UniProt ID | RPA43_YEAST | |
---|---|---|
UniProt AC | P46669 | |
Protein Name | DNA-directed RNA polymerase I subunit RPA43 | |
Gene Name | RPA43 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 326 | |
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. Through its association with RRN3 is involved in recruitment of Pol I to rDNA promoters. In vitro, the A13-A43 subcomplex binds single-stranded RNA.. | |
Protein Sequence | MSQVKRANENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMYLENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDADPLSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHNDVEEDADVINTDENNGNNNNEDNKDSNGGSNSLGKFSFGNRSLGHWVDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLISDADEEGNGYNSSRSQAESLPIVSNKKIVFDDEVSIENKESHKELDLPEVKEDNGSEIVYEENTSESNDGESSDSD | |
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 |
---|---|---|---|---|---|
25 | Phosphorylation | KKHKKQVTNPIDEKN HHHHHHCCCCCCCCC | 32.55 | 28889911 | |
31 | Acetylation | VTNPIDEKNGTSNCI CCCCCCCCCCCCCEE | 57.86 | 24489116 | |
72 | Acetylation | HLNPLVMKYNNKVGG HHCHHHHHCCCCCCE | 37.03 | 24489116 | |
88 | Ubiquitination | VLGYEGLKILDADPL EEEECCEEEEECCCC | 52.67 | 24961812 | |
96 | Phosphorylation | ILDADPLSKEDTSEK EEECCCCCCCCCCCC | 39.11 | 21440633 | |
97 | Acetylation | LDADPLSKEDTSEKL EECCCCCCCCCCCCC | 68.26 | 24489116 | |
103 | Acetylation | SKEDTSEKLIKITPD CCCCCCCCCEECCCC | 56.11 | 24489116 | |
203 | Phosphorylation | DSNGGSNSLGKFSFG CCCCCCCCCCEEECC | 39.95 | 28889911 | |
206 | Acetylation | GGSNSLGKFSFGNRS CCCCCCCEEECCCCC | 43.03 | 24489116 | |
208 | Phosphorylation | SNSLGKFSFGNRSLG CCCCCEEECCCCCCC | 35.41 | 28889911 | |
220 | Phosphorylation | SLGHWVDSNGEPIDG CCCCEECCCCCCCCC | 36.80 | 28889911 | |
228 | Acetylation | NGEPIDGKLRFTVRN CCCCCCCEEEEEEEE | 32.51 | 24489116 | |
244 | Phosphorylation | HTTGRVVSVDGTLIS CCCCCEEEEECEEEC | 16.19 | 22369663 | |
248 | Phosphorylation | RVVSVDGTLISDADE CEEEEECEEECCCCC | 19.22 | 22369663 | |
251 | Phosphorylation | SVDGTLISDADEEGN EEECEEECCCCCCCC | 29.83 | 22369663 | |
260 | Phosphorylation | ADEEGNGYNSSRSQA CCCCCCCCCCCHHHH | 18.83 | 22369663 | |
262 | Phosphorylation | EEGNGYNSSRSQAES CCCCCCCCCHHHHHC | 20.74 | 22369663 | |
263 | Phosphorylation | EGNGYNSSRSQAESL CCCCCCCCHHHHHCC | 32.11 | 22369663 | |
265 | Phosphorylation | NGYNSSRSQAESLPI CCCCCCHHHHHCCCE | 35.37 | 22369663 | |
269 | Phosphorylation | SSRSQAESLPIVSNK CCHHHHHCCCEECCC | 42.32 | 22369663 | |
274 | Phosphorylation | AESLPIVSNKKIVFD HHCCCEECCCEEEEC | 43.59 | 22369663 | |
276 | Acetylation | SLPIVSNKKIVFDDE CCCEECCCEEEECCC | 36.05 | 25381059 | |
285 | Phosphorylation | IVFDDEVSIENKESH EEECCCCCCCCHHHC | 23.33 | 22369663 | |
293 | Acetylation | IENKESHKELDLPEV CCCHHHCCCCCCCCC | 70.06 | 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 RPA43_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPA43_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 RPA43_YEAST !! |
Kegg Drug | ||||||
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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-285, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND MASSSPECTROMETRY. | |
"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-244; SER-251; TYR-260;SER-262; SER-263; SER-265; SER-269 AND SER-285, AND MASS SPECTROMETRY. |