| UniProt ID | RPC7_YEAST | |
|---|---|---|
| UniProt AC | P17890 | |
| Protein Name | DNA-directed RNA polymerase III subunit RPC7 | |
| Gene Name | RPC31 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 251 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. C31 is involved in the formation of the initiation complex.. | |
| Protein Sequence | MSSYRGGSRGGGSNYMSNLPFGLGYGDVGKNHITEFPSIPLPINGPITNKERSLAVKYINFGKTVKDGPFYTGSMSLIIDQQENSKSGKRKPNIILDEDDTNDGIERYSDKYLKKRKIGISIDDHPYNLNLFPNELYNVMGINKKKLLAISKFNNADDVFTGTGLQDENIGLSMLAKLKELAEDVDDASTGDGAAKGSKTGEGEDDDLADDDFEEDEDEEDDDDYNAEKYFNNGDDDDYGDEEDPNEEAAF | |
| 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 |
|---|---|---|---|---|---|
| 17 | Phosphorylation | GGGSNYMSNLPFGLG CCCCCCHHCCCCCCC | 25.51 | 27017623 | |
| 50 | Acetylation | INGPITNKERSLAVK CCCCCCCCCCCEEEE | 45.94 | 24489116 | |
| 57 | Acetylation | KERSLAVKYINFGKT CCCCEEEEEEECCCE | 34.50 | 24489116 | |
| 101 | Phosphorylation | IILDEDDTNDGIERY EECCCCCCCCHHHHH | 47.75 | 21082442 | |
| 111 | Acetylation | GIERYSDKYLKKRKI HHHHHHHHHHHHCCE | 46.68 | 24489116 | |
| 152 | Acetylation | KKLLAISKFNNADDV HHEEEEECCCCCCCC | 46.10 | 25381059 | |
| 189 | Phosphorylation | AEDVDDASTGDGAAK HHCCCCCCCCCCCCC | 39.66 | 22369663 | |
| 190 | Phosphorylation | EDVDDASTGDGAAKG HCCCCCCCCCCCCCC | 40.80 | 22369663 | |
| 198 | Phosphorylation | GDGAAKGSKTGEGED CCCCCCCCCCCCCCC | 26.74 | 20377248 |
| 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 RPC7_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPC7_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 RPC7_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 SER-189, 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-189 AND THR-190, ANDMASS SPECTROMETRY. | |
| "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-189, AND MASSSPECTROMETRY. | |
