MED14_YEAST
ID MED14_YEAST Reviewed; 1082 AA.
AC P19263; D6VY72; Q07999;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 14;
DE AltName: Full=Glucose repression regulatory protein 1;
DE AltName: Full=Mediator complex subunit 14;
GN Name=RGR1; Synonyms=MED14; OrderedLocusNames=YLR071C;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2196447; DOI=10.1128/mcb.10.8.4130-4138.1990;
RA Sakai A., Shimizu Y., Kondou S., Chibazakura T., Hishinuma F.;
RT "Structure and molecular analysis of RGR1, a gene required for glucose
RT repression of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:4130-4138(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [5]
RP PROTEIN SEQUENCE OF 857-868, AND COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=7479899; DOI=10.1073/pnas.92.24.10864;
RA Li Y., Bjoerklund S., Jiang Y.W., Kim Y.-J., Lane W.S., Stillman D.J.,
RA Kornberg R.D.;
RT "Yeast global transcriptional regulators Sin4 and Rgr1 are components of
RT mediator complex/RNA polymerase II holoenzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10864-10868(1995).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND COMPONENT OF MEDIATOR
RP COMPLEX.
RX PubMed=11383511;
RA Liu Y., Ranish J.A., Aebersold R., Hahn S.;
RT "Yeast nuclear extract contains two major forms of RNA polymerase II
RT mediator complexes.";
RL J. Biol. Chem. 276:7169-7175(2001).
RN [7]
RP FUNCTION.
RX PubMed=7635307; DOI=10.1093/genetics/140.1.47;
RA Jiang Y.W., Dohrmann P.R., Stillman D.J.;
RT "Genetic and physical interactions between yeast RGR1 and SIN4 in chromatin
RT organization and transcriptional regulation.";
RL Genetics 140:47-54(1995).
RN [8]
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 [9]
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 [10]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=14623974; DOI=10.1073/pnas.2036346100;
RA Kuras L., Borggrefe T., Kornberg R.D.;
RT "Association of the Mediator complex with enhancers of active genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13887-13891(2003).
RN [11]
RP NOMENCLATURE.
RX PubMed=15175151; DOI=10.1016/j.molcel.2004.05.011;
RA Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J.,
RA Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M.,
RA Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P.,
RA Fukasawa T., Gustafsson C.M., Han M., He X., Herman P.K., Hinnebusch A.G.,
RA Holmberg S., Holstege F.C.P., Jaehning J.A., Kim Y.-J., Kuras L., Leutz A.,
RA Lis J.T., Meisterernest M., Naeaer A.M., Nasmyth K., Parvin J.D.,
RA Ptashne M., Reinberg D., Ronne H., Sadowski I., Sakurai H., Sipiczki M.,
RA Sternberg P.W., Stillman D.J., Strich R., Struhl K., Svejstrup J.Q.,
RA Tuck S., Winston F., Roeder R.G., Kornberg R.D.;
RT "A unified nomenclature for protein subunits of mediator complexes linking
RT transcriptional regulators to RNA polymerase II.";
RL Mol. Cell 14:553-557(2004).
RN [12]
RP PHOSPHORYLATION BY KIN28.
RX PubMed=14749387; DOI=10.1128/mcb.24.4.1721-1735.2004;
RA Liu Y., Kung C., Fishburn J., Ansari A.Z., Shokat K.M., Hahn S.;
RT "Two cyclin-dependent kinases promote RNA polymerase II transcription and
RT formation of the scaffold complex.";
RL Mol. Cell. Biol. 24:1721-1735(2004).
RN [13]
RP TOPOLOGY OF THE MEDIATOR COMPLEX.
RX PubMed=15477388; DOI=10.1093/nar/gkh878;
RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
RT "A high resolution protein interaction map of the yeast Mediator complex.";
RL Nucleic Acids Res. 32:5379-5391(2004).
RN [14]
RP CHARACTERIZATION OF THE MEDIATOR COMPLEX.
