ID RSC6_YEAST Reviewed; 483 AA. AC P25632; D6VR60; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 02-SEP-2026, entry version 179. DE RecName: Full=Chromatin structure-remodeling complex protein RSC6; DE AltName: Full=Remodel the structure of chromatin complex subunit 6; GN Name=RSC6; OrderedLocusNames=YCR052W; ORFNames=YCR52W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1574125; DOI=10.1038/357038a0; RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., RA Richterich P., Roberts A.B., Rodriguez F., Sanz E., RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., RA Sgouros J.G.; RT "The complete DNA sequence of yeast chromosome III."; RL Nature 357:38-46(1992). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP PROTEIN SEQUENCE OF 416-427, FUNCTION, AND COMPOSITION OF THE RSC COMPLEX. RX PubMed=8980231; DOI=10.1016/s0092-8674(00)81820-6; RA Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H., RA Tempst P., Du J., Laurent B.C., Kornberg R.D.; RT "RSC, an essential, abundant chromatin-remodeling complex."; RL Cell 87:1249-1260(1996). RN [5] RP FUNCTION, AND INTERACTION WITH RSC8. RX PubMed=9685490; DOI=10.1093/nar/26.16.3739; RA Treich I., Ho L., Carlson M.; RT "Direct interaction between Rsc6 and Rsc8/Swh3, two proteins that are RT conserved in SWI/SNF-related complexes."; RL Nucleic Acids Res. 26:3739-3745(1998). RN [6] RP FUNCTION OF THE RSC COMPLEX. RX PubMed=10025404; DOI=10.1016/s0092-8674(00)80551-6; RA Lorch Y., Zhang M., Kornberg R.D.; RT "Histone octamer transfer by a chromatin-remodeling complex."; RL Cell 96:389-392(1999). RN [7] RP FUNCTION OF THE RSC COMPLEX. RX PubMed=10329629; DOI=10.1093/emboj/18.10.2836; RA Moreira J.M.A., Holmberg S.; RT "Transcriptional repression of the yeast CHA1 gene requires the chromatin- RT remodeling complex RSC."; RL EMBO J. 18:2836-2844(1999). RN [8] RP COMPOSITION OF THE RSC COMPLEX. RX PubMed=10619019; DOI=10.1016/s1097-2765(00)80382-2; RA Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., RA Winston F.; RT "Two functionally distinct forms of the RSC nucleosome-remodeling complex, RT containing essential AT hook, BAH, and bromodomains."; RL Mol. Cell 4:715-723(1999). RN [9] RP FUNCTION OF THE RSC COMPLEX. RX PubMed=12183366; DOI=10.1101/gad.995002; RA Saha A., Wittmeyer J., Cairns B.R.; RT "Chromatin remodeling by RSC involves ATP-dependent DNA translocation."; RL Genes Dev. 16:2120-2134(2002). RN [10] RP FUNCTION OF THE RSC COMPLEX. RX PubMed=12072455; DOI=10.1093/genetics/161.2.575; RA Chai B., Hsu J.-M., Du J., Laurent B.C.; RT "Yeast RSC function is required for organization of the cellular RT cytoskeleton via an alternative PKC1 pathway."; RL Genetics 161:575-584(2002). RN [11] RP FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION OF THE RP RSC COMPLEX WITH HISTONES. RX PubMed=12697820; DOI=10.1128/mcb.23.9.3202-3215.2003; RA Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.; RT "The yeast RSC chromatin-remodeling complex is required for kinetochore RT function in chromosome segregation."; RL Mol. Cell. Biol. 23:3202-3215(2003). RN [12] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Component of the chromatin structure-remodeling complex CC (RSC), which is involved in transcription regulation and nucleosome CC positioning. RSC is responsible for the transfer of a histone octamer CC from a nucleosome core particle to naked DNA. The reaction requires ATP CC and involves an activated RSC-nucleosome intermediate. Remodeling CC reaction also involves DNA translocation, DNA twist and conformational CC change. As a reconfigurer of centromeric and flanking nucleosomes, RSC CC complex is required both for proper kinetochore function in chromosome CC segregation and, via a PKC1-dependent signaling pathway, for CC organization of the cellular cytoskeleton. This subunit is essential CC for mitotic growth and suppresses formamide sensitivity of the RSC8 CC mutants. {ECO:0000269|PubMed:10025404, ECO:0000269|PubMed:10329629, CC ECO:0000269|PubMed:12072455, ECO:0000269|PubMed:12183366, CC ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:8980231, CC ECO:0000269|PubMed:9685490}. CC -!- SUBUNIT: Interacts directly with RSC8. Component of the two forms of CC the RSC complex composed of at least either RSC1 or RSC2, and ARP7, CC ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, CC STH1, HTL1 and probably RTT102. The complexes interact with histone and CC histone variant components of centromeric chromatin. CC {ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:9685490}. CC -!