| UniProt ID | RPA34_YEAST | |
|---|---|---|
| UniProt AC | P47006 | |
| Protein Name | DNA-directed RNA polymerase I subunit RPA34 | |
| Gene Name | RPA34 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 233 | |
| 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.. | |
| Protein Sequence | MSKLSKDYVSDSDSDDEVISNEFSIPDGFKKCKHLKNFPLNGDNKKKAKQQQVWLIKFPSNVDISKLKSLPVDFESSTTMTIDKHDYKIMDDTDIESSLTQDNLSNMTLLVPSESKESLKIASTAKDNAPLQFDKVFSVSETAKIPAIDYSKVRVPRKDVPKVEGLKLEHFATGYDAEDFHVAEEVKENKKEPKKRSHHDDEEESSEKKKKKKEKREKREKKDKKDKKKKHRD | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MSKLSKDYVSDS ---CCCCCCCCCCCC | 27.50 | 19779198 | |
| 8 | Phosphorylation | MSKLSKDYVSDSDSD CCCCCCCCCCCCCCC | 12.94 | 19795423 | |
| 10 | Phosphorylation | KLSKDYVSDSDSDDE CCCCCCCCCCCCCCC | 25.76 | 17330950 | |
| 12 | Phosphorylation | SKDYVSDSDSDDEVI CCCCCCCCCCCCCHH | 31.35 | 17330950 | |
| 14 | Phosphorylation | DYVSDSDSDDEVISN CCCCCCCCCCCHHHC | 51.41 | 17330950 | |
| 20 | Phosphorylation | DSDDEVISNEFSIPD CCCCCHHHCCCCCCC | 35.17 | 19779198 | |
| 24 | Phosphorylation | EVISNEFSIPDGFKK CHHHCCCCCCCCHHH | 27.34 | 19779198 | |
| 36 | Acetylation | FKKCKHLKNFPLNGD HHHCCCCCCCCCCCC | 57.15 | 24489116 | |
| 60 | Phosphorylation | VWLIKFPSNVDISKL EEEEECCCCCCHHHC | 53.25 | 25521595 | |
| 65 | Phosphorylation | FPSNVDISKLKSLPV CCCCCCHHHCCCCCC | 27.72 | 25521595 | |
| 93 | Phosphorylation | DYKIMDDTDIESSLT CEEECCCCCCCCCCC | 34.31 | 21440633 | |
| 97 | Phosphorylation | MDDTDIESSLTQDNL CCCCCCCCCCCCCCC | 30.86 | 21551504 | |
| 98 | Phosphorylation | DDTDIESSLTQDNLS CCCCCCCCCCCCCCC | 23.73 | 21551504 | |
| 100 | Phosphorylation | TDIESSLTQDNLSNM CCCCCCCCCCCCCCC | 35.51 | 21440633 | |
| 113 | Phosphorylation | NMTLLVPSESKESLK CCEEEEECCCHHHHH | 47.20 | 23749301 | |
| 115 | Phosphorylation | TLLVPSESKESLKIA EEEEECCCHHHHHEE | 46.17 | 28889911 | |
| 118 | Phosphorylation | VPSESKESLKIASTA EECCCHHHHHEECCC | 38.40 | 23749301 | |
| 123 | Phosphorylation | KESLKIASTAKDNAP HHHHHEECCCCCCCC | 32.16 | 19823750 | |
| 124 | Phosphorylation | ESLKIASTAKDNAPL HHHHEECCCCCCCCC | 28.80 | 19823750 | |
| 126 | Succinylation | LKIASTAKDNAPLQF HHEECCCCCCCCCCC | 52.16 | 23954790 | |
| 126 | Acetylation | LKIASTAKDNAPLQF HHEECCCCCCCCCCC | 52.16 | 24489116 | |
| 138 | Phosphorylation | LQFDKVFSVSETAKI CCCCEEEECCCCCCC | 27.93 | 28889911 | |
| 150 | Phosphorylation | AKIPAIDYSKVRVPR CCCCCCCCCCCCCCC | 12.32 | 28889911 | |
| 151 | Phosphorylation | KIPAIDYSKVRVPRK CCCCCCCCCCCCCCC | 22.41 | 28889911 | |
| 152 | Acetylation | IPAIDYSKVRVPRKD CCCCCCCCCCCCCCC | 28.03 | 24489116 | |
| 162 | Acetylation | VPRKDVPKVEGLKLE CCCCCCCCCCCEECE | 53.41 | 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 RPA34_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPA34_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 RPA34_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14,AND MASS SPECTROMETRY. | |
| "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-14; SER-60; SER-115 ANDSER-118, AND MASS SPECTROMETRY. | |
