| UniProt ID | RPC3_YEAST | |
|---|---|---|
| UniProt AC | P32349 | |
| Protein Name | DNA-directed RNA polymerase III subunit RPC3 | |
| Gene Name | RPC82 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 654 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.. | |
| Protein Sequence | MDELLGEALSAENQTGESTVESEKLVTPEDVMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVALGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQETAISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEEEHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSLFVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNSPLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTSLRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQVYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAELVEEKTPGLTFNAIDLARHLPAELDLRGSLLSRKPSDNKKRSGSNAAASLPSKKLKTEDGFVIPALPAAVSKSLQESGDTQEEDEEEEDLDADTEDPHSASLINSHLKILASSNFPFLNETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRLSRCIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVEIQEVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMANLLFKKEKLKQENSTLLKKANRDDVKGRENELLLPSELNQLKMVNERELNVFARLSRLLSLWEVFQMA | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | ELLGEALSAENQTGE HHHHHHHHCCCCCCC | 40.35 | 30377154 | |
| 15 | Phosphorylation | ALSAENQTGESTVES HHHCCCCCCCCCCCC | 55.27 | 30377154 | |
| 19 | Phosphorylation | ENQTGESTVESEKLV CCCCCCCCCCCCCCC | 24.80 | 30377154 | |
| 22 | Phosphorylation | TGESTVESEKLVTPE CCCCCCCCCCCCCHH | 35.38 | 30377154 | |
| 27 | Phosphorylation | VESEKLVTPEDVMTI CCCCCCCCHHHHEEH | 31.25 | 28889911 | |
| 106 | Phosphorylation | TQLRCVKYLQETAIS HHHHHHHHHHHHHCC | 8.01 | 19823750 | |
| 110 | Phosphorylation | CVKYLQETAISGKKT HHHHHHHHHCCCCCE | 19.14 | 19823750 | |
| 113 | Phosphorylation | YLQETAISGKKTTYY HHHHHHCCCCCEEEE | 41.94 | 19823750 | |
| 230 | Phosphorylation | YKNIPRNSPLSDLKK HCCCCCCCCHHHHHH | 28.62 | 23749301 | |
| 268 | Acetylation | QILTVDPKTSLRIVK HCEEECCCCCCEEEC | 46.40 | 24489116 | |
| 392 | Phosphorylation | PSDNKKRSGSNAAAS CCCCCCCCCCCCCCC | 56.29 | 22369663 | |
| 394 | Phosphorylation | DNKKRSGSNAAASLP CCCCCCCCCCCCCCC | 25.25 | 22369663 | |
| 399 | Phosphorylation | SGSNAAASLPSKKLK CCCCCCCCCCCCCCC | 35.77 | 29136822 | |
| 402 | Phosphorylation | NAAASLPSKKLKTED CCCCCCCCCCCCCCC | 47.95 | 19823750 | |
| 421 | Phosphorylation | PALPAAVSKSLQESG CCHHHHHHHHHHHHC | 16.29 | 30377154 | |
| 423 | Phosphorylation | LPAAVSKSLQESGDT HHHHHHHHHHHHCCC | 27.98 | 22369663 | |
| 427 | Phosphorylation | VSKSLQESGDTQEED HHHHHHHHCCCCCCC | 29.07 | 22369663 | |
| 430 | Phosphorylation | SLQESGDTQEEDEEE HHHHHCCCCCCCHHH | 41.21 | 22369663 | |
| 444 | Phosphorylation | EEDLDADTEDPHSAS HCCCCCCCCCHHHHH | 43.97 | 22369663 | |
| 449 | Phosphorylation | ADTEDPHSASLINSH CCCCCHHHHHHHHHH | 25.58 | 22369663 | |
| 451 | Phosphorylation | TEDPHSASLINSHLK CCCHHHHHHHHHHHH | 32.56 | 22369663 | |
| 455 | Phosphorylation | HSASLINSHLKILAS HHHHHHHHHHHHHHH | 24.17 | 22369663 | |
| 462 | Phosphorylation | SHLKILASSNFPFLN HHHHHHHHCCCCCCC | 23.51 | 27017623 | |
| 471 | Phosphorylation | NFPFLNETKPGVYYV CCCCCCCCCCCEEEE | 41.27 | 27017623 | |
| 489 | Phosphorylation | KLMPVLKSSVYEYVI HHHHHHHHCHHHHHH | 22.37 | 28889911 | |
| 490 | Phosphorylation | LMPVLKSSVYEYVIA HHHHHHHCHHHHHHH | 27.42 | 30377154 | |
| 492 | Phosphorylation | PVLKSSVYEYVIAST HHHHHCHHHHHHHHH | 11.95 | 28889911 | |
| 494 | Phosphorylation | LKSSVYEYVIASTLG HHHCHHHHHHHHHHC | 4.58 | 28889911 | |
| 498 | Phosphorylation | VYEYVIASTLGPSAM HHHHHHHHHHCHHHH | 17.03 | 28889911 | |
| 503 | Phosphorylation | IASTLGPSAMRLSRC HHHHHCHHHHHHHHH | 32.66 | 30377154 | |
| 508 | Phosphorylation | GPSAMRLSRCIRDNK CHHHHHHHHHHHCCC | 18.10 | 28889911 | |
| 520 | Acetylation | DNKLVSEKIINSTAL CCCCHHHHHHCCHHH | 41.18 | 22865919 | |
| 545 | Phosphorylation | ASLIRYNSVEIQEVP HHHHHHCCEECEECC | 16.52 | 30377154 | |
| 600 | Phosphorylation | EKLKQENSTLLKKAN HHHHHHHHHHHHHHC | 21.49 | 30377154 |
| 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 RPC3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPC3_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 RPC3_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-27 AND SER-394, 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 SER-392 AND SER-394, ANDMASS SPECTROMETRY. | |
| "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-394, AND MASSSPECTROMETRY. | |
