| UniProt ID | RSC1_YEAST | |
|---|---|---|
| UniProt AC | P53236 | |
| Protein Name | Chromatin structure-remodeling complex subunit RSC1 | |
| Gene Name | RSC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 928 | |
| 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 is involved in meiotic sporulation through regulating IME2 expression.. | |
| Protein Sequence | MVEQDNGFLQKLLKTQYDAVFHLKDENGIEIYPIFNVLPPKKEYPDYYIIIRNPISLNTLKKRLPHYTSPQDFVNDFAQIPWNAMTYNAKDSVIYKYAILLESFIKGKIVHNIRKHYPEVTYPSLGRIPEIFAESMQPSDLSSNPINTQENDEKAGLNPEMKMAFAKLDSSITERKPTNQDYRMQQKNSPAFPTHSASITPQPLASPTPVVNYANITSAHPKTHVRRGRPPVIDLPYVLRIKNILKMMRREVDQNNKTLTLCFEKLPDRNEEPTYYSVITDPICLMDIRKKVKSRKYRNFHTFEEDFQLMLTNFKLYYSQDQSNIIRAQLLEKNFNRLVRIELSKPDEDYLPEGELRYPLDDVEINDEKYQIGDWVLLHNPNDINKPIVGQIFRLWSTTDGNKWLNACWYFRPEQTVHRVDRLFYKNEVMKTGQYRDHPIQDIKGKCYVIHFTRFQRGDPSTKVNGPQFVCEFRYNESDKVFNKIRTWKACLPEELRDQDEPTIPVNGRKFFKYPSPIADLLPANATLNDKVPEPTEGAPTAPPLVGAVYLGPKLERDDLGEYSTSDDCPRYIIRPNDPPEEGKIDYETGTIITDTLTTSSMPRVNSSSTIRLPTLKQTKSIPSSNFRSSSNTPLLHQNFNQTSNFLKLENMNNSSHNLLSHPSVPKFQSPSLLEQSSRSKYHSAKKQTQLSSTAPKKPASKSFTLSSMINTLTAHTSKYNFNHIVIEAPGAFVVPVPMEKNIRTIQSTERFSRSNLKNAQNLGNTAINDINTANEQIIWFKGPGVKITERVIDSGNDLVRVPLNRWFCKNKRRKLDYEDIEEDVMEPPNDFSEDMIANIFNPPPSLNLDMDLNLSPSSNNSSNFMDLSTIASGDNDGKECDTAEESEDENEDTEDEHEIEDIPTTSAFGLNSSAEYLAFRLREFNKL | |
| 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 |
|---|---|---|---|---|---|
| 170 | Phosphorylation | MAFAKLDSSITERKP HHHHHCCCCHHCCCC | 33.79 | 30377154 | |
| 171 | Phosphorylation | AFAKLDSSITERKPT HHHHCCCCHHCCCCC | 32.94 | 30377154 | |
| 173 | Phosphorylation | AKLDSSITERKPTNQ HHCCCCHHCCCCCCH | 31.52 | 30377154 | |
| 178 | Phosphorylation | SITERKPTNQDYRMQ CHHCCCCCCHHHHHH | 48.85 | 21126336 | |
| 189 | Phosphorylation | YRMQQKNSPAFPTHS HHHHHCCCCCCCCCC | 25.33 | 21440633 | |
| 194 | Phosphorylation | KNSPAFPTHSASITP CCCCCCCCCCCCCCC | 23.24 | 21440633 | |
| 196 | Phosphorylation | SPAFPTHSASITPQP CCCCCCCCCCCCCCC | 26.62 | 24961812 | |
| 198 | Phosphorylation | AFPTHSASITPQPLA CCCCCCCCCCCCCCC | 29.97 | 20377248 | |
| 200 | Phosphorylation | PTHSASITPQPLASP CCCCCCCCCCCCCCC | 17.24 | 21440633 | |
| 206 | Phosphorylation | ITPQPLASPTPVVNY CCCCCCCCCCCEECC | 36.67 | 25752575 | |
| 208 | Phosphorylation | PQPLASPTPVVNYAN CCCCCCCCCEECCCC | 26.64 | 21440633 | |
| 213 | Phosphorylation | SPTPVVNYANITSAH CCCCEECCCCCCCCC | 6.87 | 21440633 | |
| 217 | Phosphorylation | VVNYANITSAHPKTH EECCCCCCCCCCCCC | 21.48 | 21440633 | |
| 218 | Phosphorylation | VNYANITSAHPKTHV ECCCCCCCCCCCCCC | 22.30 | 20377248 | |
| 242 | Acetylation | LPYVLRIKNILKMMR HHHHHHHHHHHHHHH | 31.34 | 25381059 | |
| 426 | Acetylation | RVDRLFYKNEVMKTG HHHHEEECCCCCCCC | 39.02 | 24489116 | |
