| UniProt ID | RT103_YEAST | |
|---|---|---|
| UniProt AC | Q05543 | |
| Protein Name | Regulator of Ty1 transposition protein 103 | |
| Gene Name | RTT103 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 409 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.. | |
| Protein Sequence | MPFSSEQFTTKLNTLEDSQESISSASKWLLLQYRDAPKVAEMWKEYMLRPSVNTRRKLLGLYLMNHVVQQAKGQKIIQFQDSFGKVAAEVLGRINQEFPRDLKKKLSRVVNILKERNIFSKQVVNDIERSLKTESSPVEALVLPQKLKDFAKDYEKLVKMHHNVCAMKMRFDKSSDELDPSSSVYEENFKTISKIGNMAKDIINESILKRESGIHKLQSTLDDEKRHLDEEQNMLSEIEFVLSAKDPSRLNKNVDEDNIIPTYEVGDGDDDDDDGDNDDDDDDDDDDKNYDDRSNDSNYGVTNISTTDKKNEVVEKTDSEHKNSTHNPSDNQFGMKRTHDMIGHDDANDIPEKKVHLDSKTSEDGTFNSEDGHYELDIEGHVGAQTDEGVENSGGVSSSIQDLLSKLAN | |
| 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 |
|---|---|---|---|---|---|
| 82 | Phosphorylation | KIIQFQDSFGKVAAE EEEEEECCHHHHHHH | 25.72 | 30377154 | |
| 133 | Phosphorylation | DIERSLKTESSPVEA HHHHHHCCCCCCHHH | 46.52 | 21126336 | |
| 135 | Phosphorylation | ERSLKTESSPVEALV HHHHCCCCCCHHHHH | 45.21 | 21551504 | |
| 136 | Phosphorylation | RSLKTESSPVEALVL HHHCCCCCCHHHHHC | 27.08 | 27214570 | |
| 146 | Acetylation | EALVLPQKLKDFAKD HHHHCCHHHHHHHHH | 56.41 | 24489116 | |
| 159 | Acetylation | KDYEKLVKMHHNVCA HHHHHHHHHHHCHHH | 42.84 | 25381059 | |
| 168 | Acetylation | HHNVCAMKMRFDKSS HHCHHHHHCCCCCCC | 14.38 | 25381059 | |
| 174 | Phosphorylation | MKMRFDKSSDELDPS HHCCCCCCCCCCCCC | 44.88 | 28889911 | |
| 182 | Phosphorylation | SDELDPSSSVYEENF CCCCCCCCCHHHHHH | 29.25 | 28889911 | |
| 194 | Acetylation | ENFKTISKIGNMAKD HHHHHHHHHHHHHHH | 51.27 | 22865919 | |
| 209 | Acetylation | IINESILKRESGIHK HHCHHHHHHHHCHHH | 53.07 | 24489116 | |
| 216 | Acetylation | KRESGIHKLQSTLDD HHHHCHHHHHHCHHH | 46.42 | 24489116 | |
| 219 | Phosphorylation | SGIHKLQSTLDDEKR HCHHHHHHCHHHHHH | 41.18 | 30377154 | |
| 236 | Phosphorylation | DEEQNMLSEIEFVLS HHHHHHHHHHHHHHC | 26.26 | 24961812 | |
| 290 | Phosphorylation | DDDDDKNYDDRSNDS CCCCCCCCCCCCCCC | 25.59 | 22369663 | |
| 294 | Phosphorylation | DKNYDDRSNDSNYGV CCCCCCCCCCCCCCC | 52.57 | 22369663 | |
| 297 | Phosphorylation | YDDRSNDSNYGVTNI CCCCCCCCCCCCCCC | 35.88 | 22369663 | |
| 299 | Phosphorylation | DRSNDSNYGVTNIST CCCCCCCCCCCCCCC | 19.54 | 22369663 | |
| 302 | Phosphorylation | NDSNYGVTNISTTDK CCCCCCCCCCCCCCC | 23.59 | 22369663 | |
| 305 | Phosphorylation | NYGVTNISTTDKKNE CCCCCCCCCCCCCCC | 27.59 | 19795423 | |
| 306 | Phosphorylation | YGVTNISTTDKKNEV CCCCCCCCCCCCCCE | 34.91 | 19795423 | |
| 307 | Phosphorylation | GVTNISTTDKKNEVV CCCCCCCCCCCCCEE | 38.74 | 19795423 | |
| 325 | Phosphorylation | DSEHKNSTHNPSDNQ CCCCCCCCCCCCCCC | 34.76 | 30377154 | |
| 329 | Phosphorylation | KNSTHNPSDNQFGMK CCCCCCCCCCCCCCC | 55.28 | 21551504 | |
| 336 | Acetylation | SDNQFGMKRTHDMIG CCCCCCCCHHHHCCC | 55.30 | 22865919 | |
| 353 | Acetylation | DANDIPEKKVHLDSK CHHHCCCCCEECCCC | 55.53 | 25381059 |
| 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 RT103_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RT103_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 RT103_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-136; SER-174 ANDSER-182, AND MASS SPECTROMETRY. | |
