| UniProt ID | RPAC2_YEAST | |
|---|---|---|
| UniProt AC | P28000 | |
| Protein Name | DNA-directed RNA polymerases I and III subunit RPAC2 | |
| Gene Name | RPC19 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 142 | |
| 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 core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.. | |
| Protein Sequence | MTEDIEQKKTATEVTPQEPKHIQEEEEQDVDMTGDEEQEEEPDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIMKNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGLKDLMDLCDVVESKFTEKIKSM | |
| 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 |
|---|---|---|---|---|---|
| 8 | Ubiquitination | MTEDIEQKKTATEVT CCCHHHHHCCCCCCC | 39.02 | 17644757 | |
| 9 | Ubiquitination | TEDIEQKKTATEVTP CCHHHHHCCCCCCCC | 42.98 | 23749301 | |
| 10 | Phosphorylation | EDIEQKKTATEVTPQ CHHHHHCCCCCCCCC | 45.94 | 22369663 | |
| 12 | Phosphorylation | IEQKKTATEVTPQEP HHHHCCCCCCCCCCC | 35.90 | 28132839 | |
| 15 | Phosphorylation | KKTATEVTPQEPKHI HCCCCCCCCCCCCCC | 17.02 | 22369663 | |
| 20 | Ubiquitination | EVTPQEPKHIQEEEE CCCCCCCCCCCHHHH | 53.22 | 17644757 | |
| 33 | Phosphorylation | EEQDVDMTGDEEQEE HHCCCCCCCCHHHHC | 36.70 | 22369663 | |
| 46 | Acetylation | EEEPDREKIKLLTQA HCCCCHHHHHHHHHC | 46.14 | 24489116 | |
| 51 | Phosphorylation | REKIKLLTQATSEDG HHHHHHHHHCCCCCC | 26.96 | 28889911 | |
| 54 | Phosphorylation | IKLLTQATSEDGTSA HHHHHHCCCCCCCCC | 23.88 | 28889911 | |
| 55 | Phosphorylation | KLLTQATSEDGTSAS HHHHHCCCCCCCCCE | 36.38 | 28889911 | |
| 82 | Ubiquitination | ALRYVIMKNPDVEFC HHHHHHHCCCCCCCC | 54.96 | 23749301 | |
| 119 | Ubiquitination | TAVDALQKGLKDLMD HHHHHHHHHHHHHHH | 68.04 | 23749301 | |
| 134 | Ubiquitination | LCDVVESKFTEKIKS HHHHHHHHHHHHHHC | 42.68 | 22106047 |
| 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 RPAC2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPAC2_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 RPAC2_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 THR-33, 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 THR-15 AND THR-33, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, AND MASSSPECTROMETRY. | |