- INTERACTION: CC P25632; Q07979: RSC58; NbExp=8; IntAct=EBI-21941, EBI-36549; CC P25632; P43609: RSC8; NbExp=13; IntAct=EBI-21941, EBI-23005; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12697820}. CC Note=Localizes to centromeric and flanking chromatin. Association with CC these loci is dependent on STH1. CC -!- MISCELLANEOUS: Present with 2470 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: To yeast SNF12. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59720; CAA42283.1; -; Genomic_DNA. DR EMBL; AY692985; AAT93004.1; -; Genomic_DNA. DR EMBL; BK006937; DAA07529.1; -; Genomic_DNA. DR PIR; S19466; S19466. DR RefSeq; NP_009981.1; NM_001178766.1. DR PDB; 6K15; EM; 3.40 A; I=1-483. DR PDB; 6KW3; EM; 7.13 A; I=1-483. DR PDB; 6KW4; EM; 7.55 A; I=1-483. DR PDB; 6KW5; EM; 10.13 A; I=1-483. DR PDB; 6TDA; EM; 15.00 A; O=1-483. DR PDB; 6V8O; EM; 3.07 A; M=1-483. DR PDB; 6V92; EM; 20.00 A; M=1-483. DR AlphaFoldDB; P25632; -. DR EMDB; EMD-0777; -. DR EMDB; EMD-0778; -. DR EMDB; EMD-0779; -. DR EMDB; EMD-10465; -. DR EMDB; EMD-21107; -. DR EMDB; EMD-21114; -. DR EMDB; EMD-9905; -. DR SMR; P25632; -. DR BioGRID; 31032; 419. DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2. DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1. DR DIP; DIP-4999N; -. DR FunCoup; P25632; 924. DR IntAct; P25632; 60. DR MINT; P25632; -. DR STRING; 4932.YCR052W; -. DR GlyGen; P25632; 1 site. DR iPTMnet; P25632; -. DR PaxDb; 4932-YCR052W; -. DR PeptideAtlas; P25632; -. DR EnsemblFungi; YCR052W_mRNA; YCR052W; YCR052W. DR GeneID; 850419; -. DR KEGG; sce:YCR052W; -. DR AGR; SGD:S000000648; -. DR SGD; S000000648; RSC6. DR VEuPathDB; FungiDB:YCR052W; -. DR eggNOG; KOG2570; Eukaryota. DR HOGENOM; CLU_032070_0_0_1; -. DR InParanoid; P25632; -. DR OMA; LRCSITI; -. DR OrthoDB; 10263741at2759; -. DR BioCyc; YEAST:G3O-29361-MONOMER; -. DR BioGRID-ORCS; 850419; 2 hits in 10 CRISPR screens. DR PRO; PR:P25632; -. DR Proteomes; UP000002311; Chromosome III. DR RNAct; P25632; protein. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IDA:SGD. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:SGD. DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1. DR InterPro; IPR036885; SWIB_MDM2_dom_sf. DR InterPro; IPR063302; SWIFT. DR PANTHER; PTHR13844; SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY D; 1. DR Pfam; PF29592; SWIFT; 1. DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1. DR PDBsum; 6K15; -. DR PDBsum; 6KW3; -. DR PDBsum; 6KW4; -. DR PDBsum; 6KW5; -. DR PDBsum; 6TDA; -. DR PDBsum; 6V8O; -. DR PDBsum; 6V92; -. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Direct protein sequencing; Nucleus; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..483 FT /note="Chromatin structure-remodeling complex protein RSC6" FT /id="PRO_0000097474" FT REGION 142..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 273..309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 148..158 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 171..180 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 30..50 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 74..81 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 238..241 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 249..262 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 269..274 FT /evidence="ECO:0007829|PDB:6V8O" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:6K15" FT HELIX 317..323 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 328..330 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 332..341 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 345..348 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 358..361 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 388..424 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 426..444 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 453..456 FT /evidence="ECO:0007829|PDB:6V8O" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:6V8O" FT TURN 465..467 FT /evidence="ECO:0007829|PDB:6K15" FT HELIX 471..473 FT /evidence="ECO:0007829|PDB:6V8O" FT HELIX 474..479 FT /evidence="ECO:0007829|PDB:6V8O" SQ SEQUENCE 483 AA; 54165 MW; 6A9998BDBC4D24B2 CRC64; MVTQTNPVPV TYPTDAYIPT YLPDDKVSNL ADLKKLIEMD SRLDLYLTRR RLDTSINLPT NTKTKDHPPN KEMLRIYVYN TTESSPRSDS GTPADSGKTT WTLRIEGKLL HESANGKHPF SEFLEGVAVD FKRLKPLGMG KKRKRDSSLS LPLNLQQPEY NDQDSTMGDN DNGEDEDSAE AESREEIVDA LEWNYDENNV VEFDGIDIKR QGKDNLRCSI TIQLRGVDGG KVQYSPNLAT LIGMQTGSVN DAVYSIYKYI LINNLFVTEQ TEAQDGSNDA EDSSNENNNK NGAGDDDGVE GSTPKDKPEL GEVKLDSLLQ KVLDTNAAHL PLMNVVQTVN KLVSPLPPII LDYTIDLSKD TTYGATTLDV DVSHILHQPQ PQPNLQKEEE TDAEDTAKLR EITKLALQLN SSAQKYQFFH ELSLHPRETL THYLWSSKQN ELVLQGDQYF NEDAARTSDI YSNNNNDRSL MGNISLLYSQ GRL //