RSC8_YEAST
ID RSC8_YEAST Reviewed; 557 AA.
AC P43609; D6VTS0; Q6B289;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Chromatin structure-remodeling complex protein RSC8;
DE AltName: Full=Remodel the structure of chromatin complex subunit 8;
DE AltName: Full=SWI3 homolog;
GN Name=RSC8; Synonyms=SWH3; OrderedLocusNames=YFR037C;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
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 PROTEIN SEQUENCE OF 233-249, FUNCTION OF THE RSC COMPLEX, AND COMPOSITION
RP 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, SELF-ASSOCIATION, AND INTERACTION WITH STH1.
RX PubMed=9121424; DOI=10.1128/mcb.17.4.1768;
RA Treich I., Carlson M.;
RT "Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-
RT related complex with an essential function in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:1768-1775(1997).
RN [7]
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 [8]
RP FUNCTION.
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 [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 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 [14]
RP INTERACTION WITH RSC6.
RX PubMed=9685490; DOI=10.1093/nar/26.16.3739;
RA Treich I., Ho L., Carlson M.;
RT "Direct interaction between Rsc6 and Rsc8/Swh3, two proteins that are
RT conserved in SWI/SNF-related complexes.";
RL Nucleic Acids Res. 26:3739-3745(1998).
RN [15]
RP MUTAGENESIS OF 347-VAL--ILE-351.
RX PubMed=12419236; DOI=10.1016/s1097-2765(02)00634-2;
RA Boyer L.A., Langer M.R., Crowley K.A., Tan S., Denu J.M., Peterson C.L.;
RT "Essential role for the SANT domain in the functioning of multiple
RT chromatin remodeling enzymes.";
RL Mol. Cell 10:935-942(2002).
RN [16]
RP INTERACTION WITH HTL1.
RX PubMed=12684875; DOI=10.1007/s00438-003-0835-1;
RA Lu Y.-M., Lin Y.-R., Tsai A., Hsao Y.-S., Li C.-C., Cheng M.Y.;
RT "Dissecting the pet18 mutation in Saccharomyces cerevisiae: HTL1 encodes a
RT 7-kDa polypeptide that interacts with components of the RSC complex.";
RL Mol. Genet. Genomics 269:321-330(2003).
RN [17]
RP INTERACTION WITH NPL6.
RX PubMed=16204215; DOI=10.1534/genetics.105.047589;
RA Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.;
RT "The RSC chromatin remodeling complex bears an essential fungal-specific
RT protein module with broad functional roles.";
RL Genetics 172:795-809(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, 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. This subunit is essential
CC for mitotic growth and for repression of CHA1 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:8980231,
CC ECO:0000269|PubMed:9121424}.
CC -!- SUBUNIT: Dimerizes via the C-terminal coiled coil. Interacts directly
CC with HTL1, NPL6, RSC6 and the N-terminus of STH1. Component of the two
CC forms of the RSC complex composed of at least either RSC1 or RSC2, and
CC ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9,
CC SFH1, STH1, HTL1 and probably RTT102. The complexes interact with
CC histone and histone variant components of centromeric chromatin.
CC {ECO:0000269|PubMed:12684875, ECO:0000269|PubMed:12697820,
CC ECO:0000269|PubMed:16204215, ECO:0000269|PubMed:9121424,
CC ECO:0000269|PubMed:9685490}.
CC -!- INTERACTION:
CC P43609; Q9URQ5: HTL1; NbExp=3; IntAct=EBI-23005, EBI-8717;
CC P43609; P32832: NPL6; NbExp=7; IntAct=EBI-23005, EBI-12202;
CC P43609; P25632: RSC6; NbExp=12; IntAct=EBI-23005, EBI-21941;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and
CC flanking chromatin. Association with these loci is dependent on STH1.
CC -!- MISCELLANEOUS: Present with 3380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D50617; BAA09276.1; -; Genomic_DNA.
DR EMBL; AY692841; AAT92860.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12480.1; -; Genomic_DNA.
DR PIR; S56292; S56292.
DR RefSeq; NP_116695.3; NM_001180002.3.
DR PDB; 6K15; EM; 3.40 A; D/H=1-557.
DR PDB; 6KW3; EM; 7.13 A; D/H=1-557.
DR PDB; 6KW4; EM; 7.55 A; D/H=1-557.
DR PDB; 6KW5; EM; 10.13 A; D/H=1-557.
DR PDB; 6TDA; EM; 15.00 A; L=1-557.
DR PDB; 6V8O; EM; 3.07 A; I/J/K/L=1-557.
DR PDB; 6V92; EM; 20.00 A; I/J/K/L=1-557.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; P43609; -.
DR SMR; P43609; -.
DR BioGRID; 31195; 510.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-1478N; -.
DR IntAct; P43609; 94.
DR MINT; P43609; -.
DR STRING; 4932.YFR037C; -.
DR iPTMnet; P43609; -.
DR MaxQB; P43609; -.
DR PaxDb; P43609; -.
DR PRIDE; P43609; -.
DR EnsemblFungi; YFR037C_mRNA; YFR037C; YFR037C.
DR GeneID; 850598; -.
DR KEGG; sce:YFR037C; -.
DR SGD; S000001933; RSC8.
DR VEuPathDB; FungiDB:YFR037C; -.
DR eggNOG; KOG1279; Eukaryota.
DR HOGENOM; CLU_004447_3_2_1; -.
DR InParanoid; P43609; -.
DR OMA; CHTCGND; -.
DR BioCyc; YEAST:G3O-30484-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P43609; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43609; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:SGD.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02336; ZZ_RSC8; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR041984; Rsc8/Ssr1/Ssr2_ZZ.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; Direct protein sequencing;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..557
FT /note="Chromatin structure-remodeling complex protein RSC8"
FT /id="PRO_0000197114"
FT DOMAIN 80..177
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 310..362
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 255..309
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..77
FT /evidence="ECO:0000255"
FT COILED 462..494
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 347..351
FT /note="Missing: Loss of function."
FT /evidence="ECO:0000269|PubMed:12419236"
FT CONFLICT 192
FT /note="D -> G (in Ref. 4; AAT92860)"
FT /evidence="ECO:0000305"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 334..341
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 347..355
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 407..489
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 557 AA; 63168 MW; D3D3120397CF0058 CRC64;
MSDTEKDKDV PMVDSHEATE EPPTTSTNTP SFPHLAQEQA KEESATLGAE VAHKKINYEQ
EAQKLEEKAL RFLAKQTHPV IIPSFASWFD ISKIHEIEKR SNPDFFNDSS RFKTPKAYKD
TRNFIINTYR LSPYEYLTIT AVRRNVAMDV ASIVKIHAFL EKWGLINYQI DPRTKPSLIG
PSFTGHFQVV LDTPQGLKPF LPENVIKQEV EGGDGAEPQV KKEFPVNLTI KKNVYDSAQD
FNALQDESRN SRQIHKVYIC HTCGNESINV RYHNLRARDT NLCSRCFQEG HFGANFQSSD
FIRLENNGNS VKKNWSDQEM LLLLEGIEMY EDQWEKIADH VGGHKRVEDC IEKFLSLPIE
DNYIREVVGS TLNGKGGDSR DGSVSGSKLM ECVNDAVQTL LQGDDKLGKV SDKSREISEK
YIEESQAIIQ ELVKLTMEKL ESKFTKLCDL ETQLEMEKLK YVKESEKMLN DRLSLSKQIL
DLNKSLEELN VSKKLVLISE QVDSGIQLVE KDQEGDDEDG NTATGHGVKR VGKEGEEVGE
GDSIAKLQPQ VYKPWSL
