| UniProt ID | URE2_YEAST | |
|---|---|---|
| UniProt AC | P23202 | |
| Protein Name | Transcriptional regulator URE2 | |
| Gene Name | URE2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 354 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of genes expressed upon nitrogen limitation. Is also an atypical glutaredoxin without a catalytical cysteine residue. Has glutathione peroxidase and thiol:disulfide oxidoreductase activities in both native and fibrillar form. Also shows insulin disulfide reductase and dehydroascorbic acid reductase (DHAR) actvites.. | |
| Protein Sequence | MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENNIKNTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE | |
| 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 | Acetylation | ------MMNNNGNQV ------CCCCCHHHH | 8.06 | 22814378 | |
| 68 | Phosphorylation | NNSGRNGSQNNDNEN CCCCCCCCCCCCCCC | 33.03 | 29136822 | |
| 78 | Acetylation | NDNENNIKNTLEQHR CCCCCHHHHHHHHHH | 46.10 | 24489116 | |
| 95 | Phosphorylation | QQAFSDMSHVEYSRI HHHHHCCHHHHHHHH | 29.39 | 23749301 | |
| 104 | Acetylation | VEYSRITKFFQEQPL HHHHHHHHHHHCCCC | 41.64 | 24489116 | |
| 104 | Ubiquitination | VEYSRITKFFQEQPL HHHHHHHHHHHCCCC | 41.64 | 23749301 | |
| 240 | Acetylation | FRYFHSQKIASAVER HHHHHHHHHHHHHHH | 43.16 | 24489116 | |
| 276 | Phosphorylation | ALVMELDTENAAAYS HHEEEECCCCHHHHH | 43.70 | 27017623 | |
| 282 | Phosphorylation | DTENAAAYSAGTTPM CCCCHHHHHCCCCCC | 8.37 | 28889911 | |
| 283 | Phosphorylation | TENAAAYSAGTTPMS CCCHHHHHCCCCCCC | 18.59 | 28889911 | |
| 287 | Phosphorylation | AAYSAGTTPMSQSRF HHHHCCCCCCCHHHC | 18.97 | 28889911 | |
| 290 | Phosphorylation | SAGTTPMSQSRFFDY HCCCCCCCHHHCCCC | 26.63 | 28889911 | |
| 292 | Phosphorylation | GTTPMSQSRFFDYPV CCCCCCHHHCCCCCE | 24.61 | 28889911 | |
| 336 | Acetylation | IEFPEVYKWTKHMMR EECHHHHHHHHHHHH | 54.27 | 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 URE2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of URE2_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 URE2_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 TYR-282; SER-283 ANDTHR-287, AND MASS SPECTROMETRY. | |
