| UniProt ID | RSC9_YEAST | |
|---|---|---|
| UniProt AC | Q03124 | |
| Protein Name | Chromatin structure-remodeling complex subunit RSC9 | |
| Gene Name | RSC9 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 581 | |
| Subcellular Localization | Nucleus . Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. | |
| Protein Description | Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit plays a role in transcriptional response to stress. It is involved in both repression and activation of mRNAs regulated by the target of rapamycin (TOR) kinases, and in the synthesis of rRNA.. | |
| Protein Sequence | MNSLASNTPLNGTPVSEAPATSSEPVNMFETMVANPIKVSRLQSNGVLTGPAANTKSIHYSLANFNVFQSLPKETARGVDDLTRMEMALLSGIPEEIKWSLKKYLTYSNKAPYMISLRTLPDLLPLFKTFILPLERIVEGLNKSSICDSKAMDSLQMGLNALLILRNLAQDTDSVQILVKDREIKSFILFILKKFQCVATGDNKWQLYEGNATFFNELTHYTLDLMEAISSYIAPAMKDDHYFQTLVSILNYTKDRYMVISILRSLSRLLVRSKANEESAADNLDHKTLSLIVSFLLLECDSELIIASLDFLYQYILPGSQRITELFKSKECSLILEATLPNLLSYNIATPDYHLLQKHKIRLIKRLKPPAPKEPPNLSEDLFQQLFKLNEPLRSTAWLRCCFEPVQEAEFTQISLWRSYESKFGQPVRESGRKLLPAVEFIKNVSNAFNNAAAIVITDPVTGKKRFVIKGIQPRFKALGIADGERESQVPISALKSKFLNDSKEITPARQNSIPEVKFPQELSDVSKVACTFLCLLSNDTDDGAGSAFCQRIRPLVLHKLADIPPLTLALSEYMENTSGL | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | VSEAPATSSEPVNMF CCCCCCCCCCCCCCH | 34.51 | 28889911 | |
| 44 | Phosphorylation | IKVSRLQSNGVLTGP EEEEEECCCCCEECC | 39.89 | 21440633 | |
| 110 | Ubiquitination | KYLTYSNKAPYMISL HHHHCCCCCCEEEEC | 44.81 | 24961812 | |
| 434 | Ubiquitination | PVRESGRKLLPAVEF CCHHHHCCHHHHHHH | 58.88 | 23749301 | |
| 507 | Phosphorylation | LNDSKEITPARQNSI CCCCCCCCHHHHCCC | 16.40 | 28152593 | |
| 513 | Phosphorylation | ITPARQNSIPEVKFP CCHHHHCCCCCCCCC | 31.05 | 25521595 | |
| 524 | Phosphorylation | VKFPQELSDVSKVAC CCCCHHHHHHHHHHH | 34.90 | 19823750 | |
| 527 | Phosphorylation | PQELSDVSKVACTFL CHHHHHHHHHHHHHH | 26.80 | 19823750 |
| 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 RSC9_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RSC9_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 RSC9_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-22 AND SER-44, 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-513, AND MASSSPECTROMETRY. | |
