| UniProt ID | RPAC1_YEAST | |
|---|---|---|
| UniProt AC | P07703 | |
| Protein Name | DNA-directed RNA polymerases I and III subunit RPAC1 {ECO:0000305} | |
| Gene Name | RPC40 {ECO:0000303|PubMed:3815519} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 335 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I (Pol I) and III (Pol III) which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPC40 is part of the polymerase core and may function as a clamp element that moves to open and close the cleft. [PubMed: 18160037] | |
| Protein Sequence | MSNIVGIEYNRVTNTTSTDFPGFSKDAENEWNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRRIMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVDPDMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPKGSTDPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPDILLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLLPQINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDARKDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTPEEIFFKSVRILKNKAEYLKNCPITQ | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSNIVGIEY ------CCCEEEEEE | 34.95 | 22814378 | |
| 2 | Phosphorylation | ------MSNIVGIEY ------CCCEEEEEE | 34.95 | 30377154 | |
| 9 | Phosphorylation | SNIVGIEYNRVTNTT CCEEEEEEEECCCCC | 13.32 | 28132839 | |
| 13 | Phosphorylation | GIEYNRVTNTTSTDF EEEEEECCCCCCCCC | 24.50 | 21126336 | |
| 15 | Phosphorylation | EYNRVTNTTSTDFPG EEEECCCCCCCCCCC | 16.86 | 28889911 | |
| 16 | Phosphorylation | YNRVTNTTSTDFPGF EEECCCCCCCCCCCC | 31.53 | 28889911 | |
| 17 | Phosphorylation | NRVTNTTSTDFPGFS EECCCCCCCCCCCCC | 24.76 | 28152593 | |
| 18 | Phosphorylation | RVTNTTSTDFPGFSK ECCCCCCCCCCCCCC | 39.30 | 27017623 | |
| 25 | Ubiquitination | TDFPGFSKDAENEWN CCCCCCCCCCCCCCC | 59.71 | 23749301 | |
| 25 | Acetylation | TDFPGFSKDAENEWN CCCCCCCCCCCCCCC | 59.71 | 24489116 | |
| 35 | Acetylation | ENEWNVEKFKKDFEV CCCCCHHHHHHHEEE | 59.19 | 24489116 | |
| 37 | Acetylation | EWNVEKFKKDFEVNI CCCHHHHHHHEEEEH | 63.60 | 24489116 | |
| 127 | Phosphorylation | LPDDEKFTDENTIVL CCCCCCCCCCCEEEE | 54.17 | 21126336 | |
| 148 | Ubiquitination | TRNPDAPKGSTDPKE CCCCCCCCCCCCHHH | 68.18 | 23749301 | |
| 148 | Acetylation | TRNPDAPKGSTDPKE CCCCCCCCCCCCHHH | 68.18 | 25381059 | |
| 154 | Acetylation | PKGSTDPKELYNNAH CCCCCCHHHHHHCCE | 64.26 | 24489116 | |
| 205 | Ubiquitination | PGQEISLKAHCILGI CCCEEEEEEEEEEEC | 29.33 | 17644757 | |
| 218 | Acetylation | GIGGDHAKFSPVSTA ECCCCCCCCCCCCHH | 42.85 | 24489116 | |
| 218 | Ubiquitination | GIGGDHAKFSPVSTA ECCCCCCCCCCCCHH | 42.85 | 17644757 | |
| 220 | Phosphorylation | GGDHAKFSPVSTASY CCCCCCCCCCCHHHH | 24.56 | 27017623 | |
| 240 | Ubiquitination | INILQPIKGESARRF CCEECCCCCHHHHHH | 64.41 | 17644757 | |
| 268 | Ubiquitination | GSDEAYVKDARKDTV CCCHHHHHHHHHCCC | 32.75 | 23749301 | |
| 272 | Ubiquitination | AYVKDARKDTVSREV HHHHHHHHCCCCHHH | 60.51 | 22817900 | |
| 288 | Acetylation | RYEEFADKVKLGRVR CHHHHHHHCEECCEE | 37.53 | 24489116 | |
| 290 | Acetylation | EEFADKVKLGRVRNH HHHHHHCEECCEECC | 51.47 | 24489116 | |
| 329 | Ubiquitination | KNKAEYLKNCPITQ- HCHHHHHHCCCCCC- | 56.45 | 23749301 |
| 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 RPAC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPAC1_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 RPAC1_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 THR-15 AND THR-16, AND MASSSPECTROMETRY. | |
