RSC4_YEAST
ID RSC4_YEAST Reviewed; 625 AA.
AC Q02206; D6VX74; Q6B1F7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Chromatin structure-remodeling complex subunit RSC4;
DE AltName: Full=RSC complex subunit RSC4;
DE AltName: Full=Remodel the structure of chromatin complex subunit 4;
GN Name=RSC4; OrderedLocusNames=YKR008W; ORFNames=YK107;
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=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 390.
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 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 [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 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP 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.
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: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 ECO:0000269|PubMed:14562095}. Note=Localizes to centromeric and
CC flanking chromatin. Association with these loci is dependent on STH1.
CC -!- MISCELLANEOUS: Present with 8570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X65124; CAA46244.1; -; Genomic_DNA.
DR EMBL; Z28233; CAA82078.1; -; Genomic_DNA.
DR EMBL; AY693123; AAT93142.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09164.2; -; Genomic_DNA.
DR PIR; S34035; S34035.
DR RefSeq; NP_012933.4; NM_001179798.4.
DR PDB; 2R0S; X-ray; 1.80 A; A=36-320.
DR PDB; 2R0V; X-ray; 2.35 A; A/B/C=1-340.
DR PDB; 2R0Y; X-ray; 1.75 A; A=36-340.
DR PDB; 2R10; X-ray; 2.20 A; A/B=1-340.
DR PDB; 6K15; EM; 3.40 A; X=1-625.
DR PDB; 6KW3; EM; 7.13 A; X=1-625.
DR PDB; 6KW4; EM; 7.55 A; X=1-625.
DR PDB; 6KW5; EM; 10.13 A; X=1-625.
DR PDB; 6TDA; EM; 15.00 A; R=1-625.
DR PDB; 6V8O; EM; 3.07 A; H=1-625.
DR PDB; 6V92; EM; 20.00 A; H=1-625.
DR PDBsum; 2R0S; -.
DR PDBsum; 2R0V; -.
DR PDBsum; 2R0Y; -.
DR PDBsum; 2R10; -.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; Q02206; -.
DR SMR; Q02206; -.
DR BioGRID; 34140; 327.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-6639N; -.
DR IntAct; Q02206; 124.
DR MINT; Q02206; -.
DR STRING; 4932.YKR008W; -.
DR iPTMnet; Q02206; -.
DR MaxQB; Q02206; -.
DR PaxDb; Q02206; -.
DR PRIDE; Q02206; -.
DR EnsemblFungi; YKR008W_mRNA; YKR008W; YKR008W.
DR GeneID; 853877; -.
DR KEGG; sce:YKR008W; -.
DR SGD; S000001716; RSC4.
DR VEuPathDB; FungiDB:YKR008W; -.
DR eggNOG; KOG1827; Eukaryota.
DR GeneTree; ENSGT00390000003017; -.
DR HOGENOM; CLU_441492_0_0_1; -.
DR InParanoid; Q02206; -.
DR OMA; DYDFNHY; -.
DR BioCyc; YEAST:G3O-31986-MON; -.
DR EvolutionaryTrace; Q02206; -.
DR PRO; PR:Q02206; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02206; 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:0070577; F:lysine-acetylated histone binding; 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:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR Gene3D; 1.20.920.10; -; 2.
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 PANTHER; PTHR16062; PTHR16062; 1.
DR PANTHER; PTHR16062:SF13; PTHR16062:SF13; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bromodomain; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..625
FT /note="Chromatin structure-remodeling complex subunit RSC4"
FT /id="PRO_0000211213"
FT DOMAIN 72..141
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 205..275
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 390
FT /note="K -> I (in Ref. 1; CAA46244 and 2; CAA82078)"
FT /evidence="ECO:0000305"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2R0Y"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:2R0Y"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2R10"
FT HELIX 139..159
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2R0Y"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2R0S"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2R0Y"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 273..291
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:2R0Y"
FT TURN 313..318
FT /evidence="ECO:0007829|PDB:2R0Y"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 449..458
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 460..467
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 508..516
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 522..530
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 597..607
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 614..623
FT /evidence="ECO:0007829|PDB:6V8O"
SQ 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
