TAF8_YEAST
ID TAF8_YEAST Reviewed; 510 AA.
AC Q03750; D6W0H0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transcription initiation factor TFIID subunit 8;
DE AltName: Full=TAFII-65;
DE AltName: Full=TBP-associated factor 65 kDa;
DE AltName: Full=TBP-associated factor 8;
GN Name=TAF8; Synonyms=TAF65; OrderedLocusNames=YML114C; ORFNames=YM8339.05C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP FUNCTION, AND TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
RX PubMed=9695952; DOI=10.1016/s0092-8674(00)81423-3;
RA Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C.,
RA Davidson I., Moras D.;
RT "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by
RT atypical evolutionary conserved motifs also found in the SPT3 family.";
RL Cell 94:239-249(1998).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION IN TFIID AND SAGA.
RX PubMed=11238921; DOI=10.1128/mcb.21.5.1841-1853.2001;
RA Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., Tora L.,
RA Davidson I.;
RT "Histone folds mediate selective heterodimerization of yeast TAF(II)25 with
RT TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7.";
RL Mol. Cell. Biol. 21:1841-1853(2001).
RN [6]
RP FUNCTION, AND HISTONE-FOLD DOMAIN CHARACTERIZATION.
RX PubMed=11295558; DOI=10.1016/s0968-0004(00)01741-2;
RA Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.;
RT "The histone fold is a key structural motif of transcription factor
RT TFIID.";
RL Trends Biochem. Sci. 26:250-257(2001).
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 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 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, 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 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).
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:11238921, ECO:0000269|PubMed:11295558,
CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863,
CC ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: In TFIID, TAF8 heterodimerizes with TAF10. The 1.2 MDa TFIID
CC complex is composed of TATA binding protein (TBP) and the 14 TBP-
CC associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8,
CC TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12,
CC and three copies of TAF14. {ECO:0000269|PubMed:10788514}.
CC -!- INTERACTION:
CC Q03750; Q12030: TAF10; NbExp=7; IntAct=EBI-27947, EBI-18889;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4684 (+/-522) molecules/cell in log phase
CC SD medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF8 family. {ECO:0000305}.
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DR EMBL; Z49210; CAA89104.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09784.1; -; Genomic_DNA.
DR PIR; S53958; S53958.
DR RefSeq; NP_013593.1; NM_001182476.1.
DR AlphaFoldDB; Q03750; -.
DR SMR; Q03750; -.
DR BioGRID; 35090; 299.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-1954N; -.
DR IntAct; Q03750; 21.
DR MINT; Q03750; -.
DR STRING; 4932.YML114C; -.
DR iPTMnet; Q03750; -.
DR MaxQB; Q03750; -.
DR PaxDb; Q03750; -.
DR PRIDE; Q03750; -.
DR EnsemblFungi; YML114C_mRNA; YML114C; YML114C.
DR GeneID; 854926; -.
DR KEGG; sce:YML114C; -.
DR SGD; S000004582; TAF8.
DR VEuPathDB; FungiDB:YML114C; -.
DR eggNOG; KOG4336; Eukaryota.
DR HOGENOM; CLU_529078_0_0_1; -.
DR InParanoid; Q03750; -.
DR OMA; YTRIQRR; -.
DR BioCyc; YEAST:G3O-32696-MON; -.
DR PRO; PR:Q03750; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03750; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
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 CDD; cd08049; TAF8; 1.
DR InterPro; IPR037818; TAF8.
DR InterPro; IPR019473; TFIID_su8_C.
DR PANTHER; PTHR46338; PTHR46338; 1.
DR Pfam; PF10406; TAF8_C; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..510
FT /note="Transcription initiation factor TFIID subunit 8"
FT /id="PRO_0000118887"
FT DOMAIN 37..103
FT /note="Histone-fold"
FT REGION 361..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..165
FT /evidence="ECO:0000255"
FT COILED 346..383
FT /evidence="ECO:0000255"
FT COMPBIAS 459..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 510 AA; 57986 MW; A6393C86D0E890CE CRC64;
MTSKTSESGT GTQSTIVQLR NLPDLTEISH LEIDAPVVEI LKKTVLFQLN SLNICISNFA
LDELVNLVTV QMDGMFRNLH NLTLLQRRSQ ASQADLKLLL REFNLDAPSL YQQFQASEFI
KSKHSTEYEK LMSWSSLAAL PHNEEDEEDE LNNIEEQQNE INVLLPPSNP LEKQIPSWLP
NFPPDHTYKF TPEFNHPITD LKTIKKEIVK ESQESEKALL NLNKSLSHIS SASNTPQPPG
LDDEDAIEQQ LEIWGNALEE RKPTITEKSF NENNIEQYAK YRVELARERV TKFEVNQLKR
TKNPFLKISE TLYLPESPHQ SHKTIQKTIE LQFRKSMTLF MHNLPKVQKL KKEKIRMAKE
ERAKSLKRRQ EELISQRTKR EQDEGHDLEL LLNNEHARDA ADDTTTPNAL NNSTIVINTN
AEDEDDDINL FGILGSSEDE NEMSSMPAEN LVAESEPPTM TAQDTTNTTP VAHNTTNIDA
TTSHSPHSTP NENAPTSPPA DIATDHDITM
