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 27-MAR-2024, entry version 195. 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; GN OrderedLocusNames=YDR207C; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 804. 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 GlyGen; P39001; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P39001; -. DR MaxQB; P39001; -. DR PaxDb; 4932-YDR207C; -. DR PeptideAtlas; P39001; -. DR EnsemblFungi; YDR207C_mRNA; YDR207C; YDR207C. DR GeneID; 851788; -. DR KEGG; sce:YDR207C; -. DR AGR; SGD:S000002615; -. 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 OrthoDB; 1706035at2759; -. DR BioCyc; YEAST:G3O-29791-MONOMER; -. DR BioGRID-ORCS; 851788; 3 hits in 13 CRISPR screens. DR PRO; PR:P39001; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P39001; Protein. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. 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; NAS:ComplexPortal. 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: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: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: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; Zn(2)-C6 fungal-type DNA-binding domain; 1. DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf. DR InterPro; IPR001138; Zn2Cys6_DnaBD. DR PANTHER; PTHR37534; TRANSCRIPTIONAL ACTIVATOR PROTEIN UGA3; 1. DR PANTHER; PTHR37534:SF46; TRANSCRIPTIONAL REGULATORY PROTEIN UME6; 1. DR Pfam; PF00172; Zn_clus; 1. DR SMART; SM00066; GAL4; 1. DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 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 //