ISW2_YEAST
ID ISW2_YEAST Reviewed; 1120 AA.
AC Q08773; D6W303;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2;
DE EC=3.6.4.-;
DE AltName: Full=Imitation switch protein 2;
GN Name=ISW2; OrderedLocusNames=YOR304W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 IDENTIFICATION IN THE ISW2 COMPLEX, FUNCTION, AND MUTAGENESIS OF LYS-215.
RX PubMed=10090725; DOI=10.1101/gad.13.6.686;
RA Tsukiyama T., Palmer J., Landel C.C., Shiloach J., Wu C.;
RT "Characterization of the imitation switch subfamily of ATP-dependent
RT chromatin-remodeling factors in Saccharomyces cerevisiae.";
RL Genes Dev. 13:686-697(1999).
RN [4]
RP FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=11081629; DOI=10.1016/s0092-8674(00)00134-3;
RA Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., Tsukiyama T.;
RT "The Isw2 chromatin remodeling complex represses early meiotic genes upon
RT recruitment by Ume6p.";
RL Cell 103:423-433(2000).
RN [5]
RP FUNCTION.
RX PubMed=11238381; DOI=10.1101/gad.190301;
RA Kent N.A., Karabetsou N., Politis P.K., Mellor J.;
RT "In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p.";
RL Genes Dev. 15:619-626(2001).
RN [6]
RP FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=11489850; DOI=10.1128/jb.183.17.4985-4993.2001;
RA Sugiyama M., Nikawa J.;
RT "The Saccharomyces cerevisiae Isw2p-Itc1p complex represses INO1 expression
RT and maintains cell morphology.";
RL J. Bacteriol. 183:4985-4993(2001).
RN [7]
RP FUNCTION OF THE ISW2 COMPLEX, AND INTERACTION WITH ITC1.
RX PubMed=11238944; DOI=10.1128/mcb.21.6.2098-2106.2001;
RA Gelbart M.E., Rechsteiner T., Richmond T.J., Tsukiyama T.;
RT "Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays:
RT analyses using recombinant yeast histones and immobilized templates.";
RL Mol. Cell. Biol. 21:2098-2106(2001).
RN [8]
RP FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=11533234; DOI=10.1128/mcb.21.19.6450-6460.2001;
RA Fazzio T.G., Kooperberg C., Goldmark J.P., Neal C., Basom R., Delrow J.,
RA Tsukiyama T.;
RT "Widespread collaboration of Isw2 and Sin3-Rpd3 chromatin remodeling
RT complexes in transcriptional repression.";
RL Mol. Cell. Biol. 21:6450-6460(2001).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION IN THE ISW2 COMPLEX, AND FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=14673157; DOI=10.1128/mcb.24.1.217-227.2004;
RA Iida T., Araki H.;
RT "Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC
RT for epigenetic inheritance of telomere position effect in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 24:217-227(2004).
RN [12]
RP IDENTIFICATION IN THE ISW2 COMPLEX.
RX PubMed=15024052; DOI=10.1128/mcb.24.7.2605-2613.2004;
RA McConnell A.D., Gelbart M.E., Tsukiyama T.;
RT "Histone fold protein Dls1p is required for Isw2-dependent chromatin
RT remodeling in vivo.";
RL Mol. Cell. Biol. 24:2605-2613(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; THR-1079 AND SER-1082,
RP AND IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19; SER-831; THR-1079
RP AND SER-1082, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Catalytic component of the ISW2 complex, which acts in
CC remodeling the chromatin by catalyzing an ATP-dependent alteration in
CC the structure of nucleosomal DNA. The ISW2 complex is involved in
CC coordinating transcriptional repression and in inheritance of telomeric
CC silencing. It is involved in repression of MAT a-specific genes, INO1,
CC and early meiotic genes during mitotic growth dependent upon
CC transcription factor UME6 and in a parallel pathway to the RPD3-SIN3
CC histone deacetylase complex. {ECO:0000269|PubMed:10090725,
CC ECO:0000269|PubMed:11081629, ECO:0000269|PubMed:11238381,
CC ECO:0000269|PubMed:11238944, ECO:0000269|PubMed:11489850,
CC ECO:0000269|PubMed:11533234, ECO:0000269|PubMed:14673157}.
CC -!- SUBUNIT: Component of the ISW2 complex, which at least consists of
CC ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ITC1.
CC {ECO:0000269|PubMed:10090725, ECO:0000269|PubMed:14673157,
CC ECO:0000269|PubMed:15024052}.
CC -!- INTERACTION:
CC Q08773; P53125: ITC1; NbExp=2; IntAct=EBI-31118, EBI-23967;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
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DR EMBL; Z75212; CAA99622.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11069.1; -; Genomic_DNA.
