TAF7_YEAST
ID TAF7_YEAST Reviewed; 590 AA.
AC Q05021; D6W052;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Transcription initiation factor TFIID subunit 7;
DE AltName: Full=TAFII-67;
DE AltName: Full=TBP-associated factor 67 kDa;
DE AltName: Full=TBP-associated factor 7;
GN Name=TAF7; Synonyms=TAF67; OrderedLocusNames=YMR227C; ORFNames=YM9959.09C;
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 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 [4]
RP FUNCTION, AND INTERACTION WITH BDF1.
RX PubMed=10783167;
RA Matangkasombut O., Buratowski R.M., Swilling N.W., Buratowski S.;
RT "Bromodomain factor 1 corresponds to a missing piece of yeast TFIID.";
RL Genes Dev. 14:951-962(2000).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-99 AND SER-104, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, 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. TAF7 is responsible for the recruitment of
CC BDF1 to TATA element containing promoters.
CC {ECO:0000269|PubMed:10783167, ECO:0000269|PubMed:10788514,
CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863}.
CC -!- SUBUNIT: TAF7 interacts with BDF1. The 1.2 MDa TFIID complex is
CC composed of TATA binding protein (TBP) and the 14 TBP-associated
CC factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13,
CC two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three
CC copies of TAF14. {ECO:0000269|PubMed:10783167,
CC ECO:0000269|PubMed:10788514}.
CC -!- INTERACTION:
CC Q05021; P35817: BDF1; NbExp=5; IntAct=EBI-27490, EBI-3493;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF7 family. {ECO:0000305}.
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DR EMBL; Z49939; CAA90198.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10126.1; -; Genomic_DNA.
DR PIR; S57594; S57594.
DR RefSeq; NP_013954.1; NM_001182734.1.
DR PDB; 4OY2; X-ray; 2.90 A; B/D/F=86-320.
DR PDBsum; 4OY2; -.
DR AlphaFoldDB; Q05021; -.
DR SMR; Q05021; -.
DR BioGRID; 35405; 191.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-6818N; -.
DR IntAct; Q05021; 13.
DR MINT; Q05021; -.
DR STRING; 4932.YMR227C; -.
DR iPTMnet; Q05021; -.
DR MaxQB; Q05021; -.
DR PaxDb; Q05021; -.
DR PRIDE; Q05021; -.
DR EnsemblFungi; YMR227C_mRNA; YMR227C; YMR227C.
DR GeneID; 855267; -.
DR KEGG; sce:YMR227C; -.
DR SGD; S000004840; TAF7.
DR VEuPathDB; FungiDB:YMR227C; -.
DR eggNOG; KOG4011; Eukaryota.
DR GeneTree; ENSGT00940000175094; -.
DR HOGENOM; CLU_016434_2_0_1; -.
DR InParanoid; Q05021; -.
DR OMA; DMMMLFG; -.
DR BioCyc; YEAST:G3O-32908-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:Q05021; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05021; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
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; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd08047; TAF7; 1.
DR InterPro; IPR037817; TAF7.
DR InterPro; IPR006751; TAFII55_prot_cons_reg.
DR PANTHER; PTHR12228; PTHR12228; 1.
DR Pfam; PF04658; TAFII55_N; 1.
DR SMART; SM01370; TAFII55_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..590
FT /note="Transcription initiation factor TFIID subunit 7"
FT /id="PRO_0000118885"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..549
FT /evidence="ECO:0000255"
FT COMPBIAS 8..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..431
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4OY2"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:4OY2"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4OY2"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:4OY2"
FT STRAND 158..175
FT /evidence="ECO:0007829|PDB:4OY2"
FT STRAND 177..197
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4OY2"
FT TURN 215..219
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4OY2"
FT TURN 270..276
FT /evidence="ECO:0007829|PDB:4OY2"
FT HELIX 283..301
FT /evidence="ECO:0007829|PDB:4OY2"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:4OY2"
SQ SEQUENCE 590 AA; 67555 MW; C014E7419B0B1C61 CRC64;
MAVIRIKKPR GPGEKDQPLE GEPKLKRIRI KTKVTDEDIK PKPKLKINLK KKKESADGKE
KKNSLKLKLN LKKNEEPVKK IHKAPKLRLK PIRIPGEAYD SEASDIEDDP LIESGVILRI
LPDIQLEFVK NSLESGDYSG ISIKWKNERH AVVTINDVMY GAILVDLPTