UME6_YEAST
ID UME6_YEAST Reviewed; 836 AA.
AC P39001; D6VSI8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Transcriptional regulatory protein UME6;
DE AltName: Full=Negative transcriptional regulator of IME2;
DE AltName: Full=Regulator of inducer of meiosis protein 16;
DE AltName: Full=Unscheduled meiotic gene expression protein 6;
GN Name=UME6; Synonyms=CAR80, CARGR1, NIM2, RIM16; OrderedLocusNames=YDR207C;
GN ORFNames=YD8142.04C;
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=Sigma 1278B;
RA Smart W.C., Park H.-D., Cooper T.G.;
RT "Sequence of the UME6/CAR80 gene from Saccharomyces cerevisiae.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7926768; DOI=10.1101/gad.8.7.796;
RA Strich R., Surosky R.T., Steber C.M., Messenguy F., Dubois E.,
RA Easton Esposito R.;
RT "UME6 is a key regulator of nitrogen repression and meiotic development.";
RL Genes Dev. 8:796-810(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RA Kumeno A.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=2690066; DOI=10.1073/pnas.86.24.10018;
RA Strich R., Slater M.R., Easton Esposito R.;
RT "Identification of negative regulatory genes that govern the expression of
RT early meiotic genes in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:10018-10022(1989).
RN [7]
RP FUNCTION.
RX PubMed=1592244; DOI=10.1093/genetics/131.1.65;
RA Mitchell A.P., Bowdish K.S.;
RT "Selection for early meiotic mutants in yeast.";
RL Genetics 131:65-72(1992).
RN [8]
RP FUNCTION.
RX PubMed=1579492; DOI=10.1093/nar/20.8.1909;
RA Park H.-D., Luche R.M., Cooper T.G.;
RT "The yeast UME6 gene product is required for transcriptional repression
RT mediated by the CAR1 URS1 repressor binding site.";
RL Nucleic Acids Res. 20:1909-1915(1992).
RN [9]
RP FUNCTION.
RX PubMed=7760793; DOI=10.1128/mcb.15.6.2955;
RA Bowdish K.S., Yuan H.E., Mitchell A.P.;
RT "Positive control of yeast meiotic genes by the negative regulator UME6.";
RL Mol. Cell. Biol. 15:2955-2961(1995).
RN [10]
RP FUNCTION.
RX PubMed=8618927; DOI=10.1073/pnas.92.26.12490;
RA Steber C.M., Easton Esposito R.;
RT "UME6 is a central component of a developmental regulatory switch
RT controlling meiosis-specific gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12490-12494(1995).
RN [11]
RP DOMAIN, AND DNA-BINDING.
RX PubMed=8528081; DOI=10.1002/pro.5560040918;
RA Anderson S.F., Steber C.M., Easton Esposito R., Coleman J.E.;
RT "UME6, a negative regulator of meiosis in Saccharomyces cerevisiae,
RT contains a C-terminal Zn2Cys6 binuclear cluster that binds the URS1 DNA
RT sequence in a zinc-dependent manner.";
RL Protein Sci. 4:1832-1843(1995).
RN [12]
RP FUNCTION, AND INTERACTION WITH IME1.
RX PubMed=8628320; DOI=10.1128/mcb.16.5.2518;
RA Rubin-Bejerano I., Mandel S., Robzyk K., Kassir Y.;
RT "Induction of meiosis in Saccharomyces cerevisiae depends on conversion of
RT the transcriptional represssor Ume6 to a positive regulator by its
RT regulated association with the transcriptional activator Ime1.";
RL Mol. Cell. Biol. 16:2518-2526(1996).
RN [13]
RP FUNCTION.
RX PubMed=8614637; DOI=10.1093/nar/24.7.1322;
RA Jackson J.C., Lopes J.M.;
RT "The yeast UME6 gene is required for both negative and positive
RT transcriptional regulation of phospholipid biosynthetic gene expression.";
RL Nucleic Acids Res. 24:1322-1329(1996).
RN [14]
RP FUNCTION, DOMAIN, AND INTERACTION WITH SIN3.
RX PubMed=9150136; DOI=10.1016/s0092-8674(00)80217-2;
RA Kadosh D., Struhl K.;
RT "Repression by Ume6 involves recruitment of a complex containing Sin3
RT corepressor and Rpd3 histone deacetylase to target promoters.";
RL Cell 89:365-371(1997).
RN [15]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9343383; DOI=10.1128/mcb.17.11.6223;
RA Sweet D.H., Jang Y.K., Sancar G.B.;
RT "Role of UME6 in transcriptional regulation of a DNA repair gene in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:6223-6235(1997).
