MED15_YEAST
ID MED15_YEAST Reviewed; 1081 AA.
AC P19659; D6W217; Q08221;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
DE AltName: Full=Autonomous replication regulatory protein 3;
DE AltName: Full=Basal expression activator protein 1;
DE AltName: Full=Defective silencing suppressor protein 4;
DE AltName: Full=Mediator complex subunit 15;
DE AltName: Full=Transcription regulatory protein GAL11;
DE AltName: Full=Ty insertion suppressor protein 13;
GN Name=GAL11 {ECO:0000303|PubMed:3062377, ECO:0000312|SGD:S000005411};
GN Synonyms=ABE1 {ECO:0000312|SGD:S000005411},
GN MED15 {ECO:0000303|PubMed:19940160}, RAR3 {ECO:0000312|SGD:S000005411},
GN SDS4 {ECO:0000312|SGD:S000005411}, SPT13 {ECO:0000312|SGD:S000005411};
GN OrderedLocusNames=YOL051W;
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 204508 / S288c;
RX PubMed=3062377; DOI=10.1128/mcb.8.11.4991-4999.1988;
RA Suzuki Y., Nogi Y., Abe A., Fukasawa T.;
RT "GAL11 protein, an auxiliary transcription activator for genes encoding
RT galactose-metabolizing enzymes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 8:4991-4999(1988).
RN [2]
RP ERRATUM OF PUBMED:3062377, AND SEQUENCE REVISION.
RX PubMed=1406662; DOI=10.1128/mcb.12.10.4806-.1992;
RA Suzuki Y., Nogi Y., Abe A., Fukasawa T.;
RL Mol. Cell. Biol. 12:4806-4806(1992).
RN [3]
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 [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] OF 1-352.
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8789261;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL Yeast 12:67-76(1996).
RN [6]
RP CHARACTERIZATION.
RX PubMed=2005915; DOI=10.1128/mcb.11.4.2311-2314.1991;
RA Long R.M., Mylin L.M., Hopper J.E.;
RT "GAL11 (SPT13), a transcriptional regulator of diverse yeast genes, affects
RT the phosphorylation state of GAL4, a highly specific transcriptional
RT activator.";
RL Mol. Cell. Biol. 11:2311-2314(1991).
RN [7]
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 [8]
RP INTERACTION WITH GAL4.
RX PubMed=11478912; DOI=10.1021/bi010011k;
RA Jeong C.-J., Yang S.-H., Xie Y., Zhang L., Johnston S.A., Kodadek T.;
RT "Evidence that Gal11 protein is a target of the Gal4 activation domain in
RT the mediator.";
RL Biochemistry 40:9421-9427(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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP 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 [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 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 [18]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=16429153; DOI=10.1038/nsmb1049;
RA Fan X., Chou D.M., Struhl K.;
RT "Activator-specific recruitment of Mediator in vivo.";
RL Nat. Struct. Mol. Biol. 13:117-120(2006).
RN [19]
RP CHARACTERIZATION OF THE MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR
RP 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 SER-1034, 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-1034, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-736; SER-752;
RP THR-793; SER-1003; SER-1018 AND SER-1034, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783; SER-785; SER-789;
RP THR-793; SER-831; SER-1003; SER-1008; SER-1018 AND SER-1034, AND
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 [24]
RP INTERACTION WITH GCN4, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 29-MET--ASP-43; 29-MET--SER-39 AND 196-TRP--VAL-199.
RX PubMed=19940160; DOI=10.1074/jbc.m109.071589;
RA Jedidi I., Zhang F., Qiu H., Stahl S.J., Palmer I., Kaufman J.D.,
RA Nadaud P.S., Mukherjee S., Wingfield P.T., Jaroniec C.P., Hinnebusch A.G.;
RT "Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX
RT domain, to recruit mediator to target genes in vivo.";
RL J. Biol. Chem. 285:2438-2455(2010).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
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. It has an important
CC role in the negative regulation of Ty transcription.
CC {ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16109375,
CC 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
CC (PubMed:17192271). The Mediator head module contains MED6, MED8, MED11,
CC SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the
CC middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9,
CC NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains
CC MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16
CC (PubMed:17192271). The head and the middle modules interact directly
CC with RNA polymerase II, whereas the elongated tail module interacts
CC with gene-specific regulatory proteins (PubMed:17192271). GAL11/MED15
CC interacts with the activator GAL4; the interaction is direct
CC (PubMed:11478912). GAL11/MED15 interacts (via multiple regions) with
CC the activator GCN4; the interaction is direct (PubMed:19940160).
CC {ECO:0000269|PubMed:11478912, ECO:0000269|PubMed:17192271,
CC ECO:0000269|PubMed:19940160}.
CC -!- INTERACTION:
CC P19659; P12383: PDR1; NbExp=5; IntAct=EBI-7305, EBI-13019;
CC P19659; P36956-1: SREBF1; Xeno; NbExp=3; IntAct=EBI-7305, EBI-948328;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16630888}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to amino acid starvation
CC (PubMed:19940160). Normal GCN4 protein level during amino acid
CC starvation (PubMed:19940160). {ECO:0000269|PubMed:19940160}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
CC {ECO:0000305}.
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DR EMBL; M22481; AAA34622.1; -; Genomic_DNA.
DR EMBL; Z74793; CAA99056.1; -; Genomic_DNA.
DR EMBL; X91067; CAA62537.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10733.1; -; Genomic_DNA.
DR PIR; S66736; S66736.
DR RefSeq; NP_014591.1; NM_001183305.1.
DR PDB; 2K0N; NMR; -; A=6-90.
DR PDB; 2LPB; NMR; -; A=158-238.
DR PDB; 6ALY; NMR; -; A=277-368.
DR PDBsum; 2K0N; -.
DR PDBsum; 2LPB; -.
DR PDBsum; 6ALY; -.
DR AlphaFoldDB; P19659; -.
DR BMRB; P19659; -.
DR SMR; P19659; -.
DR BioGRID; 34353; 187.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-2334N; -.
DR IntAct; P19659; 20.
DR MINT; P19659; -.
DR STRING; 4932.YOL051W; -.
DR iPTMnet; P19659; -.
DR MaxQB; P19659; -.
DR PaxDb; P19659; -.
DR PRIDE; P19659; -.
DR EnsemblFungi; YOL051W_mRNA; YOL051W; YOL051W.
DR GeneID; 854106; -.
DR KEGG; sce:YOL051W; -.
DR SGD; S000005411; GAL11.
DR VEuPathDB; FungiDB:YOL051W; -.
DR eggNOG; ENOG502QVXD; Eukaryota.
DR HOGENOM; CLU_009962_0_0_1; -.
DR InParanoid; P19659; -.
DR OMA; KYWESMK; -.
DR BioCyc; YEAST:G3O-33462-MON; -.
DR EvolutionaryTrace; P19659; -.
DR PRO; PR:P19659; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P19659; protein.
DR GO; GO:0070847; C:core mediator complex; IDA:SGD.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0001095; F:TFIIE-class transcription factor complex binding; IDA:SGD.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; IDA: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:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
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:0070202; P:regulation of establishment of protein localization to chromosome; IMP:SGD.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:SGD.
DR CDD; cd12191; gal11_coact; 1.
DR Gene3D; 1.10.246.20; -; 1.
DR InterPro; IPR033789; Gal11_coact.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR036546; MED15_KIX.
DR InterPro; IPR008626; Mediator_Med15_fun.
DR Pfam; PF18535; Gal11_ABD1; 1.
DR Pfam; PF16987; KIX_2; 1.
DR Pfam; PF05397; Med15_fungi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1081
FT /note="Mediator of RNA polymerase II transcription subunit
FT 15"
FT /id="PRO_0000096363"
FT REPEAT 422..423
FT /note="1"
FT REPEAT 424..425
FT /note="2"
FT REPEAT 426..427
FT /note="3"
FT REPEAT 428..429
FT /note="4"
FT REPEAT 430..431
FT /note="5"
FT REPEAT 432..433
FT /note="6"
FT REPEAT 434..435
FT /note="7"
FT REPEAT 436..437
FT /note="8"
FT REPEAT 438..439
FT /note="9"
FT REPEAT 440..441
FT /note="10"
FT REPEAT 442..443
FT /note="11"
FT REPEAT 444..445
FT /note="12; approximate"
FT REPEAT 446..447
FT /note="13; approximate"
FT REPEAT 448..449
FT /note="14"
FT REPEAT 450..451
FT /note="15"
FT REPEAT 452..453
FT /note="16"
FT REPEAT 454..455
FT /note="17"
FT REPEAT 456..457
FT /note="18"
FT REPEAT 458..459
FT /note="19"
FT REPEAT 460..461
FT /note="20"
FT REPEAT 462..463
FT /note="21"
FT REPEAT 464..465
FT /note="22"
FT REPEAT 466..467
FT /note="23"
FT REPEAT 468..469
FT /note="24"
FT REPEAT 470..471
FT /note="25"
FT REPEAT 472..473
FT /note="26"
FT REPEAT 474..475
FT /note="27"
FT REPEAT 476..477
FT /note="28"
FT REPEAT 478..479
FT /note="29"
FT REPEAT 480..481
FT /note="30"
FT REGION 25..49
FT /note="Interaction with GCN4"
FT /evidence="ECO:0000269|PubMed:19940160"
FT REGION 238..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..481
FT /note="30 X 2 AA approximate tandem repeats of Q-A"
FT REGION 476..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 793
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 29..43
FT /note="MDINTLNGGSSDTAD->ADIATANGGAADAAA: Decreases the
FT interaction between the mediator complex and GCN4.
