TAF2_YEAST
ID TAF2_YEAST Reviewed; 1407 AA.
AC P23255; D6VR51;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Transcription initiation factor TFIID subunit 2;
DE AltName: Full=TAFII-150;
DE AltName: Full=TBP-associated factor 150 kDa;
DE AltName: Full=TBP-associated factor 2;
DE AltName: Full=TSM-1;
GN Name=TAF2; Synonyms=TAF150, TSM1; OrderedLocusNames=YCR042C;
GN ORFNames=YCR42C, YCR724;
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=1789011; DOI=10.1002/yea.320070815;
RA Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C.,
RA Soustelle C.;
RT "The MAT locus revisited within a 9.8 kb fragment of chromosome III
RT containing BUD5 and two new open reading frames.";
RL Yeast 7:881-888(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RY570;
RX PubMed=1840512; DOI=10.1007/bf00312761;
RA Ray B.L., White C.I., Haber J.E.;
RT "The TSM1 gene of Saccharomyces cerevisiae overlaps the MAT locus.";
RL Curr. Genet. 20:25-31(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 PROTEIN SEQUENCE OF 165-174 AND 991-1000, AND CHARACTERIZATION.
RC STRAIN=ATCC 76621 / YPH252;
RX PubMed=7667272; DOI=10.1073/pnas.92.18.8224;
RA Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S.,
RA Kornberg R.D., Weil P.A.;
RT "Identification and characterization of a TFIID-like multiprotein complex
RT from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10788514; DOI=10.1074/jbc.275.18.13895;
RA Sanders S.L., Weil P.A.;
RT "Identification of two novel TAF subunits of the yeast Saccharomyces
RT cerevisiae TFIID complex.";
RL J. Biol. Chem. 275:13895-13900(2000).
RN [7]
RP FUNCTION, AND TFIID STOICHIOMETRY.
RX PubMed=12138208; DOI=10.1128/mcb.22.16.6000-6013.2002;
RA Sanders S.L., Garbett K.A., Weil P.A.;
RT "Molecular characterization of Saccharomyces cerevisiae TFIID.";
RL Mol. Cell. Biol. 22:6000-6013(2002).
RN [8]
RP FUNCTION.
RX PubMed=12516863; DOI=10.1023/a:1021258713850;
RA Martinez E.;
RT "Multi-protein complexes in eukaryotic gene transcription.";
RL Plant Mol. Biol. 50:925-947(2002).
RN [9]
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 [10]
RP 3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID.
RX PubMed=12093743; DOI=10.1093/emboj/cdf342;
RA Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A.,
RA Kirschner D.B., Tora L., Schultz P.;
RT "Mapping histone fold TAFs within yeast TFIID.";
RL EMBO J. 21:3424-3433(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158; THR-161 AND SER-163, 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).
CC -!- FUNCTION: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID. Binding of TFIID to a promoter
CC (with or without TATA element) is the initial step in pre-initiation
CC complex (PIC) formation. TFIID plays a key role in the regulation of
CC gene expression by RNA polymerase II through different activities such
CC as transcription activator interaction, core promoter recognition and
CC selectivity, TFIIA and TFIIB interaction, chromatin modification
CC (histone acetylation by TAF1), facilitation of DNA opening and
CC initiation of transcription. {ECO:0000269|PubMed:10788514,
CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863}.
CC -!- SUBUNIT: The 1.2 MDa TFIID complex is composed of TATA binding protein
CC (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2,
CC TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6,
CC TAF9, TAF10, TAF12, and three copies of TAF14.
CC {ECO:0000269|PubMed:10788514}.
CC -!- INTERACTION:
CC P23255; P46677: TAF1; NbExp=4; IntAct=EBI-18862, EBI-18855;
CC P23255; P38129: TAF5; NbExp=9; IntAct=EBI-18862, EBI-18868;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF2 family. {ECO:0000305}.
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DR EMBL; X63853; CAA45337.1; -; Genomic_DNA.
DR EMBL; M60486; AAA35179.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42290.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07520.1; -; Genomic_DNA.
DR PIR; S19455; BWBYM1.
DR RefSeq; NP_009971.1; NM_001178756.1.
DR AlphaFoldDB; P23255; -.
DR SMR; P23255; -.
DR BioGRID; 31024; 48.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-343N; -.
DR IntAct; P23255; 19.
DR MINT; P23255; -.
DR STRING; 4932.YCR042C; -.
DR iPTMnet; P23255; -.
DR MaxQB; P23255; -.
DR PaxDb; P23255; -.
DR PRIDE; P23255; -.
