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Chromatin structure-remodeling complex subunit RSC4 (RSC complex subunit RSC4) (Remodel the structure of chromatin complex subunit 4)

 RSC4_YEAST              Reviewed;         625 AA.
Q02206; D6VX74; Q6B1F7;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 2.
18-JUL-2018, entry version 173.
RecName: Full=Chromatin structure-remodeling complex subunit RSC4;
AltName: Full=RSC complex subunit RSC4;
AltName: Full=Remodel the structure of chromatin complex subunit 4;
Name=RSC4; OrderedLocusNames=YKR008W; ORFNames=YK107;
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=ATCC 204508 / S288c;
PubMed=1441752; DOI=10.1002/yea.320080908;
Duesterhoeft A., Philippsen P.;
"DNA sequencing and analysis of a 24.7 kb segment encompassing
centromere CEN11 of Saccharomyces cerevisiae reveals nine previously
unknown open reading frames.";
Yeast 8:749-759(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 390.
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[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]
COMPOSITION OF THE RSC COMPLEX.
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).
[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]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND 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. {ECO:0000269|PubMed:10025404,
ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:12072455,
ECO:0000269|PubMed:12183366, ECO:0000269|PubMed:12697820,
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:
Self; NbExp=3; IntAct=EBI-16204, EBI-16204;
Q12406:ARP7; NbExp=10; IntAct=EBI-16204, EBI-2962;
Q05123:ARP9; NbExp=9; IntAct=EBI-16204, EBI-2972;
Q9URQ5:HTL1; NbExp=3; IntAct=EBI-16204, EBI-8717;
P32832:NPL6; NbExp=12; IntAct=EBI-16204, EBI-12202;
P53236:RSC1; NbExp=8; IntAct=EBI-16204, EBI-16192;
Q06488:RSC2; NbExp=14; IntAct=EBI-16204, EBI-16198;
Q06639:RSC3; NbExp=8; IntAct=EBI-16204, EBI-22058;
Q07979:RSC58; NbExp=20; IntAct=EBI-16204, EBI-36549;
P25632:RSC6; NbExp=13; IntAct=EBI-16204, EBI-21941;
P43609:RSC8; NbExp=37; IntAct=EBI-16204, EBI-23005;
Q03124:RSC9; NbExp=12; IntAct=EBI-16204, EBI-27977;
P53330:RTT102; NbExp=6; IntAct=EBI-16204, EBI-23637;
Q06168:SFH1; NbExp=11; IntAct=EBI-16204, EBI-35813;
P32597:STH1; NbExp=31; IntAct=EBI-16204, EBI-18410;
P34160:STO1; NbExp=8; IntAct=EBI-16204, EBI-745;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12697820,
ECO:0000269|PubMed:14562095}. Note=Localizes to centromeric and
flanking chromatin. Association with these loci is dependent on
STH1.
-!- MISCELLANEOUS: Present with 8570 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X65124; CAA46244.1; -; Genomic_DNA.
EMBL; Z28233; CAA82078.1; -; Genomic_DNA.
EMBL; AY693123; AAT93142.1; -; Genomic_DNA.
EMBL; BK006944; DAA09164.2; -; Genomic_DNA.
PIR; S34035; S34035.
RefSeq; NP_012933.4; NM_001179798.4.
PDB; 2R0S; X-ray; 1.80 A; A=36-320.
PDB; 2R0V; X-ray; 2.35 A; A/B/C=1-340.
PDB; 2R0Y; X-ray; 1.75 A; A=36-340.
PDB; 2R10; X-ray; 2.20 A; A/B=1-340.
PDBsum; 2R0S; -.
PDBsum; 2R0V; -.
PDBsum; 2R0Y; -.
PDBsum; 2R10; -.
ProteinModelPortal; Q02206; -.
SMR; Q02206; -.
BioGrid; 34140; 319.
ComplexPortal; CPX-1888; RSC complex variant RSC2.
ComplexPortal; CPX-1889; RSC complex variant RSC1.
DIP; DIP-6639N; -.
IntAct; Q02206; 142.
MINT; Q02206; -.
STRING; 4932.YKR008W; -.
iPTMnet; Q02206; -.
MaxQB; Q02206; -.
PaxDb; Q02206; -.
PRIDE; Q02206; -.
EnsemblFungi; YKR008W; YKR008W; YKR008W.
GeneID; 853877; -.
KEGG; sce:YKR008W; -.