FT Decreases transcription of GCN4-dependent targets.
FT Sensitive to amino acid starvation."
FT /evidence="ECO:0000269|PubMed:19940160"
FT MUTAGEN 29..39
FT /note="MDINTLNGGSS->ADIATLNGGAA: Decreases the interaction
FT between the mediator complex and GCN4. Decreases
FT transcription of GCN4-dependent targets. Sensitive to amino
FT acid starvation."
FT /evidence="ECO:0000269|PubMed:19940160"
FT MUTAGEN 196..199
FT /note="WQQV->AQAA: Decreases transcription of GCN4-
FT dependent targets. Decreases recruitment of the mediator
FT complex to the upstream activating sequence (UAS) of amino-
FT acid starvation responsive genes. Sensitive to amino acid
FT starvation."
FT /evidence="ECO:0000269|PubMed:19940160"
FT CONFLICT 171
FT /note="N -> T (in Ref. 1; AAA34622)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="P -> Q (in Ref. 1; AAA34622)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="N -> T (in Ref. 1; AAA34622)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="P -> Q (in Ref. 1; AAA34622)"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2K0N"
FT HELIX 14..35
FT /evidence="ECO:0007829|PDB:2K0N"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:2K0N"
FT HELIX 63..89
FT /evidence="ECO:0007829|PDB:2K0N"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 210..232
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:6ALY"
FT HELIX 302..322
FT /evidence="ECO:0007829|PDB:6ALY"
FT HELIX 330..353
FT /evidence="ECO:0007829|PDB:6ALY"
SQ SEQUENCE 1081 AA; 120309 MW; 275C78721B5415C7 CRC64;
MSAAPVQDKD TLSNAERAKN VNGLLQVLMD INTLNGGSSD TADKIRIHAK NFEAALFAKS
SSKKEYMDSM NEKVAVMRNT YNTRKNAVTA AAANNNIKPV EQHHINNLKN SGNSANNMNV
NMNLNPQMFL NQQAQARQQV AQQLRNQQQQ QQQQQQQQRR QLTPQQQQLV NQMKVAPIPK
QLLQRIPNIP PNINTWQQVT ALAQQKLLTP QDMEAAKEVY KIHQQLLFKA RLQQQQAQAQ
AQANNNNNGL PQNGNINNNI NIPQQQQMQP PNSSANNNPL QQQSSQNTVP NVLNQINQIF
SPEEQRSLLQ EAIETCKNFE KTQLGSTMTE PVKQSFIRKY INQKALRKIQ ALRDVKNNNN
ANNNGSNLQR AQNVPMNIIQ QQQQQNTNNN DTIATSATPN AAAFSQQQNA SSKLYQMQQQ
QQAQAQAQAQ AQAQAQAQAQ AQAAQAAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ
AHAQHQPSQQ PQQAQQQPNP LHGLTPTAKD VEVIKQLSLD ASKTNLRLTD VTNSLSNEEK
EKIKMKLKQG QKLFVQVSNF APQVYIITKN ENFLKEVFQL RIFVKEILEK CAEGIFVVKL
DTVDRLIIKY QKYWESMRIQ ILRRQAILRQ QQQMANNNGN PGTTSTGNNN NIATQQNMQQ
SLQQMQHLQQ LKMQQQQQQQ QQQQQQQQQQ QQQQQQHIYP SSTPGVANYS AMANAPGNNI
PYMNHKNTSS MDFLNSMENT PKVPVSAAAT PSLNKTINGK VNGRTKSNTI PVTSIPSTNK
KLSISNAASQ QPTPRSASNT AKSTPNTNPS PLKTQTKNGT PNPNNMKTVQ SPMGAQPSYN
SAIIENAFRK EELLLKDLEI RKLEISSRFK HRQEIFKDSP MDLFMSTLGD CLGIKDEEML
TSCTIPKAVV DHINGSGKRK PTKAAQRARD QDSIDISIKD NKLVMKSKFN KSNRSYSIAL
SNVAAIFKGI GGNFKDLSTL VHSSSPSTSS NMDVGNPRKR KASVLEISPQ DSIASVLSPD
SNIMSDSKKI KVDSPDDPFM TKSGATTSEK QEVTNEAPFL TSGTSSEQFN VWDWNNWTSA
T