RN [16]
RP FUNCTION, INTERACTION WITH RIM11 AND IME1, PHOSPHORYLATION, AND MUTAGENESIS
RP OF THR-99 AND 99-THR--SER-109.
RX PubMed=9372955; DOI=10.1128/mcb.17.12.7230;
RA Malathi K., Xiao Y., Mitchell A.P.;
RT "Interaction of yeast repressor-activator protein Ume6p with glycogen
RT synthase kinase 3 homolog Rim11p.";
RL Mol. Cell. Biol. 17:7230-7236(1997).
RN [17]
RP FUNCTION.
RX PubMed=9710596; DOI=10.1128/mcb.18.9.5121;
RA Kadosh D., Struhl K.;
RT "Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex
RT generates a highly localized domain of repressed chromatin in vivo.";
RL Mol. Cell. Biol. 18:5121-5127(1998).
RN [18]
RP FUNCTION.
RX PubMed=9572144; DOI=10.1038/33952;
RA Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M.;
RT "Transcriptional repression by UME6 involves deacetylation of lysine 5 of
RT histone H4 by RPD3.";
RL Nature 392:831-835(1998).
RN [19]
RP FUNCTION, AND DNA-BINDING.
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 [20]
RP FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-99; THR-103 AND SER-107, AND
RP INTERACTION WITH MCK1.
RX PubMed=10891485; DOI=10.1128/mcb.20.15.5447-5453.2000;
RA Xiao Y., Mitchell A.P.;
RT "Shared roles of yeast glycogen synthase kinase 3 family members in
RT nitrogen-responsive phosphorylation of meiotic regulator Ume6p.";
RL Mol. Cell. Biol. 20:5447-5453(2000).
RN [21]
RP FUNCTION.
RX PubMed=10931932; DOI=10.1093/nar/28.16.3160;
RA Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr.,
RA Lopes J.M.;
RT "Combinatorial regulation of phospholipid biosynthetic gene expression by
RT the UME6, SIN3 and RPD3 genes.";
RL Nucleic Acids Res. 28:3160-3167(2000).
RN [22]
RP FUNCTION, INTERACTION WITH SIN3 AND TEA1, AND MUTAGENESIS OF ALA-523;
RP ALA-524; ALA-525; VAL-526; LEU-527; SER-528; MET-530 AND LYS-635.
RX PubMed=11238941; DOI=10.1128/mcb.21.6.2057-2069.2001;
RA Washburn B.K., Easton Esposito R.;
RT "Identification of the Sin3-binding site in Ume6 defines a two-step process
RT for conversion of Ume6 from a transcriptional repressor to an activator in
RT yeast.";
RL Mol. Cell. Biol. 21:2057-2069(2001).
RN [23]
RP FUNCTION.
RX PubMed=12370439; DOI=10.1073/pnas.202495299;
RA Williams R.M., Primig M., Washburn B.K., Winzeler E.A., Bellis M.,
RA Sarrauste de Menthiere C., Davis R.W., Easton Esposito R.;
RT "The Ume6 regulon coordinates metabolic and meiotic gene expression in
RT yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13431-13436(2002).
RN [24]
RP FUNCTION.
RX PubMed=12693549; DOI=10.1093/dnares/10.1.1;
RA Aburatani S., Tashiro K., Savoie C.J., Nishizawa M., Hayashi K., Ito Y.,
RA Muta S., Yamamoto K., Ogawa M., Enomoto A., Masaki M., Watanabe S.,
RA Maki Y., Takahashi Y., Eguchi Y., Sakaki Y., Kuhara S.;
RT "Discovery of novel transcription control relationships with gene
RT regulatory networks generated from multiple-disruption full genome
RT expression libraries.";
RL DNA Res. 10:1-8(2003).
RN [25]
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 [26]
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 [27]
RP FUNCTION.
RX PubMed=12799429; DOI=10.1093/nar/gkg425;
RA Shimizu M., Takahashi K., Lamb T.M., Shindo H., Mitchell A.P.;
RT "Yeast Ume6p repressor permits activator binding but restricts TBP binding
RT at the HOP1 promoter.";
RL Nucleic Acids Res. 31:3033-3037(2003).
RN [28]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA Washburn M.P., Workman J.L.;
RT "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT the Rpd3L complex.";
RL Biochim. Biophys. Acta 1731:77-87(2005).
RN [29]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15837806; DOI=10.1101/gr.3578205;
RA Doniger S.W., Huh J., Fay J.C.;
RT "Identification of functional transcription factor binding sites using
RT closely related Saccharomyces species.";
RL Genome Res. 15:701-709(2005).
RN [30]
RP IDENTIFICATION BY 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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-150, AND
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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-141; SER-150;
RP SER-228; SER-316; SER-318 AND SER-645, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 RPD3C(L) histone deacetylase complex (HDAC)
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. Binds to the URS1 site (5'-AGCCGCCGA-3') and recruits the RPD3
CC histone deacetylase complex to the promoters to negatively regulate the
CC expression of many genes including CAR1 (arginase), several required
CC for sporulation, mating type switching, inositol metabolism, and
CC oxidative carbon metabolism. Recruits also the ISW2 chromatin
CC remodeling complex to promoters in a second gene repression pathway.
CC Associates with the master regulator of meiosis IME1 in order to
CC activate the expression of meiosis genes. Has both a positive and
CC negative role in regulating phospholipid biosynthesis.
CC {ECO:0000269|PubMed:10891485, ECO:0000269|PubMed:10931932,
CC ECO:0000269|PubMed:11081629, ECO:0000269|PubMed:11238941,
CC ECO:0000269|PubMed:12370439, ECO:0000269|PubMed:12693549,
CC ECO:0000269|PubMed:12799429, ECO:0000269|PubMed:1579492,
CC ECO:0000269|PubMed:15837806, ECO:0000269|PubMed:1592244,
CC ECO:0000269|PubMed:2690066, ECO:0000269|PubMed:7760793,
CC ECO:0000269|PubMed:7926768, ECO:0000269|PubMed:8614637,
CC ECO:0000269|PubMed:8618927, ECO:0000269|PubMed:8628320,
CC ECO:0000269|PubMed:9150136, ECO:0000269|PubMed:9343383,
CC ECO:0000269|PubMed:9372955, ECO:0000269|PubMed:9572144,
CC ECO:0000269|PubMed:9710596}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC Interacts with RIM11, MCK1 and IME1. {ECO:0000269|PubMed:10891485,
CC ECO:0000269|PubMed:11238941, ECO:0000269|PubMed:16314178,
CC ECO:0000269|PubMed:8628320, ECO:0000269|PubMed:9150136,
CC ECO:0000269|PubMed:9372955}.
CC -!- INTERACTION:
CC P39001; P21190: IME1; NbExp=3; IntAct=EBI-20086, EBI-9199;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by RIM11 and MCK1. {ECO:0000269|PubMed:10891485,
CC ECO:0000269|PubMed:9372955}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L32186; AAA34471.1; -; Genomic_DNA.
DR EMBL; L24539; AAC14472.1; -; Unassigned_DNA.
DR EMBL; D23663; BAA04890.1; -; Genomic_DNA.
DR EMBL; Z68194; CAA92346.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12048.1; -; Genomic_DNA.
DR PIR; S61570; S61570.
DR RefSeq; NP_010493.1; NM_001180515.1.
DR PDB; 6XAW; X-ray; 1.84 A; B=500-543.
DR PDBsum; 6XAW; -.
DR AlphaFoldDB; P39001; -.
DR SMR; P39001; -.
DR BioGRID; 32257; 798.
DR ComplexPortal; CPX-1415; IME1-UME6 transcription activation complex.
DR DIP; DIP-959N; -.
DR ELM; P39001; -.
DR IntAct; P39001; 11.
DR MINT; P39001; -.
DR STRING; 4932.YDR207C; -.
DR iPTMnet; P39001; -.
DR MaxQB; P39001; -.
DR PaxDb; P39001; -.
DR PRIDE; P39001; -.
DR EnsemblFungi; YDR207C_mRNA; YDR207C; YDR207C.
DR GeneID; 851788; -.
DR KEGG; sce:YDR207C; -.
DR SGD; S000002615; UME6.
DR VEuPathDB; FungiDB:YDR207C; -.
DR eggNOG; ENOG502RX7Y; Eukaryota.
DR HOGENOM; CLU_022046_0_0_1; -.
DR InParanoid; P39001; -.
DR OMA; DPKENDT; -.
DR BioCyc; YEAST:G3O-29791-MON; -.
DR PRO; PR:P39001; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39001; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD.
DR GO; GO:0034389; P:lipid droplet organization; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0010674; P:negative regulation of transcription from RNA polymerase II promoter involved in meiotic cell cycle; IMP:SGD.
DR GO; GO:0001081; P:nitrogen catabolite repression of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0010673; P:positive regulation of transcription from RNA polymerase II promoter involved in meiotic cell cycle; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IDA:ComplexPortal.
