MED5_YEAST
ID MED5_YEAST Reviewed; 1132 AA.
AC P53114; D6VTZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 5;
DE AltName: Full=Mediator complex subunit 5;
DE AltName: Full=Negative regulator of URS2 protein 1;
GN Name=NUT1; Synonyms=MED5; OrderedLocusNames=YGL151W; ORFNames=G1876;
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=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
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 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 [5]
RP FUNCTION.
RX PubMed=9671481; DOI=10.1128/mcb.18.8.4707;
RA Tabtiang R.K., Herskowitz I.;
RT "Nuclear proteins Nut1p and Nut2p cooperate to negatively regulate a Swi4p-
RT dependent lacZ reporter gene in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 18:4707-4718(1998).
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 ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=14623974; DOI=10.1073/pnas.2036346100;
RA Kuras L., Borggrefe T., Kornberg R.D.;
RT "Association of the Mediator complex with enhancers of active genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13887-13891(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 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 [16]
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 [17]
RP IDENTIFICATION BY MASS 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 [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 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:9671481}.
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 {ECO:0000269|PubMed:17192271}.
CC -!- INTERACTION:
CC P53114; Q12321: MED1; NbExp=3; IntAct=EBI-12407, EBI-32854;
CC P53114; P32259: SIN4; NbExp=4; IntAct=EBI-12407, EBI-17172;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2491 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 5 family.
CC {ECO:0000305}.
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DR EMBL; Z48618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z72673; CAA96863.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07960.1; -; Genomic_DNA.
DR PIR; S60433; S60433.
DR RefSeq; NP_011364.1; NM_001181016.1.
DR AlphaFoldDB; P53114; -.
DR BioGRID; 33102; 622.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-6632N; -.
DR IntAct; P53114; 32.
DR MINT; P53114; -.
DR STRING; 4932.YGL151W; -.
DR iPTMnet; P53114; -.
DR MaxQB; P53114; -.
DR PaxDb; P53114; -.
DR PRIDE; P53114; -.
DR EnsemblFungi; YGL151W_mRNA; YGL151W; YGL151W.
DR GeneID; 852726; -.
DR KEGG; sce:YGL151W; -.
DR SGD; S000003119; NUT1.
DR VEuPathDB; FungiDB:YGL151W; -.
DR eggNOG; ENOG502R1HB; Eukaryota.
DR HOGENOM; CLU_281615_0_0_1; -.
DR InParanoid; P53114; -.
DR OMA; FTCFAQF; -.
DR BioCyc; YEAST:G3O-30643-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR PRO; PR:P53114; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53114; protein.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0043966; P:histone H3 acetylation; 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; IMP:SGD.
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 InterPro; IPR014801; Mediator_Med5_fun.
DR PANTHER; PTHR35784; PTHR35784; 1.
DR Pfam; PF08689; Med5; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1132
FT /note="Mediator of RNA polymerase II transcription subunit
FT 5"
FT /id="PRO_0000096387"
FT REGION 998..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 128794 MW; BBD54661A4DB5F09 CRC64;
MEKESVYNLA LKCAERQLTS MEFSNLYKEF FNEKFPSLIQ EEEEDTTTTA NINEVKKASD
LVDTPSNNTA ATADTTHLHE ALDIVCSDFV KILNLEKPLI LADYIVEVLL VNYNSDMIKC
FLPKLNSVRN SLLLAHFFSK SCSFFAKLSD TLIIDQVRKD LGNVIVPNIL SLDMNSMNKE
LIAIVSKLLQ TTLKLSPSPI LLTSAGCKNG SFTLLNQLSQ TNKLLFKRVS QTFEAKLHFK
DTKPFLNKDS TNEFVGSPSL TSPQYIPSPL SSTKPPGSVN SAAKYKDMKL LRYYKNIWLN
NKIINWEISN PDFLSKYSAI TSSIFQESFN SVQNLDQLLT DLIETSFTCF AQFVSNKQYH
QANSNLTLLE RKWVIFITKH LPLLILENSS RSPRVVTNAL DNIDEKVVKA IRIYFTEKDD
NKTNNEDLFD DYPSTSLDIR HDFIKGLIML NLQPASVINN YLREDQMIDT SILPTRDDLF
VRNLQGIQEV VHNTNSFIIS SLDTLELESI TESITHDSSN GLFQVLHNFE SVAPTKQREI
VKAFLSIFED AIKELNYNRI AKICALLFFN FSHSLTTILS FSSPAALMKT LIKFVDLSRN
GRNGSNGNDE SSEYETINIS LSFSWAILLI INLTQTYGIS VVDVALKYPE LSIKNSFIIN
FISNLPNVSD KYYLEESNVN DSDMLTKSHN TVQSWLCDLF VNGSITDQLI QNIETRQLAN
LIPFIVKQVL LSVEIGVLTD ISSLIGGFEY FLQPLLLVGL IKTFYWLEQF LSCVKNDTIS
EDILQGIFNL LNTLFNPVTL NEDSKAFHTA VLRLNAIPLL KVLRKFRVQS QSNYGIYSSD
AQGDPNLEPL IAKLVAVLNV SPVYDVDPRI INSENDYSRK QLGYGKFLIL NENPINKIMT
NQINSFWSLH SSTYYNLDYL FELIELVTPK SFLFDVLKTL EYKLATYGVP GSENKRGSLD
SEHVFDYFFY FLVLYDVKTA EEASQLIEYM ENDAKKSKGD VDIKGEDLHE KNDSAEVRQE
TQPKAEATQD DDFDMLFGEN DTSTQAYEEE EENEDNDGNN RTNNVPMIKA EETPSKTNKI
SILKRHSFAV LLHERKLLND LALENGEITK TENEKFISYH DKYLCMLKTC VF