EuPathDB; FungiDB:YKR008W; -.
SGD; S000001716; RSC4.
HOGENOM; HOG000142075; -.
InParanoid; Q02206; -.
KO; K11759; -.
OMA; SQNENMY; -.
OrthoDB; EOG092C3W5G; -.
BioCyc; YEAST:G3O-31986-MONOMER; -.
EvolutionaryTrace; Q02206; -.
PRO; PR:Q02206; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR037382; Rsc/polybromo.
PANTHER; PTHR16062; PTHR16062; 1.
Pfam; PF00439; Bromodomain; 2.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS00633; BROMODOMAIN_1; 2.
PROSITE; PS50014; BROMODOMAIN_2; 2.
1: Evidence at protein level;
3D-structure; Bromodomain; Chromatin regulator; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 625 Chromatin structure-remodeling complex
subunit RSC4.
/FTId=PRO_0000211213.
DOMAIN 72 141 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 205 275 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CONFLICT 390 390 K -> I (in Ref. 1; CAA46244 and 2;
CAA82078). {ECO:0000305}.
HELIX 47 50 {ECO:0000244|PDB:2R0Y}.
HELIX 58 72 {ECO:0000244|PDB:2R0Y}.
HELIX 74 77 {ECO:0000244|PDB:2R0Y}.
HELIX 78 80 {ECO:0000244|PDB:2R0Y}.
TURN 86 88 {ECO:0000244|PDB:2R0Y}.
HELIX 90 95 {ECO:0000244|PDB:2R0Y}.
HELIX 102 107 {ECO:0000244|PDB:2R0Y}.
HELIX 115 133 {ECO:0000244|PDB:2R0Y}.
STRAND 136 138 {ECO:0000244|PDB:2R10}.
HELIX 139 159 {ECO:0000244|PDB:2R0Y}.
HELIX 160 163 {ECO:0000244|PDB:2R0Y}.
HELIX 169 184 {ECO:0000244|PDB:2R0Y}.
HELIX 187 195 {ECO:0000244|PDB:2R0Y}.
HELIX 196 198 {ECO:0000244|PDB:2R0Y}.
STRAND 205 207 {ECO:0000244|PDB:2R0S}.
HELIX 211 213 {ECO:0000244|PDB:2R0Y}.
TURN 219 221 {ECO:0000244|PDB:2R0Y}.
HELIX 223 228 {ECO:0000244|PDB:2R0Y}.
HELIX 235 244 {ECO:0000244|PDB:2R0Y}.
HELIX 250 267 {ECO:0000244|PDB:2R0Y}.
HELIX 273 291 {ECO:0000244|PDB:2R0Y}.
HELIX 293 302 {ECO:0000244|PDB:2R0Y}.
TURN 313 318 {ECO:0000244|PDB:2R0Y}.
SEQUENCE 625 AA; 72291 MW; B25614F50FA0D108 CRC64;
MVVKKRKLAT EAGGSDERPK YLPGKHPKNQ EKTPHVDYNA PLNPKSELFL DDWHIPKFNR
FISFTLDVLI DKYKDIFKDF IKLPSRKFHP QYYYKIQQPM SINEIKSRDY EYEDGPSNFL
LDVELLTKNC QAYNEYDSLI VKNSMQVVML IEFEVLKAKN LKRNYLINSE VKAKLLHYLN
KLVDATEKKI NQALLGASSP KNLDDKVKLS EPFMELVDKD ELPEYYEIVH SPMALSIVKQ
NLEIGQYSKI YDFIIDMLLV FQNAHIFNDP SALIYKDATT LTNYFNYLIQ KEFFPELQDL
NERGEINLEF DKFEFENYLA IGGGGPAAAG ALAISALDND IEPESNREDL IDQADYDFNH
FEGLGNGYNR SLLTEDYLLN PNNFKKLIAK PETVQSEVKN ERSTTSDIEK TNSLESEHLK
IPKYNVIKSM QKEMQSLSEQ HTMEYKPYKL IQQIYIFSSK NLYSQATKPL LGSRPSCNQN
WVEYIFNGNE LSQNENAFSF MLQPMQTFLT LQSHLTSSLK DTETLLTINK EPVKSRTSNV
NSNLSQPQQQ ENDVIGNDTK QDIENLTIGG GNNNDIVGND NDKRNNITEI FDIRLSEGLN
HLMFRCEDKI SHETEFMNFW INVLP


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