| UniProt ID | PLR1_YEAST | |
|---|---|---|
| UniProt AC | Q06494 | |
| Protein Name | Putative pyridoxal reductase | |
| Gene Name | YPR127W | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 345 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).. | |
| Protein Sequence | MSVADLKNNIHKLDTGYGLMSLTWRAEPIPQSQAFEAMHRVVELSRERGHKAFFNVGEFYGPDFINLSYVHDFFAKYPDLRKDVVISCKGGADNATLTPRGSHDDVVQSVKNSVSAIGGYIDIFEVARIDTSLCTKGEVYPYESFEALAEMISEGVIGGISLSEVNEEQIRAIHKDWGKFLTCVEVELSLFSNDILHNGIAKTCAELGLSIICYSPLGRGLLTGQLKSNADIPEGDFRKSLKRFSDESLKKNLTLVRFLQEEIVDKRPQNNSITLAQLALGWVKHWNKVPEYSGAKFIPIPSGSSISKVNENFDEQKTKLTDQEFNAINKYLTTFHTVGDRYEMA | |
| 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 | Acetylation | -MSVADLKNNIHKLD -CCHHHHHHCCCCCC | 48.79 | 24489116 | |
| 32 | Phosphorylation | RAEPIPQSQAFEAMH ECEECCHHHHHHHHH | 20.37 | 22369663 | |
| 87 | Phosphorylation | LRKDVVISCKGGADN CCCCEEEEECCCCCC | 9.73 | 27214570 | |
| 89 | Ubiquitination | KDVVISCKGGADNAT CCEEEEECCCCCCCE | 54.30 | 23749301 | |
| 96 | Phosphorylation | KGGADNATLTPRGSH CCCCCCCEECCCCCH | 37.10 | 22369663 | |
| 98 | Phosphorylation | GADNATLTPRGSHDD CCCCCEECCCCCHHH | 13.44 | 22369663 | |
| 245 | Phosphorylation | RKSLKRFSDESLKKN HHHHHHCCHHHHHHH | 44.49 | 22369663 | |
| 248 | Phosphorylation | LKRFSDESLKKNLTL HHHCCHHHHHHHHHH | 50.94 | 22369663 | |
| 296 | Ubiquitination | VPEYSGAKFIPIPSG CCCCCCCCEEECCCC | 47.56 | 24961812 | |
| 305 | Phosphorylation | IPIPSGSSISKVNEN EECCCCCCHHHHCCC | 34.11 | 21440633 | |
| 308 | Acetylation | PSGSSISKVNENFDE CCCCCHHHHCCCCCH | 47.62 | 24489116 | |
| 319 | Acetylation | NFDEQKTKLTDQEFN CCCHHHHHCCHHHHH | 57.32 | 24489116 |
| 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 PLR1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PLR1_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 PLR1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PLR1_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-87 AND THR-98, AND MASSSPECTROMETRY. | |
