ID MED20_YEAST Reviewed; 210 AA.
AC P34162; D3DKY9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 27-MAR-2024, entry version 181.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 20;
DE AltName: Full=Hyper-recombination suppressor protein 2;
DE AltName: Full=Mediator complex subunit 20;
DE AltName: Full=Suppressor of RNA polymerase B 2;
GN Name=SRB2; Synonyms=HRS2, MED20; OrderedLocusNames=YHR041C;
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 PRO-14.
RX PubMed=1591782; DOI=10.1016/0092-8674(92)90298-q;
RA Koleske A.J., Buratowski S., Nonet M., Young R.A.;
RT "A novel transcription factor reveals a functional link between the RNA
RT polymerase II CTD and TFIID.";
RL Cell 69:883-894(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 CHARACTERIZATION.
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 [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 INTERACTION WITH SRB4 AND SRB5.
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 [7]
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 [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 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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17]
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 [18]
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 MED8; SRB4
RP AND SRB5.
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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-210 IN COMPLEX WITH MED8 AND
RP SRB5, AND X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SRB5.
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:16076843,
CC ECO:0000269|PubMed:16109375, ECO:0000269|PubMed:16263706,
CC ECO:0000269|PubMed:16885025}.
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. MED1 interacts
CC directly with MED4 and MED7. SRB2/MED20 interacts directly with
CC SRB4/MED17 and SRB5/MED18. {ECO:0000269|PubMed:16885025,
CC ECO:0000269|PubMed:16964259, ECO:0000269|PubMed:17192271,
CC ECO:0000269|PubMed:9660972}.
CC -!- INTERACTION:
CC P34162; P32585: SRB5; NbExp=6; IntAct=EBI-18018, EBI-18032;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 20 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S36754; AAB22223.1; -; Genomic_DNA.
DR EMBL; U00062; AAB68920.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06733.1; -; Genomic_DNA.
DR PIR; A38105; A38105.
DR RefSeq; NP_011907.1; NM_001179171.1.
DR PDB; 2HZM; X-ray; 2.40 A; A/C/E/G=1-210.
DR PDB; 2HZS; X-ray; 2.70 A; A/C/E/G=2-210.
DR PDB; 3J1O; EM; 16.00 A; M=1-210.
DR PDB; 3RJ1; X-ray; 4.30 A; F/M/T=1-210.
DR PDB; 4GWP; X-ray; 4.20 A; F=1-210.
DR PDB; 4GWQ; X-ray; 4.50 A; F=1-210.
DR PDB; 4V1O; EM; 9.70 A; Y=2-210.
DR PDB; 5OQM; EM; 5.80 A; f=1-210.
DR PDB; 5SVA; EM; 15.30 A; R=1-210.
DR PDB; 7UI9; EM; 3.30 A; t=1-210.
DR PDB; 7UIF; EM; 4.60 A; t=1-210.
DR PDB; 7UIG; EM; 4.30 A; t=1-210.
DR PDB; 7UIO; EM; 3.30 A; At/Bt=1-210.
DR PDB; 8CEO; EM; 3.60 A; f=1-210.
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 PDBsum; 7UI9; -.
DR PDBsum; 7UIF; -.
DR PDBsum; 7UIG; -.
DR PDBsum; 7UIO; -.
DR PDBsum; 8CEO; -.
DR AlphaFoldDB; P34162; -.
DR EMDB; EMD-26542; -.
DR EMDB; EMD-26544; -.
DR EMDB; EMD-26551; -.
DR EMDB; EMD-2786; -.
DR EMDB; EMD-3850; -.
DR EMDB; EMD-8305; -.
DR SMR; P34162; -.
DR BioGRID; 36473; 676.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-107N; -.
DR IntAct; P34162; 23.
DR MINT; P34162; -.
DR STRING; 4932.YHR041C; -.
DR MaxQB; P34162; -.
DR PaxDb; 4932-YHR041C; -.
DR PeptideAtlas; P34162; -.
DR EnsemblFungi; YHR041C_mRNA; YHR041C; YHR041C.
DR GeneID; 856437; -.
DR KEGG; sce:YHR041C; -.
DR AGR; SGD:S000001083; -.
DR SGD; S000001083; SRB2.
DR VEuPathDB; FungiDB:YHR041C; -.
DR eggNOG; ENOG502RXMU; Eukaryota.
DR HOGENOM; CLU_065844_1_0_1; -.
DR InParanoid; P34162; -.
DR OMA; QRQSIKG; -.
DR OrthoDB; 2041863at2759; -.
DR BioCyc; YEAST:G3O-31100-MONOMER; -.
DR BioGRID-ORCS; 856437; 1 hit in 10 CRISPR screens.
DR EvolutionaryTrace; P34162; -.
DR PRO; PR:P34162; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P34162; 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:0019904; F:protein domain specific binding; IGI:SGD.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0010688; P:negative regulation of ribosomal protein gene transcription by RNA polymerase II; 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 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: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 Gene3D; 3.30.310.180; -; 2.
DR InterPro; IPR016532; Med20.
DR InterPro; IPR013921; Mediator_Med20.
DR Pfam; PF08612; Med20; 1.
DR PIRSF; PIRSF007945; SRB2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..210
FT /note="Mediator of RNA polymerase II transcription subunit
FT 20"
FT /id="PRO_0000096374"
FT MUTAGEN 14
FT /note="P->H: In SRB2-1; suppresses the phenotypic defects
FT of an RNA polymerase II CTD truncation."
FT /evidence="ECO:0000269|PubMed:1591782"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2HZS"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2HZS"
FT STRAND 56..73
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:2HZM"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 116..132
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:2HZM"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2HZM"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:2HZM"
SQ SEQUENCE 210 AA; 22894 MW; C30BF309D43AFB2A CRC64;
MGKSAVIFVE RATPATLTEL KDALSNSILS VRDPWSIDFR TYRCSIKNLP ADVSKLMYSI
TFHHHGRQTV LIKDNSAMVT TAAAADIPPA LVFNGSSTGV PESIDTILSS KLSNIWMQRQ
LIKGDAGETL ILDGLTVRLV NLFSSTGFKG LLIELQADEA GEFETKIAGI EGHLAEIRAK
EYKTSSDSLG PDTSNEICDL AYQYVRALEL
//
