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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
 
 
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