LGE1_YEAST
ID LGE1_YEAST Reviewed; 332 AA.
AC Q02796; D6W3V9; Q6Q5I8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Transcriptional regulatory protein LGE1 {ECO:0000305};
DE AltName: Full=Large cells protein 1 {ECO:0000303|PubMed:12089449};
GN Name=LGE1 {ECO:0000303|PubMed:12089449}; OrderedLocusNames=YPL055C;
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 [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 [2]
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 [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=12089449; DOI=10.1126/science.1070850;
RA Jorgensen P., Nishikawa J.L., Breitkreutz B.-J., Tyers M.;
RT "Systematic identification of pathways that couple cell growth and division
RT in yeast.";
RL Science 297:395-400(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH BRE1.
RX PubMed=12535538; DOI=10.1016/s1097-2765(02)00826-2;
RA Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C.,
RA Madhani H.D.;
RT "A conserved RING finger protein required for histone H2B
RT monoubiquitination and cell size control.";
RL Mol. Cell 11:261-266(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 FUNCTION, AND INTERACTION WITH BRE1.
RX PubMed=15528187; DOI=10.1074/jbc.m408333200;
RA Zhang X., Kolaczkowska A., Devaux F., Panwar S.L., Hallstrom T.C., Jacq C.,
RA Moye-Rowley W.S.;
RT "Transcriptional regulation by Lge1p requires a function independent of its
RT role in histone H2B ubiquitination.";
RL J. Biol. Chem. 280:2759-2770(2005).
RN [9]
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 [10]
RP METHYLATION AT ARG-39.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [11]
RP METHYLATION AT ARG-30.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
CC -!- FUNCTION: Required to activate transcription of PDR3, a gene involved
CC in retrograde regulation of multidrug resistance, a phenomenon that
CC takes place in cells that have lost their mitochondrial genome. Also
CC required for ubiquitination of histone H2B to form H2BK123ub1.
CC H2BK123ub1 gives a specific tag for epigenetic transcriptional
CC activation, telomeric silencing, and is also a prerequisite for H3K4me
CC and H3K79me formation. Its precise role in H2BK123ub1 formation however
CC is unclear and is independent of retrograde regulation of multidrug
CC resistance function. {ECO:0000269|PubMed:12535538,
CC ECO:0000269|PubMed:15528187}.
CC -!- SUBUNIT: Probably interacts with BRE1. {ECO:0000269|PubMed:12535538,
CC ECO:0000269|PubMed:15528187}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U39205; AAB68310.1; -; Genomic_DNA.
DR EMBL; AY558038; AAS56364.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11375.1; -; Genomic_DNA.
DR PIR; S60935; S60935.
DR RefSeq; NP_015270.1; NM_001183869.1.
DR AlphaFoldDB; Q02796; -.
DR SMR; Q02796; -.
DR BioGRID; 36125; 811.
DR DIP; DIP-6470N; -.
DR IntAct; Q02796; 81.
DR MINT; Q02796; -.
DR STRING; 4932.YPL055C; -.
DR iPTMnet; Q02796; -.
DR MaxQB; Q02796; -.
DR PaxDb; Q02796; -.
DR PRIDE; Q02796; -.
DR EnsemblFungi; YPL055C_mRNA; YPL055C; YPL055C.
DR GeneID; 856052; -.
DR KEGG; sce:YPL055C; -.
DR SGD; S000005976; LGE1.
DR VEuPathDB; FungiDB:YPL055C; -.
DR eggNOG; ENOG502SA4A; Eukaryota.
DR HOGENOM; CLU_826809_0_0_1; -.
DR InParanoid; Q02796; -.
DR OMA; YSANSRH; -.
DR BioCyc; YEAST:G3O-33967-MON; -.
DR PRO; PR:Q02796; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02796; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016571; P:histone methylation; IMP:SGD.
DR GO; GO:0016574; P:histone ubiquitination; IMP:SGD.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:SGD.
DR GO; GO:0006513; P:protein monoubiquitination; IMP:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Coiled coil; Methylation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..332
FT /note="Transcriptional regulatory protein LGE1"
FT /id="PRO_0000076234"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..328
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 39
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT CONFLICT 28
FT /note="R -> Q (in Ref. 3; AAS56364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 37309 MW; C3300ED944003F9D CRC64;
MSGYTGNNYS RYSSTPPRQR GGYHHARRSR GGAGGSYYRG GNASYGARYN SDYEQPPQEG
DLRQTGAYYR NGYTDTRPYY SANSRHYQAQ PSPRYNNGTN SYHLPQRGNS QDTNGRTTSA
SQEDNDEKRV KSRYRNMQAD HPRQQPMSVG STSSRNGSSG NSSTSSTSNG LPPPPSVSSI
TNNRSYHSSA YPYSSSHTYN NYHHRETPPP PPSNGYYAKG YPVHVPENRS NSDGSSSSVV
KKKRILDMKD SPFIYLTDFD KNVKKTNNTE SECEKAREVF KESDSIDSAL EELNLKINSN
ELELRLLNNQ CDKHALNIQL TQEKLDSLLL MQ
