| UniProt ID | RSC2_YEAST | |
|---|---|---|
| UniProt AC | Q06488 | |
| Protein Name | Chromatin structure-remodeling complex subunit RSC2 | |
| Gene Name | RSC2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 889 | |
| 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, and is also essential for 2-micron plasmid maintenance and for normal REP1 protein localization.. | |
| Protein Sequence | MMPDDNSNSSTQNSSALYKDLRKEYESLFTLKEDSGLEISPIFNVLPPKKDYPDYYAVIKNPVSFNTLKKRIPHYTDAQQFMNDVVQIPWNAKTYNTRDSGIYKYALVLEKYLKDTIYPNLKEKYPQLVYPDLGPLPDEPGYEEFQQKLREKAEEVARANAARAESSSSMNSTEAARRLRKTRTSVKRESEPGTDTNNDEDYEATDMDIDNPKDADFPDLIRKPLININPYTRKPLRDNRSTTPSHSGTPQPLGPRHRQVSRTQVKRGRPPIIDLPYIQRMKNVMKVLKKEVLDSGIGLTDLFERLPDRHRDANYYIMIANPISLQDINKKVKTRRYKTFQEFQNDFNLMLTNFRISHRGDPESIKISNILEKTFTSLARFELSKPDRSFIPEGELRYPLDEVIVNNISYHVGDWALLRNQNDPQKPIVGQIFRLWKTPDGKQWLNACWYYRPEQTVHRVDRLFYKNEVMKTGQYRDHLVSNLVGKCYVIHFTRYQRGNPDMKLEGPLFVCEFRYNESDKIFNKIRTWKACLPEEIRDLDEATIPVNGRKFFKYPSPIRHLLPANATPHDRVPEPTMGSPDAPPLVGAVYMRPKMQRDDLGEYATSDDCPRYIIRPNDSPEEGQVDIETGTITTNTPTANALPKTGYSSSKLSSLRYNRSSMSLENQNAIGQQQIPLSRVGSPGAGGPLTVQGLKQHQLQRLQQQQHQYQQQKRSQASRYNIPTIIDDLTSQASRGNLGNIMIDAASSFVLPISITKNVDVLQRTDLHSQTKRSGREEMFPWKKTKGEILWFRGPSVIVNERIINSGDPHLSLPLNRWFTTNKKRKLEYEEVEETMEDVTGKDKDDDGLEPDVENEKESLPGPFVLGLRPSAKFTAHRLSMLRPPSSSS | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MMPDDNSNSSTQNS -CCCCCCCCCCCCCH | 45.12 | 27214570 | |
| 10 | Phosphorylation | PDDNSNSSTQNSSAL CCCCCCCCCCCHHHH | 37.96 | 28889911 | |
| 11 | Phosphorylation | DDNSNSSTQNSSALY CCCCCCCCCCHHHHH | 31.43 | 20190278 | |
| 166 | Phosphorylation | ANAARAESSSSMNST HHHHHHHCCCCCCHH | 34.24 | 28889911 | |
| 167 | Phosphorylation | NAARAESSSSMNSTE HHHHHHCCCCCCHHH | 20.24 | 30377154 | |
| 168 | Phosphorylation | AARAESSSSMNSTEA HHHHHCCCCCCHHHH | 42.77 | 30377154 | |
| 169 | Phosphorylation | ARAESSSSMNSTEAA HHHHCCCCCCHHHHH | 24.75 | 25752575 | |
| 172 | Phosphorylation | ESSSSMNSTEAARRL HCCCCCCHHHHHHHH | 20.98 | 28889911 | |
| 182 | Phosphorylation | AARRLRKTRTSVKRE HHHHHHHHHHHCCCC | 32.52 | 24961812 | |
| 184 | Phosphorylation | RRLRKTRTSVKRESE HHHHHHHHHCCCCCC | 43.00 | 24961812 | |
| 185 | Phosphorylation | RLRKTRTSVKRESEP HHHHHHHHCCCCCCC | 23.50 | 24961812 | |
| 190 | Phosphorylation | RTSVKRESEPGTDTN HHHCCCCCCCCCCCC | 53.80 | 29136822 | |
| 194 | Phosphorylation | KRESEPGTDTNNDED CCCCCCCCCCCCCHH | 50.82 | 20377248 | |
| 196 | Phosphorylation | ESEPGTDTNNDEDYE CCCCCCCCCCCHHCC | 35.44 | 29136822 | |
| 202 | Phosphorylation | DTNNDEDYEATDMDI CCCCCHHCCCCCCCC | 12.86 | 28889911 | |
| 205 | Phosphorylation | NDEDYEATDMDIDNP CCHHCCCCCCCCCCC | 21.66 | 29136822 | |
| 241 | Phosphorylation | KPLRDNRSTTPSHSG CCCCCCCCCCCCCCC | 42.77 | 22369663 | |
| 242 | Phosphorylation | PLRDNRSTTPSHSGT CCCCCCCCCCCCCCC | 39.22 | 22369663 | |
