| UniProt ID | RPA49_YEAST | |
|---|---|---|
| UniProt AC | Q01080 | |
| Protein Name | DNA-directed RNA polymerase I subunit RPA49 | |
| Gene Name | RPA49 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 415 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. The heterodimer formed by RPA34 and RPA49 stimulates transcript elongation by Pol I. Subunit RPA49 can bind both single-stranded and double-stranded DNA.. | |
| Protein Sequence | MSVKRSVSEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSEKDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKSIQLYKAPVLVSKVVSKSSKNLRGPKIKSKSDTRPSALRNALGEAFGTKKAKKAIADLERNRIDSDKLTDSAIDIVDSVRTASKDLPTRAQLDEITSNDRPTPLANIDATDVEQIYPIESIIPKKELQFIRVSSILKEADKEKKLELFPYQNNSKYVAKKLDSLTQPSQMTKLQLLYYLSLLLGVYENRRVNNKTKLLERLNSPPEILVDGILSRFTVIKPGQFGRSKDRSYFIDPQNEDKILCYILAIIMHLDNFIVEITPLAHELNLKPSKVVSLFRVLGAIVKGATVAQAEAFGIPKSTAASYKIATMKVPFKLPEMTRRGRGPRR | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MSVKRSVSEIEIE --CCCCCCCCEEEEE | 25.03 | 25521595 | |
| 8 | Phosphorylation | MSVKRSVSEIEIESV CCCCCCCCEEEEEEC | 33.82 | 22369663 | |
| 14 | Phosphorylation | VSEIEIESVQDQPSV CCEEEEEECCCCCCE | 30.64 | 22369663 | |
| 20 | Phosphorylation | ESVQDQPSVAVGSFF EECCCCCCEEECCCC | 19.64 | 29688323 | |
| 25 | Phosphorylation | QPSVAVGSFFKGFRA CCCEEECCCCCCCCC | 22.40 | 29688323 | |
| 34 | Phosphorylation | FKGFRAPSDTTFDLY CCCCCCCCCCCCCCC | 46.75 | 19823750 | |
| 36 | Phosphorylation | GFRAPSDTTFDLYKK CCCCCCCCCCCCCCC | 33.43 | 29734811 | |
| 37 | Phosphorylation | FRAPSDTTFDLYKKK CCCCCCCCCCCCCCC | 21.83 | 19823750 | |
| 42 | Succinylation | DTTFDLYKKKKSEKD CCCCCCCCCCCCCCC | 66.47 | 23954790 | |
| 42 | Acetylation | DTTFDLYKKKKSEKD CCCCCCCCCCCCCCC | 66.47 | 24489116 | |
| 92 | Acetylation | KKSIQLYKAPVLVSK CCEEEEEECCCHHHH | 55.60 | 24489116 | |
| 99 | Acetylation | KAPVLVSKVVSKSSK ECCCHHHHHHCCCCC | 38.89 | 24489116 | |
| 122 | Phosphorylation | SKSDTRPSALRNALG CCCCCCHHHHHHHHH | 36.32 | 21440633 | |
| 135 | Acetylation | LGEAFGTKKAKKAIA HHHHHCCHHHHHHHH | 51.63 | 25381059 | |
| 151 | Phosphorylation | LERNRIDSDKLTDSA HHHCCCCHHHCCHHH | 33.98 | 22369663 | |
| 153 | Acetylation | RNRIDSDKLTDSAID HCCCCHHHCCHHHHH | 58.18 | 24489116 | |
| 155 | Phosphorylation | RIDSDKLTDSAIDIV CCCHHHCCHHHHHHH | 33.38 | 22369663 | |
| 157 | Phosphorylation | DSDKLTDSAIDIVDS CHHHCCHHHHHHHHH | 23.14 | 22369663 | |
| 164 | Phosphorylation | SAIDIVDSVRTASKD HHHHHHHHHHHHCCC | 11.56 | 22369663 | |
| 167 | Phosphorylation | DIVDSVRTASKDLPT HHHHHHHHHCCCCCC | 32.88 | 28889911 | |
| 169 | Phosphorylation | VDSVRTASKDLPTRA HHHHHHHCCCCCCHH | 26.53 | 23749301 | |
| 170 | Acetylation | DSVRTASKDLPTRAQ HHHHHHCCCCCCHHH | 61.90 | 24489116 | |
| 220 | Phosphorylation | LQFIRVSSILKEADK HHEEEHHHHHHHHCH | 29.14 | 21440633 | |
| 241 | Acetylation | FPYQNNSKYVAKKLD ECCCCCHHHHHHHHH | 45.96 | 24489116 |
| 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 RPA49_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPA49_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 RPA49_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-8 AND SER-34, AND MASSSPECTROMETRY. | |
