| UniProt ID | RSC7_YEAST | |
|---|---|---|
| UniProt AC | P32832 | |
| Protein Name | Chromatin structure-remodeling complex subunit RSC7 | |
| Gene Name | NPL6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 435 | |
| Subcellular Localization | Nucleus . | |
| 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. Together with HTL1, LDB7, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity. Acidic protein important for nuclear protein localization.. | |
| Protein Sequence | MSDSEGGLASEVEHEKRSRSTSNRPNYAIDTEDLDIDENDENEDDDYREEEANEGVNEEEISDEEEQINKSGRNKRRHVDEEEDLSEDKGVTRSRNRSKFKKPVFPGIDDAEENLNPLKVVNEEYVLPDDPEGETKITADGDLLGGREFLVRTFTLTEKGNRKFMLATEPARIVGFRDSYLFFQTHPNLYKFILNQTQKNDLIDRGVLPYSYRNRQIALVTARGVFKEFGAKIIRGGKHITDDYYASELRTKGNVIEGKLAGDPIDKSARALETMMYPASENGINPAKNQVEFFEHRPHGHMSNSNIIASGSKLSSTNWLYQHSAACSRFNSDLFYDRVKVLLVDQQGLRDAYTNILHIPESTQSTTVLGWRRSKNDSPSDTSIVYETVIHDNDLNKPKTGLSEIPKEIYEDVVDEDVLRAITEQQNFEKCNEYI | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSDSEGGLA ------CCCCCCCCH | 50.25 | 22369663 | |
| 4 | Phosphorylation | ----MSDSEGGLASE ----CCCCCCCCHHH | 30.73 | 22369663 | |
| 10 | Phosphorylation | DSEGGLASEVEHEKR CCCCCCHHHHHHHHH | 47.41 | 22369663 | |
| 16 | Acetylation | ASEVEHEKRSRSTSN HHHHHHHHHCCCCCC | 58.54 | 24489116 | |
| 18 | Phosphorylation | EVEHEKRSRSTSNRP HHHHHHHCCCCCCCC | 41.47 | 22369663 | |
| 62 | Phosphorylation | GVNEEEISDEEEQIN CCCHHHCCHHHHHHH | 42.10 | 27214570 | |
| 86 | Phosphorylation | VDEEEDLSEDKGVTR CCCCCCCCCCCCCCC | 56.95 | 25533186 | |
| 89 | Acetylation | EEDLSEDKGVTRSRN CCCCCCCCCCCCCCC | 51.75 | 24489116 | |
| 92 | Phosphorylation | LSEDKGVTRSRNRSK CCCCCCCCCCCCHHH | 31.43 | 29136822 | |
| 101 | Acetylation | SRNRSKFKKPVFPGI CCCHHHCCCCCCCCC | 60.96 | 25381059 | |
| 102 | Acetylation | RNRSKFKKPVFPGID CCHHHCCCCCCCCCC | 49.93 | 25381059 | |
| 155 | Phosphorylation | EFLVRTFTLTEKGNR EEEEEEEEEEECCCE | 31.96 | 28889911 | |
| 244 | Phosphorylation | GKHITDDYYASELRT CCCCCCCCHHHHHHC | 12.07 | 27017623 | |
| 245 | Phosphorylation | KHITDDYYASELRTK CCCCCCCHHHHHHCC | 15.62 | 27017623 | |
| 252 | Acetylation | YASELRTKGNVIEGK HHHHHHCCCCEECCC | 41.89 | 24489116 | |
| 259 | Acetylation | KGNVIEGKLAGDPID CCCEECCCCCCCCCC | 23.52 | 24489116 | |
| 267 | Acetylation | LAGDPIDKSARALET CCCCCCCHHHHHHHH | 46.89 | 24489116 | |
| 268 | Phosphorylation | AGDPIDKSARALETM CCCCCCHHHHHHHHH | 21.17 | 30377154 | |
| 280 | Phosphorylation | ETMMYPASENGINPA HHHHCCHHHCCCCCC | 27.39 | 25752575 | |
| 332 | Phosphorylation | AACSRFNSDLFYDRV HHHHHCCCCHHHHHE | 32.74 | 30377154 | |
| 374 | Phosphorylation | TVLGWRRSKNDSPSD EEEEEEECCCCCCCC | 27.51 | 30377154 | |
| 378 | Phosphorylation | WRRSKNDSPSDTSIV EEECCCCCCCCCEEE | 35.38 | 22369663 | |
| 380 | Phosphorylation | RSKNDSPSDTSIVYE ECCCCCCCCCEEEEE | 58.43 | 22369663 | |
| 382 | Phosphorylation | KNDSPSDTSIVYETV CCCCCCCCEEEEEEE | 25.37 | 29734811 | |
| 383 | Phosphorylation | NDSPSDTSIVYETVI CCCCCCCEEEEEEEE | 18.30 | 22369663 | |
| 386 | Phosphorylation | PSDTSIVYETVIHDN CCCCEEEEEEEECCC | 12.29 | 20377248 | |
| 388 | Phosphorylation | DTSIVYETVIHDNDL CCEEEEEEEECCCCC | 13.68 | 19823750 | |
| 430 | Ubiquitination | TEQQNFEKCNEYI-- HHHHCHHHHHHCC-- | 37.92 | 23749301 |
| 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 RSC7_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RSC7_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 RSC7_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-86 AND THR-155, 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-86, AND MASSSPECTROMETRY. | |
| "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-86, AND MASSSPECTROMETRY. | |