DR PIR; S67208; S67208.
DR RefSeq; NP_014948.1; NM_001183724.1.
DR AlphaFoldDB; Q08773; -.
DR SMR; Q08773; -.
DR BioGRID; 34692; 343.
DR ComplexPortal; CPX-728; ISW2 chromatin remodeling complex.
DR ComplexPortal; CPX-734; ISW2 chromatin remodeling complex variant 2.
DR DIP; DIP-6603N; -.
DR IntAct; Q08773; 40.
DR MINT; Q08773; -.
DR STRING; 4932.YOR304W; -.
DR iPTMnet; Q08773; -.
DR MaxQB; Q08773; -.
DR PaxDb; Q08773; -.
DR PRIDE; Q08773; -.
DR EnsemblFungi; YOR304W_mRNA; YOR304W; YOR304W.
DR GeneID; 854480; -.
DR KEGG; sce:YOR304W; -.
DR SGD; S000005831; ISW2.
DR VEuPathDB; FungiDB:YOR304W; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000176603; -.
DR HOGENOM; CLU_000315_0_0_1; -.
DR InParanoid; Q08773; -.
DR OMA; IHDWQFF; -.
DR BioCyc; YEAST:G3O-33788-MON; -.
DR PRO; PR:Q08773; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08773; protein.
DR GO; GO:0008623; C:CHRAC; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005880; C:nuclear microtubule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0015616; F:DNA translocase activity; IDA:SGD.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0060195; P:negative regulation of antisense RNA transcription; IGI:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IGI:SGD.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1120
FT /note="ISWI chromatin-remodeling complex ATPase ISW2"
FT /id="PRO_0000240453"
FT DOMAIN 196..361
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 494..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 886..938
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 312..315
FT /note="DEAH box"
FT COMPBIAS 17..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1079
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 215
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:10090725"
SQ SEQUENCE 1120 AA; 130327 MW; F71007D7B25C9348 CRC64;
MTTQQEEQRS DTKNSKSESP SEVLVDTLDS KSNGSSDDDN IGQSEELSDK EIYTVEDRPP
EYWAQRKKKF VLDVDPKYAK QKDKSDTYKR FKYLLGVTDL FRHFIGIKAK HDKNIQKLLK
QLDSDANKLS KSHSTVSSSS RHHRKTEKEE DAELMADEEE EIVDTYQEDI FVSESPSFVK
SGKLRDYQVQ GLNWLISLHE NKLSGILADE MGLGKTLQTI SFLGYLRYVK QIEGPFLIIV
PKSTLDNWRR EFLKWTPNVN VLVLHGDKDT RADIVRNIIL EARFDVLITS YEMVIREKNA
LKRLAWQYIV IDEAHRIKNE QSALSQIIRL FYSKNRLLIT GTPLQNNLHE LWALLNFLLP
DIFGDSELFD EWFEQNNSEQ DQEIVIQQLH SVLNPFLLRR VKADVEKSLL PKIETNVYVG
MTDMQIQWYK SLLEKDIDAV NGAVGKREGK TRLLNIVMQL RKCCNHPYLF EGAEPGPPYT
TDEHLIFNSG KMIILDKLLK RLKEKGSRVL IFSQMSRLLD ILEDYCYFRD FEYCRIDGST
SHEERIEAID EYNKPNSEKF VFLLTTRAGG LGINLVTADT VILFDSDWNP QADLQAMDRA
HRIGQKKQVH VYRFVTENAI EEKVIERAAQ KLRLDQLVIQ QGTGKKTASL GNSKDDLLDM
IQFGAKNMFE KKASKVTVDA DIDDILKKGE QKTQELNAKY QSLGLDDLQK FNGIENQSAY
EWNGKSFQKK SNDKVVEWIN PSRRERRREQ TTYSVDDYYK EIIGGGSKSA SKQTPQPKAP
RAPKVIHGQD FQFFPKELDA LQEKEQLYFK KKVNYKVTSY DITGDIRNEG SDAEEEEGEY
KNAANTEGHK GHEELKRRIE EEQEKINSAP DFTQEDELRK QELISKAFTN WNKRDFMAFI
NACAKYGRDD MENIKKSIDS KTPEEVEVYA KIFWERLKEI NGWEKYLHNV ELGEKKNEKL
KFQETLLRQK IEQCKHPLHE LIIQYPPNNA RRTYNTLEDK FLLLAVNKYG LRADKLYEKL
KQEIMMSDLF TFDWFIKTRT VHELSKRVHT LLTLIVREYE QPDANKKKRS RTSATREDTP
LSQNESTRAS TVPNLPTTMV TNQKDTNDHV DKRTKIDQEA
