| UniProt ID | ESS1_YEAST | |
|---|---|---|
| UniProt AC | P22696 | |
| Protein Name | Peptidyl-prolyl cis-trans isomerase ESS1 | |
| Gene Name | ESS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 170 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Essential PPIase specific for phosphoserine and phosphothreonine N-terminal to the proline residue. Required for efficient pre-mRNA 3'-end processing and transcription termination, probably by inducing conformational changes by proline-directed isomerization in the C-terminal domain (CTD) of RPB1, thereby altering cofactor binding with the RNA polymerase II transcription complex. Also targets the SIN3-RPD3 histone deacetylase complex (HDAC).. | |
| Protein Sequence | MPSDVASRTGLPTPWTVRYSKSKKREYFFNPETKHSQWEEPEGTNKDQLHKHLRDHPVRVRCLHILIKHKDSRRPASHRSENITISKQDATDELKTLITRLDDDSKTNSFEALAKERSDCSSYKRGGDLGWFGRGEMQPSFEDAAFQLKVGEVSDIVESGSGVHVIKRVG | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MPSDVASRTG -----CCCCHHHHCC | 43.34 | 30377154 | |
| 13 | Phosphorylation | ASRTGLPTPWTVRYS HHHCCCCCCCEEEEC | 36.18 | 27017623 | |
| 16 | Phosphorylation | TGLPTPWTVRYSKSK CCCCCCCEEEECCCC | 9.05 | 27017623 | |
| 46 | Acetylation | EEPEGTNKDQLHKHL CCCCCCCHHHHHHHH | 46.84 | 22865919 | |
| 87 | Acetylation | SENITISKQDATDEL CCCEEEEHHHCCHHH | 48.63 | 24489116 | |
| 95 | Acetylation | QDATDELKTLITRLD HHCCHHHHHHHHHCC | 38.96 | 24489116 | |
| 106 | Acetylation | TRLDDDSKTNSFEAL HHCCCCCCCCHHHHH | 59.73 | 24489116 | |
| 106 | Ubiquitination | TRLDDDSKTNSFEAL HHCCCCCCCCHHHHH | 59.73 | 23749301 | |
| 107 | Phosphorylation | RLDDDSKTNSFEALA HCCCCCCCCHHHHHH | 39.79 | 27214570 | |
| 109 | Phosphorylation | DDDSKTNSFEALAKE CCCCCCCHHHHHHHH | 29.69 | 25752575 | |
| 115 | Acetylation | NSFEALAKERSDCSS CHHHHHHHHHCCCCC | 55.28 | 24489116 | |
| 124 | Acetylation | RSDCSSYKRGGDLGW HCCCCCCCCCCCCCC | 46.65 | 25381059 | |
| 140 | Phosphorylation | GRGEMQPSFEDAAFQ CCCCCCCCHHHHHHE | 25.11 | 25752575 | |
| 154 | Phosphorylation | QLKVGEVSDIVESGS EEECEEHHHHHHCCC | 19.81 | 30377154 | |
| 159 | Phosphorylation | EVSDIVESGSGVHVI EHHHHHHCCCCEEEE | 27.62 | 19779198 | |
| 161 | Phosphorylation | SDIVESGSGVHVIKR HHHHHCCCCEEEEEE | 47.09 | 25752575 |
| 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 ESS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ESS1_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 ESS1_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-109; SER-140 ANDSER-161, AND MASS SPECTROMETRY. | |
