MED31_YEAST
ID MED31_YEAST Reviewed; 127 AA.
AC P38633; D6VU21;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 31;
DE AltName: Full=Hpr1 suppressor protein 1;
DE AltName: Full=Mediator complex subunit 31;
GN Name=SOH1; Synonyms=MED31; OrderedLocusNames=YGL127C; ORFNames=G2864;
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 200060 / W303;
RX PubMed=7982575; DOI=10.1093/genetics/137.4.945;
RA Fan H.-Y., Klein H.L.;
RT "Characterization of mutations that suppress the temperature-sensitive
RT growth of the hpr1 delta mutant of Saccharomyces cerevisiae.";
RL Genetics 137:945-956(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8686378;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<145::aid-yea888>3.0.co;2-e;
RA Rodriguez-Belmonte E., Rodriguez Torres A.M., Tizon B., Cadahia J.L.,
RA Gonzalez-Siso I., Ramil E., Becerra M., Gonzalez-Dominguez M., Cerdan E.;
RT "Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII
RT reveals a novel member of the DnaJ family.";
RL Yeast 12:145-148(1996).
RN [3]
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 [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 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 [7]
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 [8]
RP COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=15356001; DOI=10.1074/jbc.m409046200;
RA Linder T., Gustafsson C.M.;
RT "The Soh1/MED31 protein is an ancient component of Schizosaccharomyces
RT pombe and Saccharomyces cerevisiae Mediator.";
RL J. Biol. Chem. 279:49455-49459(2004).
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 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: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.
CC -!- INTERACTION:
CC P38633; Q12321: MED1; NbExp=2; IntAct=EBI-17658, EBI-32854;
CC P38633; Q06213: NUT2; NbExp=3; IntAct=EBI-17658, EBI-12414;
CC P38633; P32569: SRB4; NbExp=4; IntAct=EBI-17658, EBI-18025;
CC P38633; P47822: SRB7; NbExp=3; IntAct=EBI-17658, EBI-18046;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 31 family.
CC {ECO:0000305}.
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DR EMBL; L31921; AAA35066.1; -; Genomic_DNA.
DR EMBL; X87252; CAA60704.1; -; Genomic_DNA.
DR EMBL; Z72649; CAA96836.1; -; Genomic_DNA.
DR EMBL; AY693006; AAT93025.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07982.1; -; Genomic_DNA.
DR PIR; S47895; S47895.
DR RefSeq; NP_011388.1; NM_001180992.1.
DR PDB; 3FBI; X-ray; 2.80 A; B/D=1-127.
DR PDB; 3FBN; X-ray; 3.01 A; B/D=1-127.
DR PDB; 5OQM; EM; 5.80 A; o=1-127.
DR PDB; 5SVA; EM; 15.30 A; X=1-127.
DR PDBsum; 3FBI; -.
DR PDBsum; 3FBN; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR AlphaFoldDB; P38633; -.
DR SMR; P38633; -.
DR BioGRID; 33124; 362.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-1179N; -.
DR IntAct; P38633; 29.
DR MINT; P38633; -.
DR STRING; 4932.YGL127C; -.
DR PaxDb; P38633; -.
DR PRIDE; P38633; -.
DR EnsemblFungi; YGL127C_mRNA; YGL127C; YGL127C.
DR GeneID; 852750; -.
DR KEGG; sce:YGL127C; -.
DR SGD; S000003095; SOH1.
DR VEuPathDB; FungiDB:YGL127C; -.
DR eggNOG; KOG4086; Eukaryota.
DR GeneTree; ENSGT00390000015531; -.
DR HOGENOM; CLU_147521_0_0_1; -.
DR InParanoid; P38633; -.
DR OMA; YLEYWCE; -.
DR BioCyc; YEAST:G3O-30623-MON; -.
DR EvolutionaryTrace; P38633; -.
DR PRO; PR:P38633; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P38633; 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:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IPI:SGD.
DR GO; GO:0006311; P:meiotic gene conversion; 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 GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR Gene3D; 1.10.10.1340; -; 1.
DR InterPro; IPR038089; Med31_sf.
DR InterPro; IPR008831; Mediator_Med31.
DR PANTHER; PTHR13186; PTHR13186; 1.
DR Pfam; PF05669; Med31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..127
FT /note="Mediator of RNA polymerase II transcription subunit
FT 31"
FT /id="PRO_0000212534"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:3FBI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3FBI"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3FBI"
SQ SEQUENCE 127 AA; 14741 MW; A2FE3B62ADC14011 CRC64;
MSSTNGNAPA TPSSDQNPLP TRFEVELEFI QSLANIQYVT YLLTQQQIWK SPNFKNYLKY
LEYWCNPPYS QCIVYPNCLF ILKLLNGFME SAIVNEDGLL EGLDELPKII QLQGPQWMNE
MVERWAN
