MED18_YEAST
ID MED18_YEAST Reviewed; 307 AA.
AC P32585; D6VUN6; Q6B1R3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 18;
DE AltName: Full=Mediator complex subunit 18;
DE AltName: Full=Suppressor of RNA polymerase B 5;
GN Name=SRB5; Synonyms=MED18; OrderedLocusNames=YGR104C;
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 MUTAGENESIS OF THR-22.
RC STRAIN=Z28;
RX PubMed=8324825; DOI=10.1016/0092-8674(93)90362-t;
RA Thompson C.M., Koleske A.J., Chao D.M., Young R.A.;
RT "A multisubunit complex associated with the RNA polymerase II CTD and TATA-
RT binding protein in yeast.";
RL Cell 73:1361-1375(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=8187178; DOI=10.1016/0092-8674(94)90221-6;
RA Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D.;
RT "A multiprotein mediator of transcriptional activation and its interaction
RT with the C-terminal repeat domain of RNA polymerase II.";
RL Cell 77:599-608(1994).
RN [6]
RP FUNCTION.
RX PubMed=9845373; DOI=10.1016/s0092-8674(00)81641-4;
RA Holstege F.C.P., Jennings E.G., Wyrick J.J., Lee T.I., Hengartner C.J.,
RA Green M.R., Golub T.R., Lander E.S., Young R.A.;
RT "Dissecting the regulatory circuitry of a eukaryotic genome.";
RL Cell 95:717-728(1998).
RN [7]
RP INTERACTION WITH SRB2.
RX PubMed=9660972; DOI=10.1016/s1097-2765(00)80088-x;
RA Koh S.S., Ansari A.Z., Ptashne M., Young R.A.;
RT "An activator target in the RNA polymerase II holoenzyme.";
RL Mol. Cell 1:895-904(1998).
RN [8]
RP INTERACTION WITH MED8, FUNCTION OF THE MEDIATOR COMPLEX, AND INTERACTION OF
RP THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=11555651; DOI=10.1074/jbc.m105961200;
RA Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.;
RT "The structural and functional organization of the yeast mediator
RT complex.";
RL J. Biol. Chem. 276:42003-42010(2001).
RN [9]
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 [10]
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 [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 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 [13]
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 [14]
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 [15]
RP FUNCTION.
RX PubMed=16109375; DOI=10.1016/j.molcel.2005.06.033;
RA van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P.,
RA van Leenen D., Holstege F.C.P.;
RT "Mediator expression profiling epistasis reveals a signal transduction
RT pathway with antagonistic submodules and highly specific downstream
RT targets.";
RL Mol. Cell 19:511-522(2005).
RN [16]
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 [17]
RP INTERACTION WITH MED1; MED8; CSE2 AND RGR1, CHARACTERIZATION OF THE
RP MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH RNA
RP 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 [18]
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).
RN [19]
RP ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX HEAD MODULE, FUNCTION OF THE
RP MEDIATOR COMPLEX HEAD MODULE, INTERACTION OF THE MEDIATOR COMPLEX HEAD
RP MODULE WITH RNA POLYMERASE II AND TFIIF, AND INTERACTION WITH SRB2 AND
RP SRB4.
RX PubMed=16885025; DOI=10.1016/j.molcel.2006.06.007;
RA Takagi Y., Calero G., Komori H., Brown J.A., Ehrensberger A.H., Hudmon A.,
RA Asturias F.J., Kornberg R.D.;
RT "Head module control of mediator interactions.";
RL Mol. Cell 23:355-364(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-307 IN COMPLEX WITH MED8 AND
RP SRB2.
RX PubMed=16964259; DOI=10.1038/nsmb1143;
RA Lariviere L., Geiger S., Hoeppner S., Roether S., Straesser K., Cramer P.;
RT "Structure and TBP binding of the Mediator head subcomplex Med8-Med18-
RT Med20.";
RL Nat. Struct. Mol. Biol. 13:895-901(2006).
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:11555651,
CC ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16109375,
CC ECO:0000269|PubMed:16263706, ECO:0000269|PubMed:16885025,
CC ECO:0000269|PubMed:9845373}.
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. SRB5/MED18
CC interacts directly with MED8 and SRB2/MED20.
CC {ECO:0000269|PubMed:11555651, ECO:0000269|PubMed:16885025,
CC ECO:0000269|PubMed:16964259, ECO:0000269|PubMed:17192271,
CC ECO:0000269|PubMed:9660972}.
