| UniProt ID | RSC4_YEAST | |
|---|---|---|
| UniProt AC | Q02206 | |
| Protein Name | Chromatin structure-remodeling complex subunit RSC4 | |
| Gene Name | RSC4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 625 | |
| 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.. | |
| Protein Sequence | MVVKKRKLATEAGGSDERPKYLPGKHPKNQEKTPHVDYNAPLNPKSELFLDDWHIPKFNRFISFTLDVLIDKYKDIFKDFIKLPSRKFHPQYYYKIQQPMSINEIKSRDYEYEDGPSNFLLDVELLTKNCQAYNEYDSLIVKNSMQVVMLIEFEVLKAKNLKRNYLINSEVKAKLLHYLNKLVDATEKKINQALLGASSPKNLDDKVKLSEPFMELVDKDELPEYYEIVHSPMALSIVKQNLEIGQYSKIYDFIIDMLLVFQNAHIFNDPSALIYKDATTLTNYFNYLIQKEFFPELQDLNERGEINLEFDKFEFENYLAIGGGGPAAAGALAISALDNDIEPESNREDLIDQADYDFNHFEGLGNGYNRSLLTEDYLLNPNNFKKLIAKPETVQSEVKNERSTTSDIEKTNSLESEHLKIPKYNVIKSMQKEMQSLSEQHTMEYKPYKLIQQIYIFSSKNLYSQATKPLLGSRPSCNQNWVEYIFNGNELSQNENAFSFMLQPMQTFLTLQSHLTSSLKDTETLLTINKEPVKSRTSNVNSNLSQPQQQENDVIGNDTKQDIENLTIGGGNNNDIVGNDNDKRNNITEIFDIRLSEGLNHLMFRCEDKISHETEFMNFWINVLP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 10 | Phosphorylation | VKKRKLATEAGGSDE CCCCCCCCCCCCCCC | 36.48 | 22369663 | |
| 15 | Phosphorylation | LATEAGGSDERPKYL CCCCCCCCCCCCCCC | 35.07 | 22369663 | |
| 25 | Acetylation | RPKYLPGKHPKNQEK CCCCCCCCCCCCCCC | 55.59 | 24489116 | |
| 32 | Acetylation | KHPKNQEKTPHVDYN CCCCCCCCCCCCCCC | 58.55 | 24489116 | |
| 82 | Acetylation | DIFKDFIKLPSRKFH HHHHHHHCCCCCCCC | 55.10 | 24489116 | |
| 87 | Acetylation | FIKLPSRKFHPQYYY HHCCCCCCCCHHHEE | 52.97 | 25381059 | |
| 181 | Acetylation | KLLHYLNKLVDATEK HHHHHHHHHHHHHHH | 47.49 | 24489116 | |
| 198 | Phosphorylation | NQALLGASSPKNLDD HHHHHCCCCCCCCCC | 45.43 | 17563356 | |
| 199 | Phosphorylation | QALLGASSPKNLDDK HHHHCCCCCCCCCCC | 39.08 | 22369663 | |
| 279 | Phosphorylation | ALIYKDATTLTNYFN CEEECCHHHHHHHHH | 32.26 | 27017623 | |
| 282 | Phosphorylation | YKDATTLTNYFNYLI ECCHHHHHHHHHHHH | 26.27 | 27017623 | |
| 284 | Phosphorylation | DATTLTNYFNYLIQK CHHHHHHHHHHHHHH | 6.48 | 27017623 | |
| 287 | Phosphorylation | TLTNYFNYLIQKEFF HHHHHHHHHHHHHHC | 8.69 | 27017623 | |
| 371 | Phosphorylation | LGNGYNRSLLTEDYL CCCCCCHHHCCCCCC | 24.88 | 30377154 | |
| 393 | Phosphorylation | KLIAKPETVQSEVKN HHHCCCHHHHHHHCC | 32.16 | 21551504 | |
| 403 | Phosphorylation | SEVKNERSTTSDIEK HHHCCCCCCCCHHHH | 29.83 | 21440633 | |
| 404 | Phosphorylation | EVKNERSTTSDIEKT HHCCCCCCCCHHHHH | 36.22 | 27214570 | |
| 405 | Phosphorylation | VKNERSTTSDIEKTN HCCCCCCCCHHHHHC | 26.16 | 19823750 | |
| 406 | Phosphorylation | KNERSTTSDIEKTNS CCCCCCCCHHHHHCC | 36.36 | 17330950 | |
| 410 | Acetylation | STTSDIEKTNSLESE CCCCHHHHHCCCCCC | 54.03 | 24489116 | |
| 411 | Phosphorylation | TTSDIEKTNSLESEH CCCHHHHHCCCCCCC | 19.76 | 22369663 | |
| 413 | Phosphorylation | SDIEKTNSLESEHLK CHHHHHCCCCCCCCC | 38.45 | 22369663 | |
| 416 | Phosphorylation | EKTNSLESEHLKIPK HHHCCCCCCCCCCCH | 35.29 | 22369663 | |
| 423 | Acetylation | SEHLKIPKYNVIKSM CCCCCCCHHHHHHHH | 53.59 | 22865919 | |
| 445 | Phosphorylation | SEQHTMEYKPYKLIQ HHHHCCCCCHHHHHH | 13.36 | 21440633 | |
| 448 | Phosphorylation | HTMEYKPYKLIQQIY HCCCCCHHHHHHHEE | 17.80 | 27017623 | |
| 455 | Phosphorylation | YKLIQQIYIFSSKNL HHHHHHEEECCCCCH | 7.50 | 27017623 | |
| 458 | Phosphorylation | IQQIYIFSSKNLYSQ HHHEEECCCCCHHHH | 30.74 | 27017623 | |
| 459 | Phosphorylation | QQIYIFSSKNLYSQA HHEEECCCCCHHHHC | 18.14 | 27017623 | |
| 468 | Acetylation | NLYSQATKPLLGSRP CHHHHCCCCCCCCCC | 36.36 | 24489116 | |
| 538 | Phosphorylation | EPVKSRTSNVNSNLS CCCCCCCCCCCCCCC | 37.36 | 30377154 | |
| 542 | Phosphorylation | SRTSNVNSNLSQPQQ CCCCCCCCCCCCCHH | 34.56 | 30377154 | |
| 545 | Phosphorylation | SNVNSNLSQPQQQEN CCCCCCCCCCHHHCC | 44.03 | 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 RSC4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RSC4_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 RSC4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-199; THR-405; SER-406;THR-411; SER-413 AND SER-545, AND MASS 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-198; SER-199 ANDSER-406, AND MASS 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-406, AND MASSSPECTROMETRY. | |
