RSC2_YEAST
ID RSC2_YEAST Reviewed; 889 AA.
AC Q06488; D6VYZ5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Chromatin structure-remodeling complex subunit RSC2;
DE AltName: Full=RSC complex subunit RSC2;
DE AltName: Full=Remodel the structure of chromatin complex subunit 2;
GN Name=RSC2; OrderedLocusNames=YLR357W; ORFNames=L9638.1;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF GLU-468 AND
RP GLY-601.
RX PubMed=12024034; DOI=10.1128/mcb.22.12.4218-4229.2002;
RA Wong M.C.V.L., Scott-Drew S.R.S., Hayes M.J., Howard P.J., Murray J.A.H.;
RT "RSC2, encoding a component of the RSC nucleosome remodeling complex, is
RT essential for 2 micrometer plasmid maintenance in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 22:4218-4229(2002).
RN [4]
RP PROTEIN SEQUENCE OF 241-253, AND 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 [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 DISRUPTION PHENOTYPE.
RX PubMed=16079223; DOI=10.1534/genetics.105.046938;
RA Jambunathan N., Martinez A.W., Robert E.C., Agochukwu N.B., Ibos M.E.,
RA Dugas S.L., Donze D.;
RT "Multiple bromodomain genes are involved in restricting the spread of
RT heterochromatic silencing at the Saccharomyces cerevisiae HMR-tRNA
RT boundary.";
RL Genetics 171:913-922(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, 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 TYR-612 AND SER-682, AND
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, and is also
CC essential for 2-micron plasmid maintenance and for normal REP1 protein
CC localization. {ECO:0000269|PubMed:10025404,
CC ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:12024034,
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 -!- DISRUPTION PHENOTYPE: Heterochromatin spreading downstream of the
CC silent mating-type locus HMR. {ECO:0000269|PubMed:16079223}.
CC -!- MISCELLANEOUS: Present with 2330 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; U19102; AAB67747.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09661.1; -; Genomic_DNA.
DR PIR; S51465; S51465.
DR RefSeq; NP_013461.1; NM_001182246.1.
DR PDB; 4BB7; X-ray; 2.40 A; A/B/C/D=401-641.
DR PDB; 6K15; EM; 3.40 A; L=1-889.
DR PDB; 6KW3; EM; 7.13 A; L=1-889.
DR PDB; 6KW4; EM; 7.55 A; L=1-889.
DR PDB; 6KW5; EM; 10.13 A; L=1-889.
DR PDB; 6V8O; EM; 3.07 A; F=1-889.
DR PDB; 6V92; EM; 20.00 A; F=1-889.
DR PDBsum; 4BB7; -.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; Q06488; -.
DR SMR; Q06488; -.
DR BioGRID; 31619; 292.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR DIP; DIP-863N; -.
DR IntAct; Q06488; 53.
DR MINT; Q06488; -.
DR STRING; 4932.YLR357W; -.
DR iPTMnet; Q06488; -.
DR MaxQB; Q06488; -.
DR PaxDb; Q06488; -.
DR PRIDE; Q06488; -.
DR EnsemblFungi; YLR357W_mRNA; YLR357W; YLR357W.
DR GeneID; 851071; -.
DR KEGG; sce:YLR357W; -.
DR SGD; S000004349; RSC2.
DR VEuPathDB; FungiDB:YLR357W; -.
DR eggNOG; KOG1827; Eukaryota.
DR GeneTree; ENSGT00940000176545; -.
DR HOGENOM; CLU_007728_2_0_1; -.
DR InParanoid; Q06488; -.
DR OMA; FFKYESP; -.
DR BioCyc; YEAST:G3O-32429-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q06488; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06488; protein.
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; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IGI:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; 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:0006276; P:plasmid maintenance; IMP:UniProtKB.
DR GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:SGD.
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 GO; GO:0070914; P:UV-damage excision repair; IMP: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 3D-structure; Bromodomain; Chromatin regulator; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..889
FT /note="Chromatin structure-remodeling complex subunit RSC2"
FT /id="PRO_0000211212"
FT DOMAIN 35..103
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 295..365
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 408..526
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 151..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 612
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 468
FT /note="E->K: In dpm3; defective in plasmid maintenance."
FT /evidence="ECO:0000269|PubMed:12024034"
FT MUTAGEN 601
FT /note="G->E: In dpm18; defective in plasmid maintenance."
FT /evidence="ECO:0000269|PubMed:12024034"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 428..437
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:4BB7"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 470..479
FT /evidence="ECO:0007829|PDB:4BB7"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:4BB7"
FT HELIX 492..497
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:4BB7"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:4BB7"
FT HELIX 528..531
FT /evidence="ECO:0007829|PDB:4BB7"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 547..555
FT /evidence="ECO:0007829|PDB:4BB7"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:4BB7"
FT TURN 627..630
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:4BB7"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 809..811
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 863..866
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 872..880
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 889 AA; 102300 MW; 7867866FD973F188 CRC64;
MMPDDNSNSS TQNSSALYKD LRKEYESLFT LKEDSGLEIS PIFNVLPPKK DYPDYYAVIK
NPVSFNTLKK RIPHYTDAQQ FMNDVVQIPW NAKTYNTRDS GIYKYALVLE KYLKDTIYPN
LKEKYPQLVY PDLGPLPDEP GYEEFQQKLR EKAEEVARAN AARAESSSSM NSTEAARRLR
KTRTSVKRES EPGTDTNNDE DYEATDMDID NPKDADFPDL IRKPLININP YTRKPLRDNR
STTPSHSGTP QPLGPRHRQV SRTQVKRGRP PIIDLPYIQR MKNVMKVLKK EVLDSGIGLT
DLFERLPDRH RDANYYIMIA NPISLQDINK KVKTRRYKTF QEFQNDFNLM LTNFRISHRG
DPESIKISNI LEKTFTSLAR FELSKPDRSF IPEGELRYPL DEVIVNNISY HVGDWALLRN
QNDPQKPIVG QIFRLWKTPD GKQWLNACWY YRPEQTVHRV DRLFYKNEVM KTGQYRDHLV
SNLVGKCYVI HFTRYQRGNP DMKLEGPLFV CEFRYNESDK IFNKIRTWKA CLPEEIRDLD
EATIPVNGRK FFKYPSPIRH LLPANATPHD RVPEPTMGSP DAPPLVGAVY MRPKMQRDDL
GEYATSDDCP RYIIRPNDSP EEGQVDIETG TITTNTPTAN ALPKTGYSSS KLSSLRYNRS
SMSLENQNAI GQQQIPLSRV GSPGAGGPLT VQGLKQHQLQ RLQQQQHQYQ QQKRSQASRY
NIPTIIDDLT SQASRGNLGN IMIDAASSFV LPISITKNVD VLQRTDLHSQ TKRSGREEMF
PWKKTKGEIL WFRGPSVIVN ERIINSGDPH LSLPLNRWFT TNKKRKLEYE EVEETMEDVT
GKDKDDDGLE PDVENEKESL PGPFVLGLRP SAKFTAHRLS MLRPPSSSS
