RSC6_YEAST
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 03-AUG-2022, entry version 163.
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=7; IntAct=EBI-21941, EBI-36549;
CC P25632; P43609: RSC8; NbExp=12; 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}.
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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 PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; P25632; -.
DR SMR; P25632; -.
DR BioGRID; 31032; 402.
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 IntAct; P25632; 50.
DR MINT; P25632; -.
DR STRING; 4932.YCR052W; -.
DR iPTMnet; P25632; -.
DR MaxQB; P25632; -.
DR PaxDb; P25632; -.
DR PRIDE; P25632; -.
DR EnsemblFungi; YCR052W_mRNA; YCR052W; YCR052W.
DR GeneID; 850419; -.
DR KEGG; sce:YCR052W; -.
DR SGD; S000000648; RSC6.
DR VEuPathDB; FungiDB:YCR052W; -.
DR eggNOG; KOG2570; Eukaryota.
DR GeneTree; ENSGT00940000176438; -.
DR HOGENOM; CLU_032070_0_0_1; -.
DR InParanoid; P25632; -.
DR OMA; LRCSITI; -.
DR BioCyc; YEAST:G3O-29361-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P25632; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25632; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR SUPFAM; SSF47592; SSF47592; 1.
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 149..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Polar 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 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
