKFTLTEQELKDI EEECEECCHHHHHHH | 32.34 | 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 GRE3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GRE3_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 GRE3_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-294, AND MASSSPECTROMETRY. | |
