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Chromatin structure-remodeling complex subunit RSC1 (RSC complex subunit RSC1) (Remodel the structure of chromatin complex subunit 1)

 RSC1_YEAST              Reviewed;         928 AA.
P53236; D6VUJ1; Q45U30;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
18-JUL-2018, entry version 162.
RecName: Full=Chromatin structure-remodeling complex subunit RSC1;
AltName: Full=RSC complex subunit RSC1;
AltName: Full=Remodel the structure of chromatin complex subunit 1;
Name=RSC1; OrderedLocusNames=YGR056W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SK1;
PubMed=16273108; DOI=10.1038/ng1674;
Deutschbauer A.M., Davis R.W.;
"Quantitative trait loci mapped to single-nucleotide resolution in
yeast.";
Nat. Genet. 37:1333-1340(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 511-526 AND 759-776, COMPOSITION OF THE RSC
COMPLEX, AND MUTAGENESIS OF 228-GLY--PRO-230.
PubMed=10619019; DOI=10.1016/S1097-2765(00)80382-2;
Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P.,
Kornberg R.D., Winston F.;
"Two functionally distinct forms of the RSC nucleosome-remodeling
complex, containing essential AT hook, BAH, and bromodomains.";
Mol. Cell 4:715-723(1999).
[5]
FUNCTION OF THE RSC COMPLEX, AND COMPOSITION OF THE RSC COMPLEX.
PubMed=8980231; DOI=10.1016/S0092-8674(00)81820-6;
Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L.,
Erdjument-Bromage H., Tempst P., Du J., Laurent B.C., Kornberg R.D.;
"RSC, an essential, abundant chromatin-remodeling complex.";
Cell 87:1249-1260(1996).
[6]
FUNCTION OF THE RSC COMPLEX.
PubMed=10025404; DOI=10.1016/S0092-8674(00)80551-6;
Lorch Y., Zhang M., Kornberg R.D.;
"Histone octamer transfer by a chromatin-remodeling complex.";
Cell 96:389-392(1999).
[7]
FUNCTION OF THE RSC COMPLEX.
PubMed=10329629; DOI=10.1093/emboj/18.10.2836;
Moreira J.M.A., Holmberg S.;
"Transcriptional repression of the yeast CHA1 gene requires the
chromatin-remodeling complex RSC.";
EMBO J. 18:2836-2844(1999).
[8]
FUNCTION.
PubMed=12702296; DOI=10.1111/j.1567-1364.2002.tb00073.x;
Yukawa M., Koyama H., Miyahara K., Tsuchiya E.;
"Functional differences between RSC1 and RSC2, components of a for
growth essential chromatin-remodeling complex of Saccharomyces
cerevisiae, during the sporulation process.";
FEMS Yeast Res. 2:87-91(2002).
[9]
FUNCTION OF THE RSC COMPLEX.
PubMed=12183366; DOI=10.1101/gad.995002;
Saha A., Wittmeyer J., Cairns B.R.;
"Chromatin remodeling by RSC involves ATP-dependent DNA
translocation.";
Genes Dev. 16:2120-2134(2002).
[10]
FUNCTION OF THE RSC COMPLEX.
PubMed=12072455;
Chai B., Hsu J.-M., Du J., Laurent B.C.;
"Yeast RSC function is required for organization of the cellular
cytoskeleton via an alternative PKC1 pathway.";
Genetics 161:575-584(2002).
[11]
FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION OF
THE RSC COMPLEX WITH HISTONES.
PubMed=12697820; DOI=10.1128/MCB.23.9.3202-3215.2003;
Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.;
"The yeast RSC chromatin-remodeling complex is required for
kinetochore function in chromosome segregation.";
Mol. Cell. Biol. 23:3202-3215(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10025404, ECO:0000269|PubMed:10329629,
ECO:0000269|PubMed:12072455, ECO:0000269|PubMed:12183366,
ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:12702296,
ECO:0000269|PubMed:8980231}.
-!- SUBUNIT: Component of the two forms of the RSC complex composed of
at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3,
RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and
probably RTT102. The complexes interact with histone and histone
variant components of centromeric chromatin.