DR GO; GO:0009847; P:spore germination; IMP:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromatin regulator; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..836
FT /note="Transcriptional regulatory protein UME6"
FT /id="PRO_0000114987"
FT DNA_BIND 771..798
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..594
FT /note="SIN3-binding"
FT REGION 636..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 99..109
FT /note="TPVHTPSGSPS->APVHAPAGAPA: Impairs meiotic genes
FT expression, sporulation and interactions with IME1 and
FT RIM11, and abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:9372955"
FT MUTAGEN 99..107
FT /note="TPVHTPSGS->APVHAPSGA: Impairs meiotic genes
FT expression and sporulation, reduces the interaction with
FT IME1, and abolishes phosphorylation."
FT MUTAGEN 99
FT /note="T->N,A: Impairs meiotic genes expression and
FT sporulation, reduces interactions with IME1 and RIM11, and
FT reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:10891485,
FT ECO:0000269|PubMed:9372955"
FT MUTAGEN 103
FT /note="T->A: Impairs meiotic genes expression and
FT sporulation, reduces interaction with IME, and reduces
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:10891485"
FT MUTAGEN 107
FT /note="S->A: Impairs meiotic genes expression and
FT sporulation, reduces interaction with IME, and reduces
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:10891485"
FT MUTAGEN 523
FT /note="A->S: Impairs SIN3-binding and gene repression
FT activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 524
FT /note="A->T: Impairs gene repression activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 525
FT /note="Missing: Impairs gene repression activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 526
FT /note="V->Q: Impairs gene repression activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 527
FT /note="L->P: Impairs SIN3-binding and gene repression
FT activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 528
FT /note="S->P: Impairs SIN3-binding and gene repression
FT activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 530
FT /note="M->T,V: Impairs SIN3-binding and gene repression
FT activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT MUTAGEN 635
FT /note="K->E: Impairs gene repression activity."
FT /evidence="ECO:0000269|PubMed:11238941"
FT CONFLICT 101
FT /note="V -> G (in Ref. 3; BAA04890)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="I -> V (in Ref. 1; AAA34471)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="N -> T (in Ref. 1; AAA34471)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="G -> D (in Ref. 1; AAA34471)"
FT /evidence="ECO:0000305"
FT HELIX 517..528
FT /evidence="ECO:0007829|PDB:6XAW"
SQ SEQUENCE 836 AA; 91124 MW; 0DDA0A6B4A157182 CRC64;
MLDKARSQSK HMDESNAAAS LLSMETTANN HHYLHNKTSR ATLMNSSQDG KKHAEDEVSD
GANSRHPTIS SASIESLKTT YDENPLLSIM KSTCAPNNTP VHTPSGSPSL KVQSGGDIKD
DPKENDTTTT TNTTLQDRRD SDNAVHAAAS PLAPSNTPSD PKSLCNGHVA QATDPQISGA
IQPQYTATNE DVFPYSSTST NSNTATTTIV AGAKKKIHLP PPQAPAVSSP GTTAAGSGAG
TGSGIRSRTG SDLPLIITSA NKNNGKTTNS PMSILSRNNS TNNNDNNSIQ SSDSRESSNN
NEIGGYLRGG TKRGGSPSND SQVQHNVHDD QCAVGVAPRN FYFNKDREIT DPNVKLDENE
SKINISFWLN SKYRDEAYSL NESSSNNASS NTDTPTNSRH ANTSSSITSR NNFQHFRFNQ
IPSQPPTSAS SFTSTNNNNP QRNNINRGED PFATSSRPST GFFYGDLPNR NNRNSPFHTN
EQYIPPPPPK YINSKLDGLR SRLLLGPNSA SSSTKLDDDL GTAAAVLSNM RSSPYRTHDK
PISNVNDMNN TNALGVPASR PHSSSFPSKG VLRPILLRIH NSEQQPIFES NNSTAVFDED
QDQNQDLSPY HLNLNSKKVL DPTFESRTRQ VTWNKNGKRI DRRLSAPEQQ QQLEVPPLKK
SRRSVGNARV ASQTNSDYNS LGESSTSSAP SSPSLKASSG LAYTADYPNA TSPDFAKSKG
KNVKPKAKSK AKQSSKKRPN NTTSKSKANN SQESNNATSS TSQGTRSRTG CWICRLRKKK
CTEERPHCFN CERLKLDCHY DAFKPDFVSD PKKKQMKLEE IKKKTKEAKR RAMKKK
