| UniProt ID | RPE_YEAST | |
|---|---|---|
| UniProt AC | P46969 | |
| Protein Name | Ribulose-phosphate 3-epimerase | |
| Gene Name | RPE1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 238 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate (By similarity). Involved in the protective response to oxidative stress.. | |
| Protein Sequence | MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCHMMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD | |
| 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 |
|---|---|---|---|---|---|
| 59 | Phosphorylation | IVTSLRRSVPRPGDA CHHHHHHCCCCCCCC | 30.00 | 22369663 | |
| 67 | Phosphorylation | VPRPGDASNTEKKPT CCCCCCCCCCCCCCC | 49.37 | 22369663 | |
| 69 | Phosphorylation | RPGDASNTEKKPTAF CCCCCCCCCCCCCEE | 46.84 | 22369663 | |
| 116 | Acetylation | QDPLHLVKLIKSKGI CCHHHHHHHHHCCCC | 51.35 | 25381059 | |
| 176 | Acetylation | KVETLRAKFPHLNIQ HHHHHHHHCCCCEEE | 53.66 | 24489116 | |
| 221 | Phosphorylation | ADPHDVISFMKEEVS CCHHHHHHHHHHHHH | 21.09 | 28889911 | |
| 229 | Acetylation | FMKEEVSKELRSRDL HHHHHHHHHHHHCCC | 66.98 | 22865919 |
| 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 RPE_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPE_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 RPE_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-221, AND MASSSPECTROMETRY. | |