CC -!- INTERACTION:
CC P32585; P38304: MED8; NbExp=8; IntAct=EBI-18032, EBI-20932;
CC P32585; P34162: SRB2; NbExp=6; IntAct=EBI-18032, EBI-18018;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1011 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 18 family.
CC {ECO:0000305}.
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DR EMBL; L12028; AAB08012.1; -; Genomic_DNA.
DR EMBL; Z72889; CAA97108.1; -; Genomic_DNA.
DR EMBL; AY693017; AAT93036.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08197.1; -; Genomic_DNA.
DR PIR; B40711; B40711.
DR RefSeq; NP_011618.3; NM_001181233.3.
DR PDB; 2HZM; X-ray; 2.40 A; B/D/F/H=2-307.
DR PDB; 2HZS; X-ray; 2.70 A; B/D/F/H=2-307.
DR PDB; 3J1O; EM; 16.00 A; L=1-307.
DR PDB; 3RJ1; X-ray; 4.30 A; E/L/S=1-307.
DR PDB; 4GWP; X-ray; 4.20 A; E=1-307.
DR PDB; 4GWQ; X-ray; 4.50 A; E=1-307.
DR PDB; 4V1O; EM; 9.70 A; X=1-307.
DR PDB; 5OQM; EM; 5.80 A; e=1-307.
DR PDB; 5SVA; EM; 15.30 A; Q=1-307.
DR PDBsum; 2HZM; -.
DR PDBsum; 2HZS; -.
DR PDBsum; 3J1O; -.
DR PDBsum; 3RJ1; -.
DR PDBsum; 4GWP; -.
DR PDBsum; 4GWQ; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR AlphaFoldDB; P32585; -.
DR SMR; P32585; -.
DR BioGRID; 33347; 96.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-1658N; -.
DR IntAct; P32585; 32.
DR MINT; P32585; -.
DR STRING; 4932.YGR104C; -.
DR MaxQB; P32585; -.
DR PaxDb; P32585; -.
DR PRIDE; P32585; -.
DR EnsemblFungi; YGR104C_mRNA; YGR104C; YGR104C.
DR GeneID; 852996; -.
DR KEGG; sce:YGR104C; -.
DR SGD; S000003336; SRB5.
DR VEuPathDB; FungiDB:YGR104C; -.
DR eggNOG; ENOG502RXWG; Eukaryota.
DR HOGENOM; CLU_058255_1_0_1; -.
DR InParanoid; P32585; -.
DR OMA; DRKSMDS; -.
DR BioCyc; YEAST:G3O-30814-MON; -.
DR EvolutionaryTrace; P32585; -.
DR PRO; PR:P32585; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32585; 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:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IMP:SGD.
DR InterPro; IPR019095; Mediator_Med18.
DR PANTHER; PTHR13321; PTHR13321; 1.
DR Pfam; PF09637; Med18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..307
FT /note="Mediator of RNA polymerase II transcription subunit
FT 18"
FT /id="PRO_0000096368"
FT REGION 117..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 22
FT /note="T->I: In SRB5-1; suppresses the phenotypic defects
FT of an RNA polymerase II CTD truncation."
FT /evidence="ECO:0000269|PubMed:8324825"
FT CONFLICT 225
FT /note="K -> R (in Ref. 4; AAT93036)"
FT /evidence="ECO:0000305"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 32..43
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2HZS"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2HZS"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 180..195
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 209..223
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2HZM"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:2HZM"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2HZM"
SQ SEQUENCE 307 AA; 34289 MW; B1148FC187C2802A CRC64;
MVQQLSLFGS IGDDGYDLLI STLTTISGNP PLLYNSLCTV WKPNPSYDVE NVNSRNQLVE
PNRIKLSKEV PFSYLIDETM MDKPLNFRIL KSFTNDKIPL NYAMTRNILH NTVPQVTNFN
STNEDQNNSK HTEDTVNESR NSDDIIDVDM DASPAPSNES CSPWSLQISD IPAAGNNRSV
SMQTIAETII LSSAGKNSSV SSLMNGLGYV FEFQYLTIGV KFFMKHGLIL ELQKIWQIEE
AGNSQITSGG FLLKAYINVS RGTDIDRINY TETALMNLKK ELQGYIELSV PDRQSMDSRV
AHGNILI