| 243 | Phosphorylation | LRDNRSTTPSHSGTP CCCCCCCCCCCCCCC | 24.84 | 22369663 | |
| 245 | Phosphorylation | DNRSTTPSHSGTPQP CCCCCCCCCCCCCCC | 28.35 | 22369663 | |
| 247 | Phosphorylation | RSTTPSHSGTPQPLG CCCCCCCCCCCCCCC | 49.01 | 22369663 | |
| 249 | Phosphorylation | TTPSHSGTPQPLGPR CCCCCCCCCCCCCCC | 23.05 | 22369663 | |
| 295 | Phosphorylation | LKKEVLDSGIGLTDL HHHHHHHCCCCHHHH | 28.31 | 22369663 | |
| 300 | Phosphorylation | LDSGIGLTDLFERLP HHCCCCHHHHHHHCC | 25.99 | 22369663 | |
| 364 | Phosphorylation | SHRGDPESIKISNIL CCCCCHHHCEEHHHH | 34.27 | 25521595 | |
| 373 | Acetylation | KISNILEKTFTSLAR EEHHHHHHHHHHHHH | 45.56 | 24489116 | |
| 481 | Phosphorylation | QYRDHLVSNLVGKCY CCHHHHHHHHCCEEE | 30.70 | 28889911 | |
| 590 | Phosphorylation | PPLVGAVYMRPKMQR CCCCEEEEECCCCCC | 6.20 | 28889911 | |
| 612 | Phosphorylation | TSDDCPRYIIRPNDS CCCCCCCEEECCCCC | 5.95 | 19779198 | |
| 619 | Phosphorylation | YIIRPNDSPEEGQVD EEECCCCCCCCCCEE | 40.63 | 21440633 | |
| 648 | Phosphorylation | ALPKTGYSSSKLSSL CCCCCCCCHHHHHHH | 29.49 | 21440633 | |
| 650 | Phosphorylation | PKTGYSSSKLSSLRY CCCCCCHHHHHHHCC | 31.51 | 21440633 | |
| 651 | Acetylation | KTGYSSSKLSSLRYN CCCCCHHHHHHHCCC | 55.10 | 24489116 | |
| 653 | Phosphorylation | GYSSSKLSSLRYNRS CCCHHHHHHHCCCCC | 30.94 | 21440633 | |
| 654 | Phosphorylation | YSSSKLSSLRYNRSS CCHHHHHHHCCCCCC | 27.57 | 21440633 | |
| 657 | Phosphorylation | SKLSSLRYNRSSMSL HHHHHHCCCCCCCCC | 21.88 | 20377248 | |
| 660 | Phosphorylation | SSLRYNRSSMSLENQ HHHCCCCCCCCCCCC | 27.10 | 22369663 | |
| 661 | Phosphorylation | SLRYNRSSMSLENQN HHCCCCCCCCCCCCC | 14.78 | 22369663 | |
| 663 | Phosphorylation | RYNRSSMSLENQNAI CCCCCCCCCCCCCCC | 34.18 | 20377248 | |
| 678 | Phosphorylation | GQQQIPLSRVGSPGA CCCCCCHHHCCCCCC | 21.40 | 21551504 | |
| 682 | Phosphorylation | IPLSRVGSPGAGGPL CCHHHCCCCCCCCCC | 19.80 | 22369663 | |
| 690 | Phosphorylation | PGAGGPLTVQGLKQH CCCCCCCCHHHHHHH | 17.57 | 22890988 | |
| 806 | Phosphorylation | VNERIINSGDPHLSL ECCEECCCCCCCCCC | 33.88 | 27214570 | |
| 873 | Acetylation | LGLRPSAKFTAHRLS EECCCCCCHHHHHHH | 47.81 | 25381059 | |
| 886 | Phosphorylation | LSMLRPPSSSS---- HHHCCCCCCCC---- | 45.60 | 27214570 | |
| 887 | Phosphorylation | SMLRPPSSSS----- HHCCCCCCCC----- | 40.13 | 21440633 | |
| 888 | Phosphorylation | MLRPPSSSS------ HCCCCCCCC------ | 44.39 | 27214570 | |
| 889 | Phosphorylation | LRPPSSSS------- CCCCCCCC------- | 46.30 | 27214570 |
| 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 RSC2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RSC2_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 RSC2_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-7; SER-10; SER-166;SER-169; THR-243; SER-660; SER-661 AND SER-682, AND MASS 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-682, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND MASSSPECTROMETRY. | |
