DLS1_YEAST
ID DLS1_YEAST Reviewed; 167 AA.
AC P40366; D6VWB7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein DLS1;
DE AltName: Full=DPB3-like subunit of ISW2 complex 1;
GN Name=DLS1; OrderedLocusNames=YJL065C; ORFNames=HRD167, J1115;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762302; DOI=10.1002/yea.320110108;
RA Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT cerevisiae includes the mitochondrial ribosomal protein L8.";
RL Yeast 11:57-60(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
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 [5]
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 [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.
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 FUNCTION, AND 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-17, 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: Functions as 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. DLS1 is partially required for the ISW2
CC complex chromatin remodeling activity and is not required for its
CC interaction with chromatin. {ECO:0000269|PubMed:11081629,
CC ECO:0000269|PubMed:11238944, ECO:0000269|PubMed:11489850,
CC ECO:0000269|PubMed:11533234, ECO:0000269|PubMed:14673157,
CC ECO:0000269|PubMed:15024052}.
CC -!- SUBUNIT: Component of the ISW2 complex, which at least consists of
CC ISW2, ITC1, DLS1 and DPB4. {ECO:0000269|PubMed:14673157,
CC ECO:0000269|PubMed:15024052}.
CC -!- INTERACTION:
CC P40366; Q04603: DPB4; NbExp=3; IntAct=EBI-25910, EBI-29938;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z34288; CAA84059.1; -; Genomic_DNA.
DR EMBL; Z49340; CAA89355.1; -; Genomic_DNA.
DR EMBL; AY558557; AAS56883.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08733.1; -; Genomic_DNA.
DR PIR; S50808; S50808.
DR RefSeq; NP_012470.1; NM_001181498.1.
DR AlphaFoldDB; P40366; -.
DR SMR; P40366; -.
DR BioGRID; 33689; 125.
DR ComplexPortal; CPX-728; ISW2 chromatin remodeling complex.
DR DIP; DIP-1788N; -.
DR IntAct; P40366; 22.
DR MINT; P40366; -.
DR STRING; 4932.YJL065C; -.
DR iPTMnet; P40366; -.
DR PaxDb; P40366; -.
DR PRIDE; P40366; -.
DR EnsemblFungi; YJL065C_mRNA; YJL065C; YJL065C.
DR GeneID; 853381; -.
DR KEGG; sce:YJL065C; -.
DR SGD; S000003601; DLS1.
DR VEuPathDB; FungiDB:YJL065C; -.
DR eggNOG; KOG1658; Eukaryota.
DR HOGENOM; CLU_1595845_0_0_1; -.
DR InParanoid; P40366; -.
DR OMA; CKKIART; -.
DR BioCyc; YEAST:G3O-31526-MON; -.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-68952; DNA replication initiation.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR PRO; PR:P40366; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40366; protein.
DR GO; GO:0008623; C:CHRAC; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..167
FT /note="Protein DLS1"
FT /id="PRO_0000203057"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 167 AA; 18793 MW; 89B9668F95D64665 CRC64;
MNNETSGKET ASAPLCSPKL PVEKVQRIAK NDPEYMDTSD DAFVATAFAT EFFVQVLTHE
SLHRQQQQQQ QQVPPLPDEL TLSYDDISAA IVHSSDGHLQ FLNDVIPTTK NLRLLVEENR
VRYTTSVMPP NEVYSAYVVN DTAPKPNIVE IDLDNDEDDD EDVTDQE
