| UniProt ID | PHO2_YEAST | |
|---|---|---|
| UniProt AC | P07269 | |
| Protein Name | Regulatory protein PHO2 | |
| Gene Name | PHO2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 559 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Regulator in phosphate metabolism and acts as a derepressor of another central regulator PHO5. Binds to the upstream activator sequence (UAS) of PHO5. It also binds to the TRP4, HIS4, and CYC1 promoters.. | |
| Protein Sequence | MMEEFSYDHDFNTHFATDLDYLQHDQQQQQQQQHDQQHNQQQQPQPQPIQTQNLEHDHDQHTNDMSASSNASDSGPQRPKRTRAKGEALDVLKRKFEINPTPSLVERKKISDLIGMPEKNVRIWFQNRRAKLRKKQHGSNKDTIPSSQSRDIANDYDRGSTDNNLVTTTSTSSIFHDEDLTFFDRIPLNSNNNYYFFDICSITVGSWNRMKSGALQRRNFQSIKELRNLSPIKINNIMSNATDLMVLISKKNSEINYFFSAMANNTKILFRIFFPLSSVTNCSLTLETDDDIINSNNTSDKNNSNTNNDDDNDDNSNEDNDNSSEDKRNAKDNFGELKLTVTRSPTFAVYFLNNAPDEDPNLNNQWSICDDFSEGRQVNDAFVGGSNIPHTLKGLQKSLRFMNSLILDYKSSNEILPTINTAIPTAAVPQQNIAPPFLNTNSSATDSNPNTNLEDSLFFDHDLLSSSITNTNNGQGSNNGRQASKDDTLNLLDTTVNSNNNHNANNEENHLAQEHLSNDADIVANPNDHLLSLPTDSELPNTPDFLKNTNELTDEHRWI | |
| 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 |
|---|---|---|---|---|---|
| 66 | Phosphorylation | DQHTNDMSASSNASD CCCCCCCCCCCCCCC | 28.06 | 27017623 | |
| 68 | Phosphorylation | HTNDMSASSNASDSG CCCCCCCCCCCCCCC | 19.47 | 27017623 | |
| 69 | Phosphorylation | TNDMSASSNASDSGP CCCCCCCCCCCCCCC | 35.81 | 27017623 | |
| 146 | Phosphorylation | SNKDTIPSSQSRDIA CCCCCCCCHHHHCCH | 36.84 | 27214570 | |
| 147 | Phosphorylation | NKDTIPSSQSRDIAN CCCCCCCHHHHCCHH | 27.16 | 27214570 | |
| 149 | Phosphorylation | DTIPSSQSRDIANDY CCCCCHHHHCCHHCC | 33.59 | 30377154 | |
| 170 | Phosphorylation | NNLVTTTSTSSIFHD CCEEECCCCCCCCCC | 24.97 | 19779198 | |
| 171 | Phosphorylation | NLVTTTSTSSIFHDE CEEECCCCCCCCCCC | 25.13 | 19779198 | |
| 173 | Phosphorylation | VTTTSTSSIFHDEDL EECCCCCCCCCCCCC | 29.39 | 19779198 | |
| 194 | Phosphorylation | PLNSNNNYYFFDICS ECCCCCCEEEEEEEE | 12.08 | 28889911 | |
| 195 | Phosphorylation | LNSNNNYYFFDICSI CCCCCCEEEEEEEEE | 10.41 | 28889911 | |
| 201 | Phosphorylation | YYFFDICSITVGSWN EEEEEEEEEEECCHH | 22.94 | 28889911 | |
| 224 | Acetylation | RRNFQSIKELRNLSP HCCHHHHHHHHCCCC | 56.81 | 24489116 | |
| 230 | Phosphorylation | IKELRNLSPIKINNI HHHHHCCCCCEEHHH | 28.29 | 28889911 | |
| 239 | Phosphorylation | IKINNIMSNATDLMV CEEHHHHCCCCCEEE | 21.37 | 29136822 | |
| 242 | Phosphorylation | NNIMSNATDLMVLIS HHHHCCCCCEEEEEE | 33.64 | 29136822 | |
| 249 | Phosphorylation | TDLMVLISKKNSEIN CCEEEEEECCCHHHH | 33.16 | 29136822 | |
| 253 | Phosphorylation | VLISKKNSEINYFFS EEEECCCHHHHHHHH | 49.05 | 29136822 | |
| 257 | Phosphorylation | KKNSEINYFFSAMAN CCCHHHHHHHHHHCC | 16.21 | 29136822 | |
| 260 | Phosphorylation | SEINYFFSAMANNTK HHHHHHHHHHCCCCE | 13.77 | 29136822 | |
| 266 | Phosphorylation | FSAMANNTKILFRIF HHHHCCCCEEEEEEE | 21.19 | 29136822 | |
| 306 | Phosphorylation | SDKNNSNTNNDDDND CCCCCCCCCCCCCCC | 34.91 | 28889911 | |
| 316 | Phosphorylation | DDDNDDNSNEDNDNS CCCCCCCCCCCCCCC | 48.90 | 23749301 | |
| 323 | Phosphorylation | SNEDNDNSSEDKRNA CCCCCCCCHHHHHHH | 37.66 | 28889911 | |
| 324 | Phosphorylation | NEDNDNSSEDKRNAK CCCCCCCHHHHHHHH | 56.95 | 28889911 | |
| 386 | Phosphorylation | NDAFVGGSNIPHTLK CCCCCCCCCCCHHHH | 26.17 | 22369663 | |
| 391 | Phosphorylation | GGSNIPHTLKGLQKS CCCCCCHHHHHHHHH | 25.47 | 22369663 | |
| 542 | Phosphorylation | TDSELPNTPDFLKNT CCCCCCCCCHHHHCH | 23.46 | 27214570 |
| 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 PHO2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHO2_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 PHO2_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-146 AND THR-542, ANDMASS SPECTROMETRY. | |