UME1_YEAST
ID UME1_YEAST Reviewed; 460 AA.
AC Q03010; D6W3M9; P87330;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcriptional regulatory protein UME1;
DE AltName: Full=WD repeat-containing transcriptional modulator 3;
GN Name=UME1; Synonyms=WTM3; OrderedLocusNames=YPL139C; ORFNames=LPI7C;
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 204626 / S288c / A364A;
RA Mallory M.J., Strich R.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9234739; DOI=10.1128/mcb.17.8.4830;
RA Pemberton L.F., Blobel G.;
RT "Characterization of the Wtm proteins, a novel family of Saccharomyces
RT cerevisiae transcriptional modulators with roles in meiotic regulation and
RT silencing.";
RL Mol. Cell. Biol. 17:4830-4841(1997).
RN [5]
RP FUNCTION, INDUCTION, DOMAINS, AND INTERACTION WITH RPD3.
RX PubMed=12954623; DOI=10.1074/jbc.m308632200;
RA Mallory M.J., Strich R.;
RT "Ume1p represses meiotic gene transcription in Saccharomyces cerevisiae
RT through interaction with the histone deacetylase Rpd3p.";
RL J. Biol. Chem. 278:44727-44734(2003).
RN [6]
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 [7]
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 [8]
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 [9]
RP IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND FUNCTION OF THE RPD3C(S) COMPLEX.
RX PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
RA Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
RA Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C.,
RA Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M.,
RA Greenblatt J.F., Buratowski S., Krogan N.J.;
RT "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
RT repressive Rpd3 complex.";
RL Cell 123:593-605(2005).
CC -!- FUNCTION: Catalytic component of the RPD3 histone deacetylase complexes
CC RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine
CC residues on the N-terminal part of the core histones (H2A, H2B, H3 and
CC H4). Histone deacetylation gives a tag for epigenetic repression and
CC plays an important role in transcriptional regulation, cell cycle
CC progression and developmental events. {ECO:0000269|PubMed:12954623,
CC ECO:0000269|PubMed:16286008, ECO:0000269|PubMed:9234739}.
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 Component of the RPD3C(S) complex composed of at least EAF3, RCO1,
CC RPD3, SIN3, and UME1. Interacts with RPD3.
CC {ECO:0000269|PubMed:12954623, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:16314178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: By glucose. {ECO:0000269|PubMed:12954623}.
CC -!- DOMAIN: The NEE-box motif is required for the association to RPD3.
CC {ECO:0000269|PubMed:12954623}.
CC -!- MISCELLANEOUS: Present with 3040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U10280; AAB40937.1; -; Genomic_DNA.
DR EMBL; U43703; AAB68221.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11295.1; -; Genomic_DNA.
DR PIR; S69046; S69046.
DR RefSeq; NP_015186.1; NM_001183953.1.
DR AlphaFoldDB; Q03010; -.
DR BioGRID; 36043; 295.
DR ComplexPortal; CPX-1851; RPD3S histone deacetylase complex.
DR ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR DIP; DIP-5290N; -.
DR IntAct; Q03010; 28.
DR MINT; Q03010; -.
DR STRING; 4932.YPL139C; -.
DR iPTMnet; Q03010; -.
DR MaxQB; Q03010; -.
DR PaxDb; Q03010; -.
DR PRIDE; Q03010; -.
DR EnsemblFungi; YPL139C_mRNA; YPL139C; YPL139C.
DR GeneID; 855964; -.
DR KEGG; sce:YPL139C; -.
DR SGD; S000006060; UME1.
DR VEuPathDB; FungiDB:YPL139C; -.
DR eggNOG; ENOG502QSEV; Eukaryota.
DR GeneTree; ENSGT00940000176348; -.
DR HOGENOM; CLU_036523_0_0_1; -.
DR InParanoid; Q03010; -.
DR OMA; WDIRTIA; -.
DR BioCyc; YEAST:G3O-34037-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q03010; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03010; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Meiosis; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..460
FT /note="Transcriptional regulatory protein UME1"
FT /id="PRO_0000051315"
FT REPEAT 233..271
FT /note="WD 1"
FT REPEAT 276..316
FT /note="WD 2"
FT REPEAT 339..379
FT /note="WD 3"
FT REPEAT 411..451
FT /note="WD 4"
FT MOTIF 14..22
FT /note="NEE-box"
SQ SEQUENCE 460 AA; 51022 MW; AA6F60448B7BCBA9 CRC64;
MSTLDIAEDN KIKNEEFKIW KKSIPSLYQH ISSLKPIFGS GVDESPSTLR SIVFTNDSSC
NKSKGVLSVP LLYSQGSEIF EVDCIVPLGL HYKKPESISE PLVQPDYTME SQKVEQTVLI
PKWEFKGETI AKMIYVDNSE INVKVIALST NGSLAWFREG VKSPVYTMME PSTSLSSASS
GNQNKPCVDF AISNDSKTLT VTKEKHLDNE NATIKLIDNS GKIGEVLRTI PVPGIKNIQE
IKFLNNQIFA TCSDDGIIRF WGNEIGKKPL WILNDSLDGK TTCFAASPFV DTLFMTGTSG
GALKVWDIRA VIALGDADAE LNINQGHNKV NELFKVHHFY SEQVSKIEFS SISPMEVVTI
GGLGNVYHWN FEPVFAIYNE IHEDFQGIIS DELEAESMAF YHTEGCRREI GENNKVNTVA
YHKYIEDLVA TVDSDGLLTV YKPFTGKVLD GSREVGAAKS