-!- INTERACTION:
Q12406:ARP7; NbExp=7; IntAct=EBI-16192, EBI-2962;
Q05123:ARP9; NbExp=4; IntAct=EBI-16192, EBI-2972;
P32832:NPL6; NbExp=5; IntAct=EBI-16192, EBI-12202;
Q02206:RSC4; NbExp=8; IntAct=EBI-16192, EBI-16204;
Q07979:RSC58; NbExp=12; IntAct=EBI-16192, EBI-36549;
P43609:RSC8; NbExp=10; IntAct=EBI-16192, EBI-23005;
P53330:RTT102; NbExp=2; IntAct=EBI-16192, EBI-23637;
Q06168:SFH1; NbExp=6; IntAct=EBI-16192, EBI-35813;
P32597:STH1; NbExp=10; IntAct=EBI-16192, EBI-18410;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12697820}.
Note=Localizes to centromeric and flanking chromatin. Association
with these loci is dependent on STH1.
-!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RSC1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; DQ115391; AAZ22469.1; -; Genomic_DNA.
EMBL; Z72841; CAA97057.1; -; Genomic_DNA.
EMBL; BK006941; DAA08152.1; -; Genomic_DNA.
PIR; S64350; S64350.
RefSeq; NP_011570.1; NM_001181185.1.
ProteinModelPortal; P53236; -.
SMR; P53236; -.
BioGrid; 33301; 282.
ComplexPortal; CPX-1889; RSC complex variant RSC1.
DIP; DIP-984N; -.
IntAct; P53236; 33.
MINT; P53236; -.
STRING; 4932.YGR056W; -.
iPTMnet; P53236; -.
MaxQB; P53236; -.
PaxDb; P53236; -.
PRIDE; P53236; -.
EnsemblFungi; YGR056W; YGR056W; YGR056W.
GeneID; 852947; -.
KEGG; sce:YGR056W; -.
EuPathDB; FungiDB:YGR056W; -.
SGD; S000003288; RSC1.
GeneTree; ENSGT00390000003017; -.
HOGENOM; HOG000247903; -.
InParanoid; P53236; -.
KO; K11756; -.
OMA; NACWYFR; -.
OrthoDB; EOG092C1S4Z; -.
BioCyc; YEAST:G3O-30773-MONOMER; -.
PRO; PR:P53236; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:InterPro.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISS:SGD.
GO; GO:0006302; P:double-strand break repair; IMP:SGD.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IPI:SGD.
GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
CDD; cd05521; Bromo_Rsc1_2_I; 1.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR001025; BAH_dom.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR037382; Rsc/polybromo.
InterPro; IPR027180; RSC1/RSC2.
InterPro; IPR035700; Rsc1/Rsc2_Bromo.
PANTHER; PTHR16062; PTHR16062; 1.
PANTHER; PTHR16062:SF15; PTHR16062:SF15; 1.
Pfam; PF01426; BAH; 1.
Pfam; PF00439; Bromodomain; 2.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00439; BAH; 1.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS51038; BAH; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 2.
1: Evidence at protein level;
Bromodomain; Chromatin regulator; Complete proteome;
Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Sporulation; Transcription;
Transcription regulation.
CHAIN 1 928 Chromatin structure-remodeling complex
subunit RSC1.
/FTId=PRO_0000211211.
DOMAIN 27 95 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 255 325 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 368 486 BAH. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 228 230 GRP->AAA: Loss of function.
{ECO:0000269|PubMed:10619019}.
CONFLICT 112 112 N -> H (in Ref. 1; AAZ22469).
{ECO:0000305}.
CONFLICT 302 302 T -> S (in Ref. 1; AAZ22469).
{ECO:0000305}.
CONFLICT 520 520 D -> H (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 712 712 T -> S (in Ref. 1; AAZ22469).
{ECO:0000305}.
CONFLICT 820 820 D -> E (in Ref. 1; AAZ22469).
{ECO:0000305}.
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


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