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Protein

ISWI chromatin-remodeling complex ATPase ISW2

Gene

ISW2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. THe ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi209 – 2168ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • centromeric DNA binding Source: SGD
  • chromatin binding Source: SGD
  • DNA translocase activity Source: SGD
  • helicase activity Source: UniProtKB-KW
  • single-stranded DNA binding Source: SGD

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: InterPro
  • chromatin remodeling Source: SGD
  • chromatin silencing at rDNA Source: SGD
  • chromatin silencing at telomere Source: SGD
  • negative regulation of antisense RNA transcription Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter by pheromones Source: SGD
  • nucleosome positioning Source: SGD
  • termination of RNA polymerase II transcription Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33788-MONOMER.
ReactomeiR-SCE-5696395. Formation of Incision Complex in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
ISWI chromatin-remodeling complex ATPase ISW2 (EC:3.6.4.-)
Alternative name(s):
Imitation switch protein 2
Gene namesi
Name:ISW2
Ordered Locus Names:YOR304W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR304W.
SGDiS000005831. ISW2.

Subcellular locationi

GO - Cellular componenti

  • CHRAC Source: SGD
  • chromosome, telomeric region Source: GOC
  • nucleus Source: SGD
  • NURF complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151K → A: Abolishes ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11201120ISWI chromatin-remodeling complex ATPase ISW2PRO_0000240453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei831 – 8311PhosphoserineCombined sources
Modified residuei1079 – 10791PhosphothreonineCombined sources
Modified residuei1082 – 10821PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08773.
PRIDEiQ08773.

PTM databases

iPTMnetiQ08773.

Interactioni

Subunit structurei

Component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ITC1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITC1P531253EBI-31118,EBI-23967

Protein-protein interaction databases

BioGridi34692. 237 interactions.
DIPiDIP-6603N.
IntActiQ08773. 36 interactions.
MINTiMINT-469536.

Structurei

3D structure databases

ProteinModelPortaliQ08773.
SMRiQ08773. Positions 172-710, 777-1058.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini196 – 361166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini494 – 645152Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini886 – 93853SANTPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi312 – 3154DEAH box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 SANT domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00830000128416.
HOGENOMiHOG000192862.
InParanoidiQ08773.
KOiK11654.
OMAiMAFINAC.
OrthoDBiEOG7M98QM.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR029915. ISWI.
IPR015194. ISWI_HAND-dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR015195. SLIDE.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF691. PTHR10799:SF691. 6 hits.
PfamiPF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF101224. SSF101224. 2 hits.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08773-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTQQEEQRS DTKNSKSESP SEVLVDTLDS KSNGSSDDDN IGQSEELSDK
60 70 80 90 100
EIYTVEDRPP EYWAQRKKKF VLDVDPKYAK QKDKSDTYKR FKYLLGVTDL
110 120 130 140 150
FRHFIGIKAK HDKNIQKLLK QLDSDANKLS KSHSTVSSSS RHHRKTEKEE
160 170 180 190 200
DAELMADEEE EIVDTYQEDI FVSESPSFVK SGKLRDYQVQ GLNWLISLHE
210 220 230 240 250
NKLSGILADE MGLGKTLQTI SFLGYLRYVK QIEGPFLIIV PKSTLDNWRR
260 270 280 290 300
EFLKWTPNVN VLVLHGDKDT RADIVRNIIL EARFDVLITS YEMVIREKNA
310 320 330 340 350
LKRLAWQYIV IDEAHRIKNE QSALSQIIRL FYSKNRLLIT GTPLQNNLHE
360 370 380 390 400
LWALLNFLLP DIFGDSELFD EWFEQNNSEQ DQEIVIQQLH SVLNPFLLRR
410 420 430 440 450
VKADVEKSLL PKIETNVYVG MTDMQIQWYK SLLEKDIDAV NGAVGKREGK
460 470 480 490 500
TRLLNIVMQL RKCCNHPYLF EGAEPGPPYT TDEHLIFNSG KMIILDKLLK
510 520 530 540 550
RLKEKGSRVL IFSQMSRLLD ILEDYCYFRD FEYCRIDGST SHEERIEAID
560 570 580 590 600
EYNKPNSEKF VFLLTTRAGG LGINLVTADT VILFDSDWNP QADLQAMDRA
610 620 630 640 650
HRIGQKKQVH VYRFVTENAI EEKVIERAAQ KLRLDQLVIQ QGTGKKTASL
660 670 680 690 700
GNSKDDLLDM IQFGAKNMFE KKASKVTVDA DIDDILKKGE QKTQELNAKY
710 720 730 740 750
QSLGLDDLQK FNGIENQSAY EWNGKSFQKK SNDKVVEWIN PSRRERRREQ
760 770 780 790 800
TTYSVDDYYK EIIGGGSKSA SKQTPQPKAP RAPKVIHGQD FQFFPKELDA
810 820 830 840 850
LQEKEQLYFK KKVNYKVTSY DITGDIRNEG SDAEEEEGEY KNAANTEGHK
860 870 880 890 900
GHEELKRRIE EEQEKINSAP DFTQEDELRK QELISKAFTN WNKRDFMAFI
910 920 930 940 950
NACAKYGRDD MENIKKSIDS KTPEEVEVYA KIFWERLKEI NGWEKYLHNV
960 970 980 990 1000
ELGEKKNEKL KFQETLLRQK IEQCKHPLHE LIIQYPPNNA RRTYNTLEDK
1010 1020 1030 1040 1050
FLLLAVNKYG LRADKLYEKL KQEIMMSDLF TFDWFIKTRT VHELSKRVHT
1060 1070 1080 1090 1100
LLTLIVREYE QPDANKKKRS RTSATREDTP LSQNESTRAS TVPNLPTTMV
1110 1120
TNQKDTNDHV DKRTKIDQEA
Length:1,120
Mass (Da):130,327
Last modified:November 1, 1996 - v1
Checksum:iF71007D7B25C9348
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75212 Genomic DNA. Translation: CAA99622.1.
BK006948 Genomic DNA. Translation: DAA11069.1.
PIRiS67208.
RefSeqiNP_014948.1. NM_001183724.1.

Genome annotation databases

EnsemblFungiiYOR304W; YOR304W; YOR304W.
GeneIDi854480.
KEGGisce:YOR304W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75212 Genomic DNA. Translation: CAA99622.1.
BK006948 Genomic DNA. Translation: DAA11069.1.
PIRiS67208.
RefSeqiNP_014948.1. NM_001183724.1.

3D structure databases

ProteinModelPortaliQ08773.
SMRiQ08773. Positions 172-710, 777-1058.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34692. 237 interactions.
DIPiDIP-6603N.
IntActiQ08773. 36 interactions.
MINTiMINT-469536.

PTM databases

iPTMnetiQ08773.

Proteomic databases

MaxQBiQ08773.
PRIDEiQ08773.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR304W; YOR304W; YOR304W.
GeneIDi854480.
KEGGisce:YOR304W.

Organism-specific databases

EuPathDBiFungiDB:YOR304W.
SGDiS000005831. ISW2.

Phylogenomic databases

GeneTreeiENSGT00830000128416.
HOGENOMiHOG000192862.
InParanoidiQ08773.
KOiK11654.
OMAiMAFINAC.
OrthoDBiEOG7M98QM.

Enzyme and pathway databases

BioCyciYEAST:G3O-33788-MONOMER.
ReactomeiR-SCE-5696395. Formation of Incision Complex in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.

Miscellaneous databases

PROiQ08773.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR029915. ISWI.
IPR015194. ISWI_HAND-dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR015195. SLIDE.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF691. PTHR10799:SF691. 6 hits.
PfamiPF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF101224. SSF101224. 2 hits.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae."
    Tsukiyama T., Palmer J., Landel C.C., Shiloach J., Wu C.
    Genes Dev. 13:686-697(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ISW2 COMPLEX, FUNCTION, MUTAGENESIS OF LYS-215.
  4. "The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p."
    Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., Tsukiyama T.
    Cell 103:423-433(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX.
  5. "In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p."
    Kent N.A., Karabetsou N., Politis P.K., Mellor J.
    Genes Dev. 15:619-626(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The Saccharomyces cerevisiae Isw2p-Itc1p complex represses INO1 expression and maintains cell morphology."
    Sugiyama M., Nikawa J.
    J. Bacteriol. 183:4985-4993(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX.
  7. "Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays: analyses using recombinant yeast histones and immobilized templates."
    Gelbart M.E., Rechsteiner T., Richmond T.J., Tsukiyama T.
    Mol. Cell. Biol. 21:2098-2106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX, INTERACTION WITH ITC1.
  8. "Widespread collaboration of Isw2 and Sin3-Rpd3 chromatin remodeling complexes in transcriptional repression."
    Fazzio T.G., Kooperberg C., Goldmark J.P., Neal C., Basom R., Delrow J., Tsukiyama T.
    Mol. Cell. Biol. 21:6450-6460(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC for epigenetic inheritance of telomere position effect in Saccharomyces cerevisiae."
    Iida T., Araki H.
    Mol. Cell. Biol. 24:217-227(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ISW2 COMPLEX, FUNCTION OF THE ISW2 COMPLEX.
  12. "Histone fold protein Dls1p is required for Isw2-dependent chromatin remodeling in vivo."
    McConnell A.D., Gelbart M.E., Tsukiyama T.
    Mol. Cell. Biol. 24:2605-2613(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ISW2 COMPLEX.
  13. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; THR-1079 AND SER-1082, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19; SER-831; THR-1079 AND SER-1082, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiISW2_YEAST
AccessioniPrimary (citable) accession number: Q08773
Secondary accession number(s): D6W303
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1520 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.