SWC4_YEAST
ID SWC4_YEAST Reviewed; 476 AA.
AC P53201; D6VUD9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=SWR1-complex protein 4;
DE AltName: Full=ESA1-associated factor 2;
GN Name=SWC4; Synonyms=EAF2, GOD1; OrderedLocusNames=YGR002C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH EAF1.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [6]
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 [7]
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 [8]
RP INTERACTION WITH YAF9.
RX PubMed=15302830; DOI=10.1128/ec.3.4.976-983.2004;
RA Bittner C.B., Zeisig D.T., Zeisig B.B., Slany R.K.;
RT "Direct physical and functional interaction of the NuA4 complex components
RT Yaf9p and Swc4p.";
RL Eukaryot. Cell 3:976-983(2004).
RN [9]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15485911; DOI=10.1128/mcb.24.21.9424-9436.2004;
RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H.,
RA Tempst P., Cote J., Cairns B.R.;
RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper
RT gene expression, histone H4 acetylation, and Htz1 replacement near
RT telomeres.";
RL Mol. Cell. Biol. 24:9424-9436(2004).
RN [10]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1, the
RT Swr1 chromatin remodeling complex, and the histone acetyltransferase
RT NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [11]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [12]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645854; DOI=10.1126/science.1090701;
RA Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT remodeling complex.";
RL Science 303:343-348(2004).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC Component of the NuA4 histone acetyltransferase complex which is
CC involved in transcriptional activation of selected genes principally by
CC acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also
CC involved in DNA repair. {ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex composed of
CC at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4,
CC SWC5, SWC7 and SWR1, and perhaps BDF1. Component of the NuA4 histone
CC acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21,
CC SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Interacts with
CC YAF9. Interacts with EAF1. {ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:14690608,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15302830,
CC ECO:0000269|PubMed:15353583, ECO:0000269|PubMed:15485911}.
CC -!- INTERACTION:
CC P53201; Q06337: EAF1; NbExp=4; IntAct=EBI-23061, EBI-35867;
CC P53201; Q12464: RVB2; NbExp=4; IntAct=EBI-23061, EBI-31814;
CC P53201; Q05471: SWR1; NbExp=7; IntAct=EBI-23061, EBI-22102;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SWC4 family. {ECO:0000305}.
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DR EMBL; Z72787; CAA96985.1; -; Genomic_DNA.
DR EMBL; AY692656; AAT92675.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08100.1; -; Genomic_DNA.
DR PIR; S64291; S64291.
DR RefSeq; NP_011516.1; NM_001181131.1.
DR AlphaFoldDB; P53201; -.
DR SMR; P53201; -.
DR BioGRID; 33246; 728.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR DIP; DIP-6510N; -.
DR IntAct; P53201; 35.
DR MINT; P53201; -.
DR STRING; 4932.YGR002C; -.
DR iPTMnet; P53201; -.
DR MaxQB; P53201; -.
DR PaxDb; P53201; -.
DR PRIDE; P53201; -.
DR EnsemblFungi; YGR002C_mRNA; YGR002C; YGR002C.
DR GeneID; 852885; -.
DR KEGG; sce:YGR002C; -.
DR SGD; S000003234; SWC4.
DR VEuPathDB; FungiDB:YGR002C; -.
DR eggNOG; KOG2656; Eukaryota.
DR GeneTree; ENSGT00390000016466; -.
DR HOGENOM; CLU_018539_4_0_1; -.
DR InParanoid; P53201; -.
DR OMA; MYQSSQG; -.
DR BioCyc; YEAST:G3O-30733-MON; -.
DR PRO; PR:P53201; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53201; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0051276; P:chromosome organization; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; IPI:SGD.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR032563; DAMP1_SANT-like.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR027109; Swc4/Dmap1.
DR PANTHER; PTHR12855; PTHR12855; 1.
DR Pfam; PF16282; SANT_DAMP1_like; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Chromatin regulator; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..476
FT /note="SWR1-complex protein 4"
FT /id="PRO_0000072345"
FT DOMAIN 156..209
FT /note="SANT"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 476 AA; 55213 MW; 512CB8DF3171E7A3 CRC64;
MSSSDIFDVL NIKQKSRSPT NGQVSVPSSS AANRPKPQVT GMQRELFNLL GENQPPVVIK
SGNNFKEKML STSKPSPWSF VEFKANNSVT LRHWVKGSKE LIGDTPKESP YSKFNQHLSI
PSFTKEEYEA FMNENEGTQK SVESEKNHNE NFTNEKKDES KNSWSFEEIE YLFNLCKKYD
LRWFLIFDRY SYNNSRTLED LKEKFYYTCR NYFKASDPSN PLLSSLNFSA EKEIERKKYL
QRLLSRSAAE IAEEEALVVE SKKFEMAAKR TLAERESLLR LLDSPHSDQT ITQYLTSQGM
SQLYNALLAD KTRKRKHDLN IPENPWMKQQ QQFAQHRQLQ QLNVKKSEVK ENLSPKKTKR
QRQEMQTALK RKSESAYAEQ LLKDFNSDER KALGVITHGE KLSPGVYLRS TKLSTFKPAL
QNKILAILQE LSLPSRPVMP SFDVMERQEE LLKKINTLID LKKHVDKYEA GMSITK