RX PubMed=16002404; DOI=10.1074/jbc.c500150200;
RA Takagi Y., Chadick J.Z., Davis J.A., Asturias F.J.;
RT "Preponderance of free mediator in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:31200-31207(2005).
RN [15]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16076843; DOI=10.1074/jbc.m506067200;
RA Nair D., Kim Y., Myers L.C.;
RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription
RT in yeast extracts.";
RL J. Biol. Chem. 280:33739-33748(2005).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [17]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16263706; DOI=10.1074/jbc.m508253200;
RA Takagi Y., Kornberg R.D.;
RT "Mediator as a general transcription factor.";
RL J. Biol. Chem. 281:80-89(2006).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
RA van de Peppel J., Werner M., Holstege F.C.P.;
RT "Genome-wide location of the coactivator mediator: binding without
RT activation and transient Cdk8 interaction on DNA.";
RL Mol. Cell 22:179-192(2006).
RN [19]
RP INTERACTION WITH SRB5, CHARACTERIZATION OF THE MEDIATOR COMPLEX, AND
RP INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=17192271; DOI=10.1074/jbc.m609484200;
RA Baidoobonso S.M., Guidi B.W., Myers L.C.;
RT "Med19(Rox3) regulates intermodule interactions in the Saccharomyces
RT cerevisiae mediator complex.";
RL J. Biol. Chem. 282:5551-5559(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1036, AND IDENTIFICATION BY
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [22]
RP ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.
RX PubMed=12191485; DOI=10.1016/s1097-2765(02)00598-1;
RA Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.;
RT "Structure of the yeast RNA polymerase II holoenzyme: mediator conformation
RT and polymerase interaction.";
RL Mol. Cell 10:409-415(2002).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. The Mediator complex, having a compact
CC conformation in its free form, is recruited to promoters by direct
CC interactions with regulatory proteins and serves for the assembly of a
CC functional preinitiation complex with RNA polymerase II and the general
CC transcription factors. The Mediator complex unfolds to an extended
CC conformation and partially surrounds RNA polymerase II, specifically
CC interacting with the unphosphorylated form of the C-terminal domain
CC (CTD) of RNA polymerase II. The Mediator complex dissociates from the
CC RNA polymerase II holoenzyme and stays at the promoter when
CC transcriptional elongation begins. {ECO:0000269|PubMed:16076843,
CC ECO:0000269|PubMed:16263706, ECO:0000269|PubMed:2196447,
CC ECO:0000269|PubMed:7635307}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of at
CC least 21 subunits that form three structurally distinct submodules. The
CC Mediator head module contains MED6, MED8, MED11, SRB4/MED17,
CC SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module
CC contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21
CC and SOH1/MED31, and the tail module contains MED2, PGD1/MED3,
CC RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules
CC interact directly with RNA polymerase II, whereas the elongated tail
CC module interacts with gene-specific regulatory proteins.
CC {ECO:0000269|PubMed:17192271}.
CC -!- INTERACTION:
CC P19263; Q12321: MED1; NbExp=3; IntAct=EBI-15087, EBI-32854;
CC P19263; Q06213: NUT2; NbExp=3; IntAct=EBI-15087, EBI-12414;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11383511,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16630888}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 14 family.
CC {ECO:0000305}.
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DR EMBL; D90051; BAA14104.1; -; Genomic_DNA.
DR EMBL; Z73243; CAA97628.1; -; Genomic_DNA.
DR EMBL; AY692942; AAT92961.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09388.1; -; Genomic_DNA.
DR PIR; S64903; S64903.
DR RefSeq; NP_013172.1; NM_001181958.1.
DR PDB; 5OQM; EM; 5.80 A; l=1-745.
DR PDBsum; 5OQM; -.
DR AlphaFoldDB; P19263; -.
DR SMR; P19263; -.
DR BioGRID; 31345; 375.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-1562N; -.
DR IntAct; P19263; 38.
DR MINT; P19263; -.
DR STRING; 4932.YLR071C; -.
DR iPTMnet; P19263; -.
DR MaxQB; P19263; -.
DR PaxDb; P19263; -.
