SFH1_YEAST
ID SFH1_YEAST Reviewed; 426 AA.
AC Q06168; D6VYW4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Chromatin structure-remodeling complex subunit SFH1;
DE AltName: Full=RSC complex subunit SFH1;
DE AltName: Full=SNF5 homolog 1;
GN Name=SFH1; OrderedLocusNames=YLR321C; ORFNames=L8543.4;
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] {ECO:0000305}
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] {ECO:0000305}
RP FUNCTION 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 [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE RSC COMPLEX, INTERACTION WITH STH1, AND
RP PHOSPHORYLATION.
RX PubMed=9154831; DOI=10.1128/mcb.17.6.3323;
RA Cao Y., Cairns B.R., Kornberg R.D., Laurent B.C.;
RT "Sfh1p, a component of a novel chromatin-remodeling complex, is required
RT for cell cycle progression.";
RL Mol. Cell. Biol. 17:3323-3334(1997).
RN [5] {ECO:0000305}
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 [6] {ECO:0000305}
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 [7] {ECO:0000305}
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 [8] {ECO:0000305}
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 [9] {ECO:0000305}
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 [10] {ECO:0000305}
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, 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).
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 required for cell cycle progression.
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:9154831}.
CC -!- SUBUNIT: Interacts directly with STH1. Component of the two forms of
CC the RSC complex composed of at least either RSC1 or RSC2, and ARP7,
CC ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1,
CC STH1, HTL1 and probably RTT102. The complexes interact with histone and
CC histone variant components of centromeric chromatin.
CC {ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:9154831}.
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 -!- PTM: Phosphorylated in the G1 phase. {ECO:0000269|PubMed:9154831}.
CC -!- MISCELLANEOUS: Present with 3940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
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DR EMBL; U20618; AAB64513.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09630.1; -; Genomic_DNA.
DR PIR; S53399; S53399.
DR RefSeq; NP_013425.1; NM_001182210.1.
DR PDB; 6K15; EM; 3.40 A; G=1-426.
DR PDB; 6KW3; EM; 7.13 A; G=1-426.
DR PDB; 6KW4; EM; 7.55 A; G=1-426.
DR PDB; 6KW5; EM; 10.13 A; G=1-426.
DR PDB; 6TDA; EM; 15.00 A; K=1-426.
DR PDB; 6V8O; EM; 3.07 A; Q=1-426.
DR PDB; 6V92; EM; 20.00 A; Q=1-426.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; Q06168; -.
DR SMR; Q06168; -.
DR BioGRID; 31585; 138.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-1898N; -.
DR IntAct; Q06168; 34.
DR MINT; Q06168; -.
DR STRING; 4932.YLR321C; -.
DR iPTMnet; Q06168; -.
DR MaxQB; Q06168; -.
DR PaxDb; Q06168; -.
DR PRIDE; Q06168; -.
DR EnsemblFungi; YLR321C_mRNA; YLR321C; YLR321C.
DR GeneID; 851032; -.
DR KEGG; sce:YLR321C; -.
DR SGD; S000004313; SFH1.
DR VEuPathDB; FungiDB:YLR321C; -.
DR eggNOG; KOG1649; Eukaryota.
DR GeneTree; ENSGT00440000038585; -.
DR HOGENOM; CLU_014421_4_0_1; -.
DR InParanoid; Q06168; -.
DR OMA; NFHNRIR; -.
DR BioCyc; YEAST:G3O-32405-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q06168; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06168; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0031055; P:chromatin remodeling at centromere; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IGI:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IGI:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR InterPro; IPR017393; Sfh1/SNF5.
DR InterPro; IPR006939; SNF5.
DR Pfam; PF04855; SNF5; 2.
DR PIRSF; PIRSF038126; SWI_SNF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..426
FT /note="Chromatin structure-remodeling complex subunit SFH1"
FT /id="PRO_0000205962"
FT REGION 201..242
FT /note="Interaction with STH1"
FT /evidence="ECO:0000269|PubMed:9154831"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 278..301
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 307..318
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 324..344
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:6K15"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:6V8O"
SQ SEQUENCE 426 AA; 48777 MW; C8D6F151249E8479 CRC64;
MSHQNQLIPQ AYISNFHNRL TNEDDGIPIF TMAQQTRQHK RAKVVNYAEY DNDLFDEFNM
NGSNFNNADT HYKDNAVSHE NTPALTNGVT MDGSEYNVLE NMNGADSIIS NNKYDAGSNM
VVESLSGLNS NNNASNGPSN KAQAQDIGNA VLPDLQDQHH NPFNILRYPK IRDTFINGKV
VSPYRLNTDQ ETKANANSGE AIMIPITLDI EHMGHTIKDQ FLWNYNDDSI SPEEFASIYC
KDLDMTSATL QTQIANIIKE QLKDLENIAA TEIMSDLHVI INLTCNLQDR FFEDNFQWNL
NDKSLTPERF ATSIVQDLGL TREFIPLISQ SLHETILKIK KDWVDGHLIQ DHVPNDAAFG
YLSGIRLDID ELGSNWCPRV EILTKEEIQK REIEKERNLR RLKRETDRLS RRGRRRLDDL
ETTMRM