| 572 | Phosphorylation | TSDDCPRYIIRPNDP CCCCCCCEEECCCCC | 5.95 | 28889911 | |
| 591 | Phosphorylation | KIDYETGTIITDTLT CCCCCCCCEEEECCC | 19.34 | 27017623 | |
| 594 | Phosphorylation | YETGTIITDTLTTSS CCCCCEEEECCCCCC | 21.05 | 27017623 | |
| 596 | Phosphorylation | TGTIITDTLTTSSMP CCCEEEECCCCCCCC | 19.84 | 27017623 | |
| 599 | Phosphorylation | IITDTLTTSSMPRVN EEEECCCCCCCCCCC | 23.16 | 27017623 | |
| 601 | Phosphorylation | TDTLTTSSMPRVNSS EECCCCCCCCCCCCC | 30.62 | 27017623 | |
| 607 | Phosphorylation | SSMPRVNSSSTIRLP CCCCCCCCCCCEECC | 23.86 | 22369663 | |
| 608 | Phosphorylation | SMPRVNSSSTIRLPT CCCCCCCCCCEECCC | 26.71 | 22369663 | |
| 609 | Phosphorylation | MPRVNSSSTIRLPTL CCCCCCCCCEECCCC | 27.89 | 22369663 | |
| 610 | Phosphorylation | PRVNSSSTIRLPTLK CCCCCCCCEECCCCC | 16.44 | 23749301 | |
| 615 | Phosphorylation | SSTIRLPTLKQTKSI CCCEECCCCCCCCCC | 51.70 | 22369663 | |
| 619 | Phosphorylation | RLPTLKQTKSIPSSN ECCCCCCCCCCCCCC | 25.77 | 28889911 | |
| 629 | Phosphorylation | IPSSNFRSSSNTPLL CCCCCCCCCCCCCCC | 33.70 | 21551504 | |
| 630 | Phosphorylation | PSSNFRSSSNTPLLH CCCCCCCCCCCCCCC | 24.29 | 21082442 | |
| 631 | Phosphorylation | SSNFRSSSNTPLLHQ CCCCCCCCCCCCCCC | 46.07 | 25752575 | |
| 633 | Phosphorylation | NFRSSSNTPLLHQNF CCCCCCCCCCCCCCC | 19.77 | 21440633 | |
| 655 | Phosphorylation | KLENMNNSSHNLLSH EEECCCCCCCCCCCC | 28.15 | 20377248 | |
| 656 | Phosphorylation | LENMNNSSHNLLSHP EECCCCCCCCCCCCC | 20.65 | 29136822 | |
| 661 | Phosphorylation | NSSHNLLSHPSVPKF CCCCCCCCCCCCCCC | 36.20 | 24961812 | |
| 664 | Phosphorylation | HNLLSHPSVPKFQSP CCCCCCCCCCCCCCH | 45.70 | 29136822 | |
| 670 | Phosphorylation | PSVPKFQSPSLLEQS CCCCCCCCHHHHHHH | 21.42 | 22369663 | |
| 672 | Phosphorylation | VPKFQSPSLLEQSSR CCCCCCHHHHHHHHH | 51.32 | 22369663 | |
| 687 | Ubiquitination | SKYHSAKKQTQLSST HHHHHHHHHHCCCCC | 59.29 | 23749301 | |
| 689 | Phosphorylation | YHSAKKQTQLSSTAP HHHHHHHHCCCCCCC | 40.12 | 30377154 | |
| 693 | Phosphorylation | KKQTQLSSTAPKKPA HHHHCCCCCCCCCCC | 36.86 | 30377154 | |
| 753 | Phosphorylation | IQSTERFSRSNLKNA HHCCHHHCHHHHHHH | 40.81 | 21126336 | |
| 789 | Phosphorylation | KGPGVKITERVIDSG ECCCCEEEEEEECCC | 16.42 | 28889911 | |
| 795 | Phosphorylation | ITERVIDSGNDLVRV EEEEEECCCCCEEEE | 28.50 | 28889911 |
| 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 RSC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RSC1_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 RSC1_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-206; SER-607; SER-655AND SER-670, 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-607, AND MASSSPECTROMETRY. | |