DR PRIDE; P19263; -.
DR EnsemblFungi; YLR071C_mRNA; YLR071C; YLR071C.
DR GeneID; 850760; -.
DR KEGG; sce:YLR071C; -.
DR SGD; S000004061; RGR1.
DR VEuPathDB; FungiDB:YLR071C; -.
DR eggNOG; KOG1875; Eukaryota.
DR GeneTree; ENSGT00390000001021; -.
DR HOGENOM; CLU_286680_0_0_1; -.
DR InParanoid; P19263; -.
DR OMA; MIDLLNW; -.
DR BioCyc; YEAST:G3O-32223-MON; -.
DR PRO; PR:P19263; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P19263; protein.
DR GO; GO:0070847; C:core mediator complex; IDA:SGD.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:ComplexPortal.
DR InterPro; IPR013947; Mediator_Med14.
DR PANTHER; PTHR12809; PTHR12809; 1.
DR Pfam; PF08638; Med14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..1082
FT /note="Mediator of RNA polymerase II transcription subunit
FT 14"
FT /id="PRO_0000096362"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1036
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 46
FT /note="G -> S (in Ref. 1; BAA14104)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="D -> V (in Ref. 1; BAA14104)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> T (in Ref. 1; BAA14104)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="E -> V (in Ref. 1; BAA14104)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="T -> A (in Ref. 1; BAA14104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1082 AA; 123358 MW; 96277001829DB539 CRC64;
MTTTIGSPQM LANEERLSNE MHALKNRSEQ NGQEQQGPVK NTQLHGPSAT DPETTATQKE
SLEMVPKDTS AATMTSAPPP ALPHVEINQV SLALVIRNLT VFTMKELAQY MKTNVHTQAN
EPNSAKKIRF LQLIIFLRTQ FLKLYVLVKW TRTIKQNNFH VLIDLLNWFR TTNMNVNNCI
WALKSSLNSM TNAKLPNVDL VTALEVLSLG RPNLPTHNFK LSGVSNSMDM VDGMAKVPIG
LILQRLKDLN LTVSIKIALM NIPKPLNSYH IKNGRIYFTV PNEFEIQLST VNRQSPLFFV
DLKLLFNTEA EQTVSAVTEA TSTNGDSENN EENSSSNGNN LPLNKPRLEK LINEILLKSN
DPLLSLYNFL HKYVLTLQLY MVHREFLKLA NGGKFSKSNL IHNYDSKKST ITVRYWLNGK
MDSKGKITIG IQRTTESLIL KWDNQSASRA KNMPVIYNNI VSNIEGILDE IMFNHARIIR
SELLARDIFQ EDEENSDVLL FQLPTTCVSM APIQLKIDLL SGQFYFRNPT PLLSNYASKI
NRAEGPEELA RILQQLKLDK IIHVLTTMFE NTGWSCSRII KIDKPIRTQV NTGGESVVKK
EDNKYAIAGN STTNSDVSLL LQRDLFIRLP HWPLNWYLIL SIISSKTSCV VEKRIGKIVS
QRGKWNLKYL DNSNVMTVKL ESITYQKIMI LQRTILNRII NHMLIDSLNQ LEIRNKICSS
EMINEQKLPQ YIIQGSNTND NISIITLELE SFLEGSKALN SILESSMFLR IDYSNSQIRL
YAKFKRNTMM IQCQIDKLYI HFVQEEPLAF YLEESFTNLG IIVQYLTKFR QKLMQLVVLT
DVVERLHKNF ESENFKIIAL QPNEISFKYL SNNDEDDKDC TIKISTNDDS IKNLTVQLSP
SNPQHIIQPF LDNSKMDYHF IFSYLQFTSS LFKALKVILN ERGGKFHESG SQYSTMVNIG
LHNLNEYQIV YYNPQAGTKI TICIELKTVL HNGRDKIQFH IHFADVAHIT TKSPAYPMMH
QVRNQVFMLD TKRLGTPESV KPANASHAIR LGNGVACDPS EIEPILMEIH NILKVDSNSS
SS
