| UniProt ID | PHO4_YEAST | |
|---|---|---|
| UniProt AC | P07270 | |
| Protein Name | Phosphate system positive regulatory protein PHO4 | |
| Gene Name | PHO4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 312 | |
| Subcellular Localization | Cytoplasm . Nucleus . Predominantly cytoplasmic under high-phosphate conditions and localized to the nucleus upon phosphate starvation. | |
| Protein Description | Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions.. | |
| Protein Sequence | MGRTTSEGIHGFVDDLEPKSSILDKVGDFITVNTKRHDGREDFNEQNDELNSQENHNSSENGNENENEQDSLALDDLDRAFELVEGMDMDWMMPSHAHHSPATTATIKPRLLYSPLIHTQSAVPVTISPNLVATATSTTSANKVTKNKSNSSPYLNKRRGKPGPDSATSLFELPDSVIPTPKPKPKPKQYPKVILPSNSTRRVSPVTAKTSSSAEGVVVASESPVIAPHGSSHSRSLSKRRSSGALVDDDKRESHKHAEQARRNRLAVALHELASLIPAEWKQQNVSAAPSKATTVEAACRYIRHLQQNVST | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MGRTTSEGIHG ----CCCCCCCCCCC | 29.01 | 19823750 | |
| 5 | Phosphorylation | ---MGRTTSEGIHGF ---CCCCCCCCCCCC | 24.34 | 19823750 | |
| 6 | Phosphorylation | --MGRTTSEGIHGFV --CCCCCCCCCCCCC | 32.96 | 19823750 | |
| 52 | Phosphorylation | EQNDELNSQENHNSS HHHHHHHHHCCCCCC | 52.04 | 19779198 | |
| 58 | Phosphorylation | NSQENHNSSENGNEN HHHCCCCCCCCCCCC | 31.32 | 19779198 | |
| 100 | Phosphorylation | MPSHAHHSPATTATI CCCCCCCCCCCCCCC | 13.33 | 9853758 | |
| 113 | Phosphorylation | TIKPRLLYSPLIHTQ CCCCHHEECCCEECC | 16.91 | 20377248 | |
| 114 | Phosphorylation | IKPRLLYSPLIHTQS CCCHHEECCCEECCC | 17.13 | 22369663 | |
| 119 | Phosphorylation | LYSPLIHTQSAVPVT EECCCEECCCCCEEE | 19.75 | 22369663 | |
| 121 | Phosphorylation | SPLIHTQSAVPVTIS CCCEECCCCCEEEEC | 32.18 | 20377248 | |
| 126 | Phosphorylation | TQSAVPVTISPNLVA CCCCCEEEECCCEEE | 15.07 | 22369663 | |
| 128 | Phosphorylation | SAVPVTISPNLVATA CCCEEEECCCEEEEE | 9.81 | 22369663 | |
| 134 | Phosphorylation | ISPNLVATATSTTSA ECCCEEEEEEECCCC | 24.00 | 22369663 | |
| 136 | Phosphorylation | PNLVATATSTTSANK CCEEEEEEECCCCCC | 23.42 | 22369663 | |
| 137 | Phosphorylation | NLVATATSTTSANKV CEEEEEEECCCCCCC | 27.50 | 23749301 | |
| 138 | Phosphorylation | LVATATSTTSANKVT EEEEEEECCCCCCCC | 22.03 | 22369663 | |
| 139 | Phosphorylation | VATATSTTSANKVTK EEEEEECCCCCCCCC | 26.13 | 22369663 | |
| 140 | Phosphorylation | ATATSTTSANKVTKN EEEEECCCCCCCCCC | 29.90 | 22369663 | |
| 145 | Phosphorylation | TTSANKVTKNKSNSS CCCCCCCCCCCCCCC | 30.43 | 27017623 | |
| 149 | Phosphorylation | NKVTKNKSNSSPYLN CCCCCCCCCCCCCCC | 51.87 | 22890988 | |
| 151 | Phosphorylation | VTKNKSNSSPYLNKR CCCCCCCCCCCCCCC | 39.52 | 22890988 | |
| 152 | Phosphorylation | TKNKSNSSPYLNKRR CCCCCCCCCCCCCCC | 23.09 | 22369663 | |
| 154 | Phosphorylation | NKSNSSPYLNKRRGK CCCCCCCCCCCCCCC | 25.51 | 22890988 | |
| 157 | Ubiquitination | NSSPYLNKRRGKPGP CCCCCCCCCCCCCCC | 40.66 | 23749301 | |
| 166 | Phosphorylation | RGKPGPDSATSLFEL CCCCCCCCCCCCCCC | 36.26 | 22369663 | |
| 168 | Phosphorylation | KPGPDSATSLFELPD CCCCCCCCCCCCCCC | 29.89 | 22369663 | |
