DOT6_YEAST
ID DOT6_YEAST Reviewed; 670 AA.
AC P40059; D3DLZ5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcriptional regulatory protein DOT6;
DE AltName: Full=Disrupter of telomere silencing protein 6;
DE AltName: Full=PAC-binding factor 2;
GN Name=DOT6; Synonyms=PBF2; OrderedLocusNames=YER088C;
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], AND FUNCTION.
RX PubMed=9755194; DOI=10.1093/genetics/150.2.613;
RA Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E.,
RA Goggin C., Mahowald M., Gottschling D.E.;
RT "Identification of high-copy disruptors of telomeric silencing in
RT Saccharomyces cerevisiae.";
RL Genetics 150:613-632(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, 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 [6]
RP IDENTIFICATION IN THE RPD3(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT "Chromatin Central: towards the comparative proteome by accurate mapping of
RT the yeast proteomic environment.";
RL Genome Biol. 9:R167.1-R167.22(2008).
RN [7]
RP DNA-BINDING.
RX PubMed=19111667; DOI=10.1016/j.molcel.2008.11.020;
RA Badis G., Chan E.T., van Bakel H., Pena-Castillo L., Tillo D., Tsui K.,
RA Carlson C.D., Gossett A.J., Hasinoff M.J., Warren C.L., Gebbia M.,
RA Talukder S., Yang A., Mnaimneh S., Terterov D., Coburn D., Li Yeo A.,
RA Yeo Z.X., Clarke N.D., Lieb J.D., Ansari A.Z., Nislow C., Hughes T.R.;
RT "A library of yeast transcription factor motifs reveals a widespread
RT function for Rsc3 in targeting nucleosome exclusion at promoters.";
RL Mol. Cell 32:878-887(2008).
RN [8]
RP 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 [9]
RP FUNCTION.
RX PubMed=19158363; DOI=10.1101/gr.090233.108;
RA Zhu C., Byers K.J., McCord R.P., Shi Z., Berger M.F., Newburger D.E.,
RA Saulrieta K., Smith Z., Shah M.V., Radhakrishnan M., Philippakis A.A.,
RA Hu Y., De Masi F., Pacek M., Rolfs A., Murthy T.V.S., Labaer J.,
RA Bulyk M.L.;
RT "High-resolution DNA-binding specificity analysis of yeast transcription
RT factors.";
RL Genome Res. 19:556-566(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-247; SER-487;
RP THR-489 AND SER-491, 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: Component of the RPD3 histone deacetylase complex RPD3C(L)
CC responsible for the deacetylation of lysine residues on the N-terminal
CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC gives a tag for epigenetic repression and plays an important role in
CC transcriptional regulation, cell cycle progression and developmental
CC events. DOT6 binds to sequences containing the core CGATG, which
CC resembles the PAC (Polymerase A and C) motif.
CC {ECO:0000269|PubMed:19158363, ECO:0000269|PubMed:9755194}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC CTI6, DEP1, DOT6, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, TOD6;
CC UME1 and UME6. {ECO:0000269|PubMed:19040720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DOT6 family. {ECO:0000305}.
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DR EMBL; U18839; AAB64643.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07749.1; -; Genomic_DNA.
DR PIR; S50591; S50591.
DR RefSeq; NP_011012.3; NM_001178979.3.
DR AlphaFoldDB; P40059; -.
DR SMR; P40059; -.
DR BioGRID; 36833; 110.
DR DIP; DIP-4823N; -.
DR IntAct; P40059; 7.
DR MINT; P40059; -.
DR STRING; 4932.YER088C; -.
DR iPTMnet; P40059; -.
DR MaxQB; P40059; -.
DR PaxDb; P40059; -.
DR PRIDE; P40059; -.
DR EnsemblFungi; YER088C_mRNA; YER088C; YER088C.
DR GeneID; 856822; -.
DR KEGG; sce:YER088C; -.
DR SGD; S000000890; DOT6.
DR VEuPathDB; FungiDB:YER088C; -.
DR eggNOG; ENOG502RXV1; Eukaryota.
DR GeneTree; ENSGT00940000176456; -.
DR HOGENOM; CLU_018984_0_0_1; -.
DR InParanoid; P40059; -.
DR OMA; EVKKMGW; -.
DR BioCyc; YEAST:G3O-30257-MON; -.
DR PRO; PR:P40059; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40059; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..670
FT /note="Transcriptional regulatory protein DOT6"
FT /id="PRO_0000197108"
FT DOMAIN 67..121
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 94..117
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 489
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 670 AA; 73048 MW; 61FD64749653FE78 CRC64;
MSISTSLNSA SIHLSSMDTH PQLHSLTRQP HSSSTAMSKN EAQESSPSLP ASSSSSTSAS
ASASSKNSSK NPSSWDPQDD LLLRHLKEVK KMGWKDISQY FPNRTPNACQ FRWRRLKSGN
LKSNKTALID INTYTGPLKI THGDETANAQ QKPSKKVEEN VLTEDTAEFT TTSSIPIPSR
KTSLPSFHAS MSFSQSPSNV TPTTIVSNAA SSMPFAPPTL PAALPHHPHQ HLHHHPHHKT
LKPRSNSHSF TNSLNQDPIV RSNDEEKYGF IPKVFVRSRR SSFAYPQQVA ITTTPSSPNS
SHVLLSSKSR RGSLANWSRR SSFNVSSNNT SRRSSMILAP NSVSNIFNVN NSGSNTASTS
NTNSRRESVI KKEFQQRLNN LSNSGGPTSN NGPIFPNSYT FMDLPHSSSV SSSSTLHKSK
RGSFSGHSMK SSCNPTNLWS KDEDALLMEN KKRNLSVMEL SILLPQRTEV EIQWRLNALS
SDADMLSPTH SPQKTLSKKT CPRMFKSGST TDDDKGSDKE DVMGDGSNDD DEDNVDPLHR
AKQSSNKTVF SSSSSNISSK DVSPDPIFSP DPADDSSNTS DAGSRCTITS DTSSSAATMN
RTPNSKNPQD IALLNNFRSE AITPRPKPSS TTTSITTETT NNMINHSSST TTTTNNSPLP
SINTIFKDML
