| UniProt ID | ESC2_YEAST | |
|---|---|---|
| UniProt AC | Q06340 | |
| Protein Name | Protein ESC2 | |
| Gene Name | ESC2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 456 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | May be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR and telomere silencing via the recruitment or stabilizing of the SIR (silent information regulators) complex.. | |
| Protein Sequence | MTGDSRSISEPSINLDPDNTSFSDENSDDFFMDNSYDIDEIDHSDESNRQSVIVDSKVTVPPSKHSTLTLSDSEDSDAKEQHQSLSRSSSKNVNIEDITEPKPDKPSGRTRGRSVMKESVVEINSSESDLDEDKNFPRSRSRSRSSIRSISPAGKYKRQKSSLLYTYDENDDFFKELAKEAKKSTTISKESTPDQRKRVYNIKFLSKLEGTINKAVQVKVLGKYEFSKILPAALDGLMKSYKIPKVMKDIYKVENVTLYWNNAKLLTFMTCNSLHIPQDFENEVSDIDVTIVSKEYEKNFEATLESKLKEEEAALLIKERQEMERKLEKKRNEQEESEYREFESELKNVEETQEIKENDTVMNTKLLQEGGSLSGNSSSMEEVMRIALMGQDNKKIYVHVRRSTPFSKIAEYYRIQKQLPQKTRVKLLFDHDELDMNECIADQDMEDEDMVDVIID | |
| 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 | TVPPSKHSTLTLSDS ECCCCCCCEEEECCC | 28.93 | 22369663 | |
| 67 | Phosphorylation | VPPSKHSTLTLSDSE CCCCCCCEEEECCCC | 24.39 | 22369663 | |
| 69 | Phosphorylation | PSKHSTLTLSDSEDS CCCCCEEEECCCCCC | 25.06 | 22369663 | |
| 71 | Phosphorylation | KHSTLTLSDSEDSDA CCCEEEECCCCCCCH | 33.58 | 22369663 | |
| 73 | Phosphorylation | STLTLSDSEDSDAKE CEEEECCCCCCCHHH | 39.67 | 22369663 | |
| 76 | Phosphorylation | TLSDSEDSDAKEQHQ EECCCCCCCHHHHHH | 35.10 | 22369663 | |
| 84 | Phosphorylation | DAKEQHQSLSRSSSK CHHHHHHHHHHHHCC | 26.62 | 19823750 | |
| 86 | Phosphorylation | KEQHQSLSRSSSKNV HHHHHHHHHHHCCCC | 35.05 | 19823750 | |
| 88 | Phosphorylation | QHQSLSRSSSKNVNI HHHHHHHHHCCCCCH | 35.27 | 19823750 | |
| 89 | Phosphorylation | HQSLSRSSSKNVNIE HHHHHHHHCCCCCHH | 44.19 | 19823750 | |
| 90 | Phosphorylation | QSLSRSSSKNVNIED HHHHHHHCCCCCHHH | 29.51 | 19823750 | |
| 105 | Acetylation | ITEPKPDKPSGRTRG CCCCCCCCCCCCCCC | 50.00 | 24489116 | |
| 125 | Phosphorylation | ESVVEINSSESDLDE HCEEEECCCCCCCCC | 40.94 | 22369663 | |
| 126 | Phosphorylation | SVVEINSSESDLDED CEEEECCCCCCCCCC | 36.31 | 22369663 | |
| 128 | Phosphorylation | VEINSSESDLDEDKN EEECCCCCCCCCCCC | 45.48 | 22369663 | |
| 145 | Phosphorylation | RSRSRSRSSIRSISP CHHHCCHHHHHCCCC | 31.22 | 22369663 | |
| 146 | Phosphorylation | SRSRSRSSIRSISPA HHHCCHHHHHCCCCC | 22.40 | 22369663 | |
| 149 | Phosphorylation | RSRSSIRSISPAGKY CCHHHHHCCCCCCCC | 26.25 | 22369663 | |
| 151 | Phosphorylation | RSSIRSISPAGKYKR HHHHHCCCCCCCCCC | 15.22 | 22369663 | |
| 161 | Phosphorylation | GKYKRQKSSLLYTYD CCCCCCCCCEEEEEC | 20.20 | 30377154 | |
| 165 | Phosphorylation | RQKSSLLYTYDENDD CCCCCEEEEECCCCH | 14.46 | 30377154 | |
| 191 | Phosphorylation | STTISKESTPDQRKR HCCCCCCCCHHHHHH | 49.31 | 23749301 | |
| 192 | Phosphorylation | TTISKESTPDQRKRV CCCCCCCCHHHHHHH | 31.79 | 23749301 | |
| 240 | Phosphorylation | ALDGLMKSYKIPKVM HHHHHHHHCCCCHHH | 20.07 | 27017623 | |
| 241 | Phosphorylation | LDGLMKSYKIPKVMK HHHHHHHCCCCHHHH | 13.86 | 27017623 | |
| 372 | Phosphorylation | KLLQEGGSLSGNSSS HHHHCCCCCCCCCCC | 30.16 | 27017623 | |
| 378 | Phosphorylation | GSLSGNSSSMEEVMR CCCCCCCCCHHHHHH | 37.39 | 23749301 | |
| 379 | Phosphorylation | SLSGNSSSMEEVMRI CCCCCCCCHHHHHHH | 29.99 | 28889911 |
| 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 ESC2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ESC2_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 ESC2_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-379, AND MASSSPECTROMETRY. | |
| "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-149 AND SER-151, ANDMASS SPECTROMETRY. | |
