| UniProt ID | RPA14_YEAST | |
|---|---|---|
| UniProt AC | P50106 | |
| Protein Name | DNA-directed RNA polymerase I subunit RPA14 | |
| Gene Name | RPA14 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 137 | |
| 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. RPA14 seems to play a role in the stability of subunits RPO26 and RPA43. In vitro, the RPA14-RPA43 subcomplex binds single-stranded RNA.. | |
| Protein Sequence | MMKGSRRTGNNTATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENIIDSTTMNTISGNAADADAAAVANTSLNIDTNLSSSISQLKRIQRDFKGLPPAQDFSAAPIQVSTTEKKETSIGVSATGGKKTTFADE | |
| 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 |
|---|---|---|---|---|---|
| 97 | Acetylation | KRIQRDFKGLPPAQD HHHHHHHCCCCCHHC | 64.92 | 24489116 | |
| 113 | Phosphorylation | SAAPIQVSTTEKKET CCCCEEEECCCCEEE | 17.15 | 30377154 | |
| 114 | Phosphorylation | AAPIQVSTTEKKETS CCCEEEECCCCEEEE | 39.87 | 30377154 | |
| 115 | Phosphorylation | APIQVSTTEKKETSI CCEEEECCCCEEEEE | 38.00 | 30377154 | |
| 117 | Acetylation | IQVSTTEKKETSIGV EEEECCCCEEEEEEE | 54.54 | 24489116 | |
| 120 | Phosphorylation | STTEKKETSIGVSAT ECCCCEEEEEEEECC | 34.23 | 22369663 | |
| 121 | Phosphorylation | TTEKKETSIGVSATG CCCCEEEEEEEECCC | 20.59 | 22369663 | |
| 125 | Phosphorylation | KETSIGVSATGGKKT EEEEEEEECCCCCCC | 18.20 | 22890988 | |
| 127 | Phosphorylation | TSIGVSATGGKKTTF EEEEEECCCCCCCCC | 38.67 | 22890988 | |
| 130 | Acetylation | GVSATGGKKTTFADE EEECCCCCCCCCCCC | 48.57 | 25381059 | |
| 133 | Phosphorylation | ATGGKKTTFADE--- CCCCCCCCCCCC--- | 26.21 | 28889911 |
| 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 RPA14_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPA14_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 RPA14_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, 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-121 AND THR-133, ANDMASS SPECTROMETRY. | |
| "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 SER-121, AND MASSSPECTROMETRY. | |
