| UniProt ID | FUS3_YEAST | |
|---|---|---|
| UniProt AC | P16892 | |
| Protein Name | Mitogen-activated protein kinase FUS3 | |
| Gene Name | FUS3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 353 | |
| Subcellular Localization | Nucleus . Cytoplasm . Periplasm . FUS3 shuttles rapidly between the cytoplasm and the nucleus independent of pheromone treatment or FUS3 phosphorylation level. Activated FUS3 translocates rapidly to the nucleus. | |
| Protein Description | Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.. | |
| Protein Sequence | MPKRIVYNISSDFQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREIKILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMTEYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYLQTYHDPNDEPEGEPIPPSFFEFDHYKEALTTKDLKKLIWNEIFS | |
| 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 |
|---|---|---|---|---|---|
| 16 | Ubiquitination | ISSDFQLKSLLGEGA CCCCHHHHHHHCCCC | 28.42 | 17644757 | |
| 33 | Ubiquitination | VVCSATHKPTGEIVA EEEEECCCCCCEEEE | 39.66 | 17644757 | |
| 42 | Ubiquitination | TGEIVAIKKIEPFDK CCEEEEEEEECCCCC | 37.65 | 17644757 | |
| 43 | Ubiquitination | GEIVAIKKIEPFDKP CEEEEEEEECCCCCC | 46.30 | 17644757 | |
| 49 | Acetylation | KKIEPFDKPLFALRT EEECCCCCCHHHHHH | 43.96 | 24489116 | |
| 49 | Ubiquitination | KKIEPFDKPLFALRT EEECCCCCCHHHHHH | 43.96 | 24961812 | |
| 126 | Ubiquitination | YQTLRAVKVLHGSNV HHHHHHHHHHCCCCC | 37.79 | 17644757 | |
| 139 | Ubiquitination | NVIHRDLKPSNLLIN CCCCCCCCHHHEEEC | 51.17 | 17644757 | |
| 147 | Phosphorylation | PSNLLINSNCDLKVC HHHEEECCCCCCEEC | 31.66 | 28889911 | |
| 152 | Ubiquitination | INSNCDLKVCDFGLA ECCCCCCEECCHHHH | 27.80 | 17644757 | |
| 177 | Phosphorylation | SEPTGQQSGMTEYVA CCCCCCCCCCCHHHH | 23.73 | 19684113 | |
| 179 | Oxidation | PTGQQSGMTEYVATR CCCCCCCCCHHHHCC | 2.89 | 15665377 | |
| 180 | Phosphorylation | TGQQSGMTEYVATRW CCCCCCCCHHHHCCH | 27.91 | 11583629 | |
| 182 | Phosphorylation | QQSGMTEYVATRWYR CCCCCCHHHHCCHHC | 6.04 | 17330950 | |
| 199 | Acetylation | EVMLTSAKYSRAMDV HHHHCCCCCHHHHHH | 43.45 | 24489116 | |
| 273 | Ubiquitination | YPAAPLEKMFPRVNP CCCCCHHHHCCCCCH | 54.23 | 24961812 | |
| 281 | Ubiquitination | MFPRVNPKGIDLLQR HCCCCCHHHHHHHHH | 64.39 | 24961812 | |
| 345 | Ubiquitination | LTTKDLKKLIWNEIF CCHHHHHHHHHHHHC | 53.13 | 22106047 |
| 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 FUS3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 180 | T | Phosphorylation |
| 1628831 |
* 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 FUS3_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 THR-180 AND TYR-182, ANDMASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, ANDMASS SPECTROMETRY. | |