| 169 | Phosphorylation | PGPDSATSLFELPDS CCCCCCCCCCCCCCC | 30.67 | 22369663 | |
| 197 | Phosphorylation | YPKVILPSNSTRRVS CCEEEECCCCCCCCC | 39.71 | 19823750 | |
| 199 | Phosphorylation | KVILPSNSTRRVSPV EEEECCCCCCCCCCC | 27.85 | 21440633 | |
| 200 | Phosphorylation | VILPSNSTRRVSPVT EEECCCCCCCCCCCE | 27.09 | 19823750 | |
| 204 | Phosphorylation | SNSTRRVSPVTAKTS CCCCCCCCCCEEECC | 16.31 | 19823750 | |
| 207 | Phosphorylation | TRRVSPVTAKTSSSA CCCCCCCEEECCCCC | 26.31 | 28132839 | |
| 210 | Phosphorylation | VSPVTAKTSSSAEGV CCCCEEECCCCCCCE | 31.23 | 22890988 | |
| 211 | Phosphorylation | SPVTAKTSSSAEGVV CCCEEECCCCCCCEE | 22.91 | 22890988 | |
| 212 | Phosphorylation | PVTAKTSSSAEGVVV CCEEECCCCCCCEEE | 38.51 | 22890988 | |
| 213 | Phosphorylation | VTAKTSSSAEGVVVA CEEECCCCCCCEEEE | 30.06 | 22890988 | |
| 221 | Phosphorylation | AEGVVVASESPVIAP CCCEEEEECCCEECC | 27.31 | 22890988 | |
| 223 | Phosphorylation | GVVVASESPVIAPHG CEEEEECCCEECCCC | 23.21 | 17330950 | |
| 231 | Phosphorylation | PVIAPHGSSHSRSLS CEECCCCCCCCCCCC | 23.11 | 21440633 | |
| 232 | Phosphorylation | VIAPHGSSHSRSLSK EECCCCCCCCCCCCC | 30.03 | 22890988 | |
| 234 | Phosphorylation | APHGSSHSRSLSKRR CCCCCCCCCCCCCCC | 26.05 | 19823750 | |
| 236 | Phosphorylation | HGSSHSRSLSKRRSS CCCCCCCCCCCCCCC | 39.75 | 19823750 | |
| 238 | Phosphorylation | SSHSRSLSKRRSSGA CCCCCCCCCCCCCCC | 25.93 | 20377248 | |
| 242 | Phosphorylation | RSLSKRRSSGALVDD CCCCCCCCCCCCCCC | 36.84 | 25521595 | |
| 243 | Phosphorylation | SLSKRRSSGALVDDD CCCCCCCCCCCCCCC | 26.69 | 25521595 | |
| 292 | Ubiquitination | NVSAAPSKATTVEAA CCCCCCCCCHHHHHH | 49.01 | 23749301 | |
| 295 | Phosphorylation | AAPSKATTVEAACRY CCCCCCHHHHHHHHH | 22.62 | 27017623 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 100 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 114 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 128 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 152 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 223 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
* 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 PHO4_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-128; SER-152; SER-204;SER-242 AND SER-243, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-242 ANDSER-243, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-243, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASSSPECTROMETRY. | |
| "Roles of phosphorylation sites in regulating activity of thetranscription factor Pho4."; Komeili A., O'Shea E.K.; Science 284:977-980(1999). Cited for: PHOSPHORYLATION AT SER-100; SER-114; SER-128; SER-152 AND SER-223. | |
| "Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDKcomplex."; O'Neill E.M., Kaffman A., Jolly E.R., O'Shea E.K.; Science 271:209-212(1996). Cited for: PHOSPHORYLATION AT SER-100; SER-114; SER-128; SER-152 AND SER-223, ANDSUBCELLULAR LOCATION. | |
