RSC9_YEAST
ID RSC9_YEAST Reviewed; 581 AA.
AC Q03124; D6W0F8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Chromatin structure-remodeling complex subunit RSC9;
DE AltName: Full=RSC complex subunit RSC9;
DE AltName: Full=Remodel the structure of chromatin complex subunit 9;
GN Name=RSC9; OrderedLocusNames=YML127W; ORFNames=YM4987.08;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 PROTEIN SEQUENCE OF 57-73 AND 401-418, FUNCTION, IDENTIFICATION IN THE RSC
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=11931764; DOI=10.1016/s1097-2765(02)00475-6;
RA Damelin M., Simon I., Moy T.I., Wilson B., Komili S., Tempst P., Roth F.P.,
RA Young R.A., Cairns B.R., Silver P.A.;
RT "The genome-wide localization of Rsc9, a component of the RSC chromatin-
RT remodeling complex, changes in response to stress.";
RL Mol. Cell 9:563-573(2002).
RN [4]
RP FUNCTION OF THE RSC COMPLEX, 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 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF
RP THE SWI/SNF COMPLEX.
RX PubMed=12524530; DOI=10.1038/nsb888;
RA Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
RA Peterson C.L.;
RT "Structural analysis of the yeast SWI/SNF chromatin remodeling complex.";
RL Nat. Struct. Biol. 10:141-145(2003).
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 plays a role in
CC transcriptional response to stress. It is involved in both repression
CC and activation of mRNAs regulated by the target of rapamycin (TOR)
CC kinases, and in the synthesis of rRNA. {ECO:0000269|PubMed:10025404,
CC ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:11931764,
CC ECO:0000269|PubMed:12072455, ECO:0000269|PubMed:12183366,
CC ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:8980231}.
CC -!- SUBUNIT: Component of the two forms of the RSC complex composed of at
CC least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30,
CC RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102.
CC The complexes interact with histone and histone variant components of
CC centromeric chromatin. {ECO:0000269|PubMed:11931764}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858,
CC ECO:0000269|PubMed:11931764, 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 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RSC9 family. {ECO:0000305}.
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DR EMBL; Z50178; CAA90556.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09772.1; -; Genomic_DNA.
DR PIR; S58201; S58201.
DR RefSeq; NP_013579.1; NM_001182490.1.
DR PDB; 6K15; EM; 3.40 A; M=1-581.
DR PDB; 6KW3; EM; 7.13 A; M=1-581.
DR PDB; 6KW4; EM; 7.55 A; M=1-581.
DR PDB; 6KW5; EM; 10.13 A; M=1-581.
DR PDB; 6TDA; EM; 15.00 A; N=1-581.
DR PDB; 6V8O; EM; 3.07 A; N=1-581.
DR PDB; 6V92; EM; 20.00 A; N=1-581.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; Q03124; -.
DR SMR; Q03124; -.
DR BioGRID; 35078; 357.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-4517N; -.
DR IntAct; Q03124; 36.
DR MINT; Q03124; -.
DR STRING; 4932.YML127W; -.
DR iPTMnet; Q03124; -.
DR MaxQB; Q03124; -.
DR PaxDb; Q03124; -.
DR PRIDE; Q03124; -.
DR EnsemblFungi; YML127W_mRNA; YML127W; YML127W.
DR GeneID; 854912; -.
DR KEGG; sce:YML127W; -.
DR SGD; S000004596; RSC9.
DR VEuPathDB; FungiDB:YML127W; -.
DR eggNOG; ENOG502QVTM; Eukaryota.
DR HOGENOM; CLU_026029_0_0_1; -.
DR InParanoid; Q03124; -.
DR OMA; SNKAPYM; -.
DR BioCyc; YEAST:G3O-32705-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR PRO; PR:Q03124; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03124; 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:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:SGD.
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:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009303; P:rRNA transcription; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR InterPro; IPR003150; DNA-bd_RFX.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; rRNA processing; Transcription;
KW Transcription regulation.
FT CHAIN 1..581
FT /note="Chromatin structure-remodeling complex subunit RSC9"
FT /id="PRO_0000097475"
FT DNA_BIND 395..476
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 60
FT /note="Y -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6K15"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 182..200
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 212..230
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 525..538
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 547..563
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 572..576
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 581 AA; 65218 MW; 04EA7901486656AB CRC64;
MNSLASNTPL NGTPVSEAPA TSSEPVNMFE TMVANPIKVS RLQSNGVLTG PAANTKSIHY
SLANFNVFQS LPKETARGVD DLTRMEMALL SGIPEEIKWS LKKYLTYSNK APYMISLRTL
PDLLPLFKTF ILPLERIVEG LNKSSICDSK AMDSLQMGLN ALLILRNLAQ DTDSVQILVK
DREIKSFILF ILKKFQCVAT GDNKWQLYEG NATFFNELTH YTLDLMEAIS SYIAPAMKDD
HYFQTLVSIL NYTKDRYMVI SILRSLSRLL VRSKANEESA ADNLDHKTLS LIVSFLLLEC
DSELIIASLD FLYQYILPGS QRITELFKSK ECSLILEATL PNLLSYNIAT PDYHLLQKHK
IRLIKRLKPP APKEPPNLSE DLFQQLFKLN EPLRSTAWLR CCFEPVQEAE FTQISLWRSY
ESKFGQPVRE SGRKLLPAVE FIKNVSNAFN NAAAIVITDP VTGKKRFVIK GIQPRFKALG
IADGERESQV PISALKSKFL NDSKEITPAR QNSIPEVKFP QELSDVSKVA CTFLCLLSND
TDDGAGSAFC QRIRPLVLHK LADIPPLTLA LSEYMENTSG L
