LEO1_YEAST
ID LEO1_YEAST Reviewed; 464 AA.
AC P38439; D6W2I1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=RNA polymerase-associated protein LEO1;
GN Name=LEO1; OrderedLocusNames=YOR123C; ORFNames=O3278, YOR3278C;
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 204510 / AB320;
RX PubMed=8018723; DOI=10.1016/0167-4781(94)90013-2;
RA Magdolen V., Lang P., Mages G., Hermann H., Bandlow W.;
RT "The gene LEO1 on yeast chromosome XV encodes a non-essential, extremely
RT hydrophilic protein.";
RL Biochim. Biophys. Acta 1218:205-209(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-326.
RX PubMed=1429680; DOI=10.1016/s0021-9258(18)50100-9;
RA Baker R.T., Tobias J.W., Varshavsky A.;
RT "Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2
RT and UBP3, and functional analysis of the UBP gene family.";
RL J. Biol. Chem. 267:23364-23375(1992).
RN [7]
RP IDENTIFICATION IN THE PAF1 COMPLEX.
RX PubMed=11884586; DOI=10.1128/mcb.22.7.1971-1980.2002;
RA Mueller C.L., Jaehning J.A.;
RT "Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II
RT complex.";
RL Mol. Cell. Biol. 22:1971-1980(2002).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15643076; DOI=10.1128/ec.4.1.209-220.2005;
RA Porter S.E., Penheiter K.L., Jaehning J.A.;
RT "Separation of the Saccharomyces cerevisiae Paf1 complex from RNA
RT polymerase II results in changes in its subnuclear localization.";
RL Eukaryot. Cell 4:209-220(2005).
RN [10]
RP FUNCTION.
RX PubMed=16246725; DOI=10.1016/j.molcel.2005.08.026;
RA Sheldon K.E., Mauger D.M., Arndt K.M.;
RT "A requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3'
RT end formation.";
RL Mol. Cell 20:225-236(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-132 AND SER-358, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-132; SER-188 AND
RP SER-358, AND 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-132; SER-358 AND
RP SER-372, AND IDENTIFICATION BY MASS 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: The PAF1 complex is a multifunctional complex. Involved in
CC transcription initiation via genetic interactions with TATA-binding
CC proteins. Involved in elongation. It regulates 3'-end formation of
CC snR47 by modulating the recruitment or stable association of NRD1 and
CC NAB3 with RNA polymerase II. Also has a role in transcription-coupled
CC histone modification. Required for activation of RAD6 ubiquitin
CC conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126'
CC histone H2B. Activates the SET1 histone methyltransferase complex for
CC methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of
CC histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.
CC {ECO:0000269|PubMed:15643076, ECO:0000269|PubMed:16246725}.
CC -!- SUBUNIT: Component of the PAF1 complex which consists of at least
CC CDC73, CTR9, LEO1, PAF1 and RTF1. {ECO:0000269|PubMed:11884586}.
CC -!- INTERACTION:
CC P38439; P89105: CTR9; NbExp=5; IntAct=EBI-10108, EBI-5283;
CC P38439; P38351: PAF1; NbExp=5; IntAct=EBI-10108, EBI-12855;
CC P38439; P53064: RTF1; NbExp=5; IntAct=EBI-10108, EBI-16303;
CC P38439; Q00772: SLT2; NbExp=2; IntAct=EBI-10108, EBI-17372;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15643076}.
CC -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}.
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DR EMBL; X77135; CAA54391.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62122.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64042.1; -; Genomic_DNA.
DR EMBL; Z75031; CAA99322.1; -; Genomic_DNA.
DR EMBL; M94916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006948; DAA10897.1; -; Genomic_DNA.
DR PIR; S45363; S45363.
DR RefSeq; NP_014766.1; NM_001183542.1.
DR AlphaFoldDB; P38439; -.
DR SMR; P38439; -.
DR BioGRID; 34518; 483.
DR ComplexPortal; CPX-1726; PAF1 complex.
DR DIP; DIP-4143N; -.
DR IntAct; P38439; 12.
DR MINT; P38439; -.
DR STRING; 4932.YOR123C; -.
DR iPTMnet; P38439; -.
DR MaxQB; P38439; -.
DR PaxDb; P38439; -.
DR PRIDE; P38439; -.
DR EnsemblFungi; YOR123C_mRNA; YOR123C; YOR123C.
DR GeneID; 854290; -.
DR KEGG; sce:YOR123C; -.
DR SGD; S000005649; LEO1.
DR VEuPathDB; FungiDB:YOR123C; -.
DR eggNOG; KOG2428; Eukaryota.
DR GeneTree; ENSGT00550000074952; -.
DR HOGENOM; CLU_052846_0_0_1; -.
DR InParanoid; P38439; -.
DR OMA; DNDQRES; -.
DR BioCyc; YEAST:G3O-33650-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:P38439; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38439; protein.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IPI:SGD.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:SGD.
DR GO; GO:0016571; P:histone methylation; IC:ComplexPortal.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:2001173; P:regulation of histone H2B conserved C-terminal lysine ubiquitination; IDA:SGD.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IGI:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR InterPro; IPR007149; Leo1.
DR PANTHER; PTHR23146; PTHR23146; 1.
DR Pfam; PF04004; Leo1; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..464
FT /note="RNA polymerase-associated protein LEO1"
FT /id="PRO_0000084406"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 134
FT /note="Q -> L (in Ref. 6; M94916)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="T -> N (in Ref. 6; M94916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 53920 MW; ABDE3D7D5A2C78A5 CRC64;
MSSESPQDQP QKEQISNNVG VTTNSTSNEE TSRSQDDNVK EVNGNDDTKE EEQEEDAELD
DLFGDDNDDD DDDDVKKSET EKSDSDSDED DEGENINHRS RHRESLGLDD DEAEEQAMYT
RKFYGEDANN FSDQDETTHT FKEENVELVR HIIPSKANVN ETASHNEIFY ARIPNFLTID
PIPFDPPSFE AKVNERASNS ASREDQLDDR LIDENTVRWR YSRDKDQHVF KESNTQIVQW
SDGTYSLKVG EECTDILVND TSNTFLTVSH DQQELIQCYE GGEIKKTLMF IPTSTNSKIH
QKLSKAVIRR NQRQSKGPGT YIVSMDPEVE KKELERKQSQ ILRDRRRRQL KEKEKQESPD
AAFETGFRKQ NSPTTYGASR RNEYEEDDFL VDDDEEEEAA FDDEEDDNEE EEEEEDADEE
NASRLRNLKR EGAAMYREEE EEEKDRSETK RRRVAVIEDD EDED
