| UniProt ID | RXT2_YEAST | |
|---|---|---|
| UniProt AC | P38255 | |
| Protein Name | Transcriptional regulatory protein RXT2 | |
| Gene Name | RXT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 430 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.. | |
| Protein Sequence | MTIRSSMKNNAELESKSVLANESNIISTFTRRIIKEKSGNYQVLKRSLDGKLIYPEATGISSNRGNKLLQRSEVVTRRDLNNSKPMIEQTVFYNGSEHRLLQTNIVTDSRRKRIKFTPDINVEPVLVGDENDIDGSEKEDENITDEYYGEEDDDDLSKLVNVKEILTPILSLGDIINHKTISRTFSSPILKNLALQIILMIEKEQMSVVRYSQFLEVFLGDHPEPIYESNLNLPSYNHNLTLPEDRGASDEDDINNKNNINEVNSNSLSTEAGHINNGMEEFGEEDPFFALPRLEQSNALLSLLPSSSGSASISTLTAAEQQQLNEEIESARQLSQIALQRNKEFIRNLQKIRKSVIKANRIRGRILNWSREYLGISDDDITIPVALRVVKRGLISATTNKTTNFEEEIENTMEDGVVDDNEPDEEANRA | |
| 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 |
|---|---|---|---|---|---|
| 8 | Acetylation | MTIRSSMKNNAELES CCCCHHCCCCHHHHC | 49.34 | 25381059 | |
| 16 | Acetylation | NNAELESKSVLANES CCHHHHCHHHHHCCH | 34.90 | 24489116 | |
| 45 | Acetylation | SGNYQVLKRSLDGKL CCCCEEEEECCCCCE | 40.87 | 22865919 | |
| 51 | Acetylation | LKRSLDGKLIYPEAT EEECCCCCEECCCCC | 31.23 | 24489116 | |
| 84 | Acetylation | RRDLNNSKPMIEQTV HHHCCCCCCCEEEEE | 40.50 | 24489116 | |
| 117 | Phosphorylation | RRKRIKFTPDINVEP CCCCCCCCCCCCCEE | 18.30 | 22890988 | |
| 136 | Phosphorylation | DENDIDGSEKEDENI CCCCCCCCCCCCCCC | 41.57 | 22890988 | |
| 144 | Phosphorylation | EKEDENITDEYYGEE CCCCCCCCCCCCCCC | 34.07 | 22369663 | |
| 147 | Phosphorylation | DENITDEYYGEEDDD CCCCCCCCCCCCCCC | 21.41 | 24961812 | |
| 167 | Phosphorylation | VNVKEILTPILSLGD CCHHHHHHHHHHHHH | 17.59 | 21440633 | |
| 171 | Phosphorylation | EILTPILSLGDIINH HHHHHHHHHHHHHCC | 30.90 | 22369663 | |
| 179 | Ubiquitination | LGDIINHKTISRTFS HHHHHCCCCCCCCCC | 42.96 | 24961812 | |
| 186 | Phosphorylation | KTISRTFSSPILKNL CCCCCCCCCHHHHHH | 34.29 | 30377154 | |
| 187 | Phosphorylation | TISRTFSSPILKNLA CCCCCCCCHHHHHHH | 16.27 | 30377154 | |
| 249 | Phosphorylation | LPEDRGASDEDDINN CCCCCCCCCHHHHCC | 44.34 | 22369663 | |
| 373 | Phosphorylation | ILNWSREYLGISDDD HHHHCHHHHCCCCCC | 14.76 | 30377154 | |
| 377 | Phosphorylation | SREYLGISDDDITIP CHHHHCCCCCCCHHH | 32.94 | 17330950 | |
| 396 | Phosphorylation | VVKRGLISATTNKTT HHHHCCEEEECCCCC | 25.30 | 21440633 | |
| 399 | Phosphorylation | RGLISATTNKTTNFE HCCEEEECCCCCCHH | 34.14 | 19779198 |
| 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 RXT2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RXT2_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 RXT2_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-249, AND MASSSPECTROMETRY. | |
