ID   MED9_YEAST              Reviewed;         149 AA.
AC   P33308; D6W1I5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   04-NOV-2026, entry version 193.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 9;
DE   AltName: Full=Chromosome segregation protein 2;
DE   AltName: Full=Mediator complex subunit 9;
GN   Name=CSE2; Synonyms=MED9; OrderedLocusNames=YNR010W; ORFNames=N2046;
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].
RX   PubMed=8336709; DOI=10.1128/mcb.13.8.4691-4702.1993;
RA   Xiao Z., McGrew J.T., Schroeder A.J., Fitzgerald-Hayes M.;
RT   "CSE1 and CSE2, two new genes required for accurate mitotic chromosome
RT   segregation in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 13:4691-4702(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7900425; DOI=10.1002/yea.320101013;
RA   Verhasselt P., Aert R., Voet M., Volckaert G.;
RT   "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT   centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL   Yeast 10:1355-1361(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
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   [6]
RP   COMPONENT OF MEDIATOR COMPLEX.
RX   PubMed=9812975; DOI=10.1074/jbc.273.47.30851;
RA   Gustafsson C.M., Myers L.C., Beve J., Spaahr H., Lui M.,
RA   Erdjument-Bromage H., Tempst P., Kornberg R.D.;
RT   "Identification of new mediator subunits in the RNA polymerase II
RT   holoenzyme from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 273:30851-30854(1998).
RN   [7]
RP   INTERACTION WITH MED4, 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   [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   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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
RP   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).
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).
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 pre-initiation complex with RNA polymerase II and the
CC       general transcription factors. The Mediator complex unfolds to an
CC       extended conformation and partially surrounds RNA polymerase II,
CC       specifically interacting with the unphosphorylated form of the C-
CC       terminal domain (CTD) of RNA polymerase II. The Mediator complex
CC       dissociates from the RNA polymerase II holoenzyme and stays at the
CC       promoter when transcriptional elongation begins.
CC       {ECO:0000269|PubMed:11555651, ECO:0000269|PubMed:16076843,
CC       ECO:0000269|PubMed:16109375, ECO:0000269|PubMed:16263706}.
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. CSE2/MED9
CC       interacts directly with MED4. {ECO:0000269|PubMed:11555651,
CC       ECO:0000269|PubMed:17192271}.
CC   -!- INTERACTION:
CC       P33308; Q12321: MED1; NbExp=3; IntAct=EBI-5174, EBI-32854;
CC       P33308; Q12343: MED4; NbExp=3; IntAct=EBI-5174, EBI-31503;
CC       P33308; Q08278: MED7; NbExp=3; IntAct=EBI-5174, EBI-10674;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1364 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 9 family.
CC       {ECO:0000305}.
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DR   EMBL; L14839; AAA34532.1; -; Genomic_DNA.
DR   EMBL; X77395; CAA54578.1; -; Genomic_DNA.
DR   EMBL; Z71625; CAA96287.1; -; Genomic_DNA.
DR   EMBL; AY558422; AAS56748.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10551.1; -; Genomic_DNA.
DR   PIR; B48083; B48083.
DR   RefSeq; NP_014407.3; NM_001183187.3.
DR   PDB; 5OQM; EM; 5.80 A; j=1-149.
DR   PDB; 5SVA; EM; 15.30 A; V=1-149.
DR   PDB; 7UI9; EM; 3.30 A; i=1-149.
DR   PDB; 7UIF; EM; 4.60 A; i=1-149.
DR   PDB; 7UIG; EM; 4.30 A; i=1-149.
DR   PDB; 7UIO; EM; 3.30 A; Ai/Bi=1-149.
DR   PDB; 8CEN; EM; 3.00 A; j=1-149.
DR   PDB; 8CEO; EM; 3.60 A; j=1-149.
DR   SMR; P33308; -.
DR   BioGRID; 35835; 581.
DR   ComplexPortal; CPX-3226; Core mediator complex.
DR   DIP; DIP-1276N; -.
DR   IntAct; P33308; 33.
DR   STRING; 4932.YNR010W; -.
DR   iPTMnet; P33308; -.
DR   PaxDb; 4932-YNR010W; -.
DR   PeptideAtlas; P33308; -.
DR   EnsemblFungi; YNR010W_mRNA; YNR010W; YNR010W.
DR   GeneID; 855744; -.
DR   KEGG; sce:YNR010W; -.
DR   VEuPathDB; FungiDB:YNR010W; -.
DR   AGR; SGD:S000005293; -.
DR   SGD; S000005293; CSE2.
DR   eggNOG; ENOG502S8AG; Eukaryota.
DR   HOGENOM; CLU_143643_0_0_1; -.
DR   InParanoid; P33308; -.
DR   OMA; AENSECM; -.
DR   OrthoDB; 4069563at2759; -.
DR   BioCyc; YEAST:G3O-33327-MONOMER; -.
DR   PRO; PR:P33308; -.
DR   CDD; cd21431; Med9-C; 1.
DR   InterPro; IPR011425; Med9.
DR   Pfam; PF07544; Med9; 1.
DR   GO; GO:0070847; C:core mediator complex; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
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 by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:ComplexPortal.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P33308; protein.
DR   BioGRID-ORCS; 855744; 3 hits in 10 CRISPR screens.
DR   AlphaFoldDB; P33308; -.
DR   EMDB; EMD-16610; -.
DR   EMDB; EMD-26542; -.
DR   EMDB; EMD-26544; -.
DR   EMDB; EMD-26545; -.
DR   EMDB; EMD-26551; -.
DR   EMDB; EMD-2786; -.
DR   EMDB; EMD-3850; -.
DR   EMDB; EMD-8305; -.
DR   FunCoup; P33308; 167.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..149
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   9"
FT                   /id="PRO_0000076529"
FT   REGION          18..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           77..99
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           136..149
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        25..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:8CEN"
FT   HELIX           66..75
FT                   /evidence="ECO:0007829|PDB:8CEN"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:8CEN"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:8CEN"
FT   HELIX           87..106
FT                   /evidence="ECO:0007829|PDB:8CEN"
FT   HELIX           110..114
FT                   /evidence="ECO:0007829|PDB:8CEN"
FT   HELIX           119..147
FT                   /evidence="ECO:0007829|PDB:8CEN"
SQ   SEQUENCE   149 AA;  17376 MW;  99D2347F5287AA3C CRC64;
     MNLQNNVLNQ IHQILLPTNP TLDKPNAEAT KEEFSSAENR DEKDYLTNQQ PKNLSTPSTS
     SNGEFIPHIF YSLHQIRKDP NNLSNQLETL TGSIRHRLKL CKSLISENED TKDLLSKSPS
     EWQDIIHQRE QELQIKRDVL DDLYRKLQR
//