MED16_YEAST
ID MED16_YEAST Reviewed; 974 AA.
AC P32259; D6W0V7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 16;
DE AltName: Full=Global transcriptional regulator SIN4;
DE AltName: Full=Mediator complex subunit 16;
DE AltName: Full=SNF1 suppressor protein 4;
DE AltName: Full=SWI4 suppressor protein 5;
DE AltName: Full=Transcriptional silencing factor 3;
DE AltName: Full=YGP1 expression regulatory protein 1;
GN Name=SIN4; Synonyms=BEL2, GAL22, MED16, RYE1, SDI3, SSF5, SSN4, TSF3;
GN OrderedLocusNames=YNL236W; ORFNames=N1135;
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=YM256;
RX PubMed=8423805; DOI=10.1128/mcb.13.2.831-840.1993;
RA Chen S., West R.W. Jr., Johnson S.L., Gans H., Kruger B., Ma J.;
RT "TSF3, a global regulatory protein that silences transcription of yeast GAL
RT genes, also mediates repression by alpha 2 repressor and is identical to
RT SIN4.";
RL Mol. Cell. Biol. 13:831-840(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1406639; DOI=10.1128/mcb.12.10.4503-4514.1992;
RA Jiang Y.W., Stillman D.J.;
RT "Involvement of the SIN4 global transcriptional regulator in the chromatin
RT structure of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:4503-4514(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Harashima S., Mabuchi H., Ramash R., Hasebe M., Tanaka A., Oshima Y.;
RT "BEL2/SIN4/TSF3 encodes a position-dependent general repressor of a diverse
RT set of genes in yeast.";
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
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 [6]
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 [7]
RP COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=7479899; DOI=10.1073/pnas.92.24.10864;
RA Li Y., Bjoerklund S., Jiang Y.W., Kim Y.-J., Lane W.S., Stillman D.J.,
RA Kornberg R.D.;
RT "Yeast global transcriptional regulators Sin4 and Rgr1 are components of
RT mediator complex/RNA polymerase II holoenzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10864-10868(1995).
RN [8]
RP INTERACTION WITH HOG1.
RX PubMed=12743037; DOI=10.1093/emboj/cdg243;
RA Alepuz P.M., de Nadal E., Zapater M., Ammerer G., Posas F.;
RT "Osmostress-induced transcription by Hot1 depends on a Hog1-mediated
RT recruitment of the RNA Pol II.";
RL EMBO J. 22:2433-2442(2003).
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 PHOSPHORYLATION BY KIN28.
RX PubMed=14749387; DOI=10.1128/mcb.24.4.1721-1735.2004;
RA Liu Y., Kung C., Fishburn J., Ansari A.Z., Shokat K.M., Hahn S.;
RT "Two cyclin-dependent kinases promote RNA polymerase II transcription and
RT formation of the scaffold complex.";
RL Mol. Cell. Biol. 24:1721-1735(2004).
RN [13]
RP STRUCTURE 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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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. Interacts with
CC HOG1. {ECO:0000269|PubMed:12743037, ECO:0000269|PubMed:17192271}.
CC -!- INTERACTION:
CC P32259; P53114: NUT1; NbExp=4; IntAct=EBI-17172, EBI-12407;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by KIN28. {ECO:0000269|PubMed:14749387}.
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 16 family.
CC {ECO:0000305}.
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DR EMBL; M93050; AAA35044.1; -; Genomic_DNA.
DR EMBL; X64516; CAA45819.1; -; Genomic_DNA.
DR EMBL; D12918; BAA02302.1; -; Genomic_DNA.
DR EMBL; Z69381; CAA93362.1; -; Genomic_DNA.
DR EMBL; Z71512; CAA96140.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10323.1; -; Genomic_DNA.
DR PIR; A44484; A44484.
DR RefSeq; NP_014163.1; NM_001183074.1.
DR AlphaFoldDB; P32259; -.
DR BioGRID; 35603; 601.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-1617N; -.
DR IntAct; P32259; 43.
DR MINT; P32259; -.
DR STRING; 4932.YNL236W; -.
DR MaxQB; P32259; -.
DR PaxDb; P32259; -.
DR PRIDE; P32259; -.
DR EnsemblFungi; YNL236W_mRNA; YNL236W; YNL236W.
DR GeneID; 855485; -.
DR KEGG; sce:YNL236W; -.
DR SGD; S000005180; SIN4.
DR VEuPathDB; FungiDB:YNL236W; -.
DR eggNOG; ENOG502QWAC; Eukaryota.
DR HOGENOM; CLU_311703_0_0_1; -.
DR InParanoid; P32259; -.
DR OMA; WYQFSNS; -.
DR BioCyc; YEAST:G3O-33235-MON; -.
DR PRO; PR:P32259; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32259; protein.
DR GO; GO:0070847; C:core mediator complex; IDA:SGD.
DR GO; GO:0016592; C:mediator complex; IDA:SGD.
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: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 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:ComplexPortal.
DR InterPro; IPR021665; Mediator_Med16.
DR Pfam; PF11635; Med16; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..974
FT /note="Mediator of RNA polymerase II transcription subunit
FT 16"
FT /id="PRO_0000096364"
FT REGION 62..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 889..893
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 974 AA; 111297 MW; 12ECF5E4CDC05A8E CRC64;
MMLGEHLMSW SKTGIIAYSD SQSSNANICL TFLESINGIN WRFHTPQKYV LHPQLHEVQY
QESSSTLSTH STTTSVNGST TAGVGSTPNF GGNSNKSPPQ FFYNISSIHW NNWFSLPGDM
LAVCDELGNM TMLITGQRPD RATTYEKLTM VFQDNVYKIY NHVMPLKPVD KLKPMNIERK
QTRKEYNTSI LEFRWLTSSK SVIVSQFCAF DSSSNTYRSR AQQVPPYGVY HPPFIKYACL
AIRKNGQIDF WYQFSNSKDH KKITLQLLDT SNQRFKDLQW LEFARITPMN DDQCMLITTY
SKLSKNISFY KLHVNWNLNA TKPNVLNDPS LKIQFILSTT LDPTDDEGHV LKLENLHVVS
KSSIEKDPSP EILVLYNVCD TSKSLVKRYR LAPTQLSAEY LVILKPDLNI DRNNSTNQIF
QSRRYNLRRH SDIVLDKKVT LITSEMFDAF VSFYFEDGTI ESYNQNDWKL ETERLISQSQ
LGKFKNIIAS PLSAGFNYGK LPLPPSVEWM KVSPSMCGVI VKQYNKKWPQ FYAAVQKNYA
DPEKDSINAT ALAFGYVKSL HKQISAEDLT IAAKTHILRI SFLDRKRAKE FITTLLKSLY
SFFNISPDAP KEIMDKIITS RPLQKIMLLQ LELGSCFSQE NIEEMARVIL YLKNVLFAFN
GVARNFHFAI EQISNNSNQQ QNPKLFQTIF SKQDLIHSLI PVAKWFVKFI TYLTQEILIL
INDPTNKEYT LVHGIFGAKM SRTLILSILN EIKKVTQIVA KFPETSYPIL NESSTFLKLV
LSESPVDFEK FETFLVDVNN KFIALCEQQP SQEREFSLLV KAEIPPEYAK VGDFLLQYAN
NAVISHANAA AVYFADTSGL KISNSEFFNP EIFHLLQPLE EGLIIDTDKL PIKNRTSKSF
SKLLYDDVTC DKLSVSEISD GKLKRCSRCG SVTRAGNIIS SDKTIVPTSI QTKRWPTMYT
RLCICSGMLF EMDG
