RSC1_YEAST
ID RSC1_YEAST Reviewed; 928 AA.
AC P53236; D6VUJ1; Q45U30;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Chromatin structure-remodeling complex subunit RSC1;
DE AltName: Full=RSC complex subunit RSC1;
DE AltName: Full=Remodel the structure of chromatin complex subunit 1;
GN Name=RSC1; OrderedLocusNames=YGR056W;
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 [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 511-526 AND 759-776, COMPOSITION OF THE RSC COMPLEX,
RP AND MUTAGENESIS OF 228-GLY--PRO-230.
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 [5]
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 [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 FUNCTION.
RX PubMed=12702296; DOI=10.1111/j.1567-1364.2002.tb00073.x;
RA Yukawa M., Koyama H., Miyahara K., Tsuchiya E.;
RT "Functional differences between RSC1 and RSC2, components of a for growth
RT essential chromatin-remodeling complex of Saccharomyces cerevisiae, during
RT the sporulation process.";
RL FEMS Yeast Res. 2:87-91(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, 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 [14]
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 involved in
CC meiotic sporulation through regulating IME2 expression.
CC {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:12702296,
CC 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.
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 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RSC1 family. {ECO:0000305}.
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DR EMBL; DQ115391; AAZ22469.1; -; Genomic_DNA.
DR EMBL; Z72841; CAA97057.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08152.1; -; Genomic_DNA.
DR PIR; S64350; S64350.
DR RefSeq; NP_011570.1; NM_001181185.1.
DR AlphaFoldDB; P53236; -.
DR SMR; P53236; -.
DR BioGRID; 33301; 288.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-984N; -.
DR IntAct; P53236; 24.
DR MINT; P53236; -.
DR STRING; 4932.YGR056W; -.
DR iPTMnet; P53236; -.
DR MaxQB; P53236; -.
DR PaxDb; P53236; -.
DR PRIDE; P53236; -.
DR EnsemblFungi; YGR056W_mRNA; YGR056W; YGR056W.
DR GeneID; 852947; -.
DR KEGG; sce:YGR056W; -.
DR SGD; S000003288; RSC1.
DR VEuPathDB; FungiDB:YGR056W; -.
DR eggNOG; KOG1827; Eukaryota.
DR GeneTree; ENSGT00940000176545; -.
DR HOGENOM; CLU_007728_2_0_1; -.
DR InParanoid; P53236; -.
DR OMA; EYPDYYI; -.
DR BioCyc; YEAST:G3O-30773-MON; -.
DR PRO; PR:P53236; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53236; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISS:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IPI:SGD.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IMP:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR CDD; cd05521; Bromo_Rsc1_2_I; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR Gene3D; 2.30.30.490; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR027180; RSC1/2/4.
DR InterPro; IPR035700; Rsc1/Rsc2_Bromo.
DR PANTHER; PTHR16062; PTHR16062; 1.
DR PANTHER; PTHR16062:SF19; PTHR16062:SF19; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Bromodomain; Chromatin regulator; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..928
FT /note="Chromatin structure-remodeling complex subunit RSC1"
FT /id="PRO_0000211211"
FT DOMAIN 27..95
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 255..325
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 368..486
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 558..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..900
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 228..230
FT /note="GRP->AAA: Loss of function."
FT /evidence="ECO:0000269|PubMed:10619019"
FT CONFLICT 112
FT /note="N -> H (in Ref. 1; AAZ22469)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="T -> S (in Ref. 1; AAZ22469)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="D -> H (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="T -> S (in Ref. 1; AAZ22469)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="D -> E (in Ref. 1; AAZ22469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 106669 MW; EFF80922FC08EC27 CRC64;
MVEQDNGFLQ KLLKTQYDAV FHLKDENGIE IYPIFNVLPP KKEYPDYYII IRNPISLNTL
KKRLPHYTSP QDFVNDFAQI PWNAMTYNAK DSVIYKYAIL LESFIKGKIV HNIRKHYPEV
TYPSLGRIPE IFAESMQPSD LSSNPINTQE NDEKAGLNPE MKMAFAKLDS SITERKPTNQ
DYRMQQKNSP AFPTHSASIT PQPLASPTPV VNYANITSAH PKTHVRRGRP PVIDLPYVLR
IKNILKMMRR EVDQNNKTLT LCFEKLPDRN EEPTYYSVIT DPICLMDIRK KVKSRKYRNF
HTFEEDFQLM LTNFKLYYSQ DQSNIIRAQL LEKNFNRLVR IELSKPDEDY LPEGELRYPL
DDVEINDEKY QIGDWVLLHN PNDINKPIVG QIFRLWSTTD GNKWLNACWY FRPEQTVHRV
DRLFYKNEVM KTGQYRDHPI QDIKGKCYVI HFTRFQRGDP STKVNGPQFV CEFRYNESDK
VFNKIRTWKA CLPEELRDQD EPTIPVNGRK FFKYPSPIAD LLPANATLND KVPEPTEGAP
TAPPLVGAVY LGPKLERDDL GEYSTSDDCP RYIIRPNDPP EEGKIDYETG TIITDTLTTS
SMPRVNSSST IRLPTLKQTK SIPSSNFRSS SNTPLLHQNF NQTSNFLKLE NMNNSSHNLL
SHPSVPKFQS PSLLEQSSRS KYHSAKKQTQ LSSTAPKKPA SKSFTLSSMI NTLTAHTSKY
NFNHIVIEAP GAFVVPVPME KNIRTIQSTE RFSRSNLKNA QNLGNTAIND INTANEQIIW
FKGPGVKITE RVIDSGNDLV RVPLNRWFCK NKRRKLDYED IEEDVMEPPN DFSEDMIANI
FNPPPSLNLD MDLNLSPSSN NSSNFMDLST IASGDNDGKE CDTAEESEDE NEDTEDEHEI
EDIPTTSAFG LNSSAEYLAF RLREFNKL