DR EnsemblFungi; YCR042C_mRNA; YCR042C; YCR042C.
DR GeneID; 850409; -.
DR KEGG; sce:YCR042C; -.
DR SGD; S000000638; TAF2.
DR VEuPathDB; FungiDB:YCR042C; -.
DR eggNOG; KOG1932; Eukaryota.
DR GeneTree; ENSGT00390000000420; -.
DR HOGENOM; CLU_002317_2_0_1; -.
DR InParanoid; P23255; -.
DR OMA; APHHIGW; -.
DR BioCyc; YEAST:G3O-29353-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR PRO; PR:P23255; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P23255; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR037813; TAF2.
DR PANTHER; PTHR15137; PTHR15137; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1407
FT /note="Transcription initiation factor TFIID subunit 2"
FT /id="PRO_0000118867"
FT REGION 252..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1350
FT /note="Highly charged"
FT COILED 304..337
FT /evidence="ECO:0000255"
FT COMPBIAS 272..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 323
FT /note="E -> G (in Ref. 2; AAA35179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1407 AA; 161471 MW; 184C8ED735443F38 CRC64;
MMSFSKNATP RAIVSESSTL HEMKFRNFRV AHEKISLDID LATHCITGSA TIIIIPLIQN
LEYVTFDCKE MTIKDVLVEN RRCDQFIHDD PLQTNLNGLT SQNVLYSDNS IEQSHFLRSK
FASLNEYPET DSKSQLTIKI PSSIKISLED ANALSNYTPI TPSIKTTPGF QESVFTPITL
QIEYEIRNPK SGIKFDTVYA DKPWLWNVYT SNGEICSSAS YWVPCVDLLD EKSTWELEFS
VPRLVKNIGT SKLIGQNGEE SEKEKEDTPE HDEEEEGKPA RVIKDEDKDS NLKNDEEGKN
SKSKDAQDND EEEEEGESDE EEEEGEEERR NIEESNNPSL RDVIVCCSEY SNIKELPHPI
DLTKKKCIFQ IINPVAPHHI GWAIGAFNSW SLPLISPPSV DAEDEVEEDK LRENVVDNVN
DTMDDDIGSD IIPIQIFTLP TQETDELTVI NSTVVCQKII DFYSKEFGSY PFTCYSMVFL
PTAPSKHMDF AALGICNTRL LYPLEVIDKA FSTTNELAWA LANQWSCVNI TPLDMNDYWC
CLGIAGYMVF QVTKKLMGNN TYKYQLKRNS EAIVEQDFEK PPIGSTFTGS SRPISWSSKD
LSFIQLKAPM ILHILDRRMT KTERSFGMSR VLPKIFLQAM SGDLPNNSLT SSHFQHVCER
VNKSKLENFF NEWVYGSGVP ILRVTQRFNR KRMVIELGIR QVQDEELGHE KVVGEEGFFK
SALDHLEHPD LNRTECFTGS MTIRIHEHDG TPYEHIVEIK DTFTKIDIQY NTKYRRLRKR
GGGANDENGV ENNNEEKPIV VDVNCLGNVY MSPEECSRFS LTEFNRTSES NELLKQNEAF
EWIRIDSDLE WICQMHINQP DYMFSSQLRQ DGDIEAQLEA IRYYEDVVVN GGVKSLVYSS
ILFRTAIDER YFFGIRLAAC EALSKYVYDP DFTGGVKHLI QIFQILFCLE DSNIPKSNNF
ENPKLYFLQC NIPKYLAKVK NENGKCPKLV KQFLLDILVY NENGENKYSD DAYVRSLIEN
VVKVALNEYK DKAYMEKVKT QLLRYENLVN WLSSYESLIK TTIMYAKYKL HKVGAYDFTE
LTGMIMHTLT LGINNGDISR ESFQNEFLMV LKIMLLEGGL KNKDALVLFT EILCFHEDSY
IRDKSVDVLS ECVNLVVMDG SLDTISDDIK SSVQSVHNEV KNIKSEDDIE LFLSGHYVDD
MKIKIEKIGR QNISGLIQIC RDMFKGYSPL KILLWDVLNL PVLSLYQRKQ IHDLVRVMYT
LINSFVVRLE TPRERRLVAK MNSNEEGKLD IVIKRESILK VHIKKEVTST VEAPKKANKI
KISLKGDKPV RKVEKQIVKP KVTSKQRKVK SHVNRMGSLP LRFVKIQQQP RVMVHLSSVP
YSQFVQITKV TSRSFMVKIR TKNDAKN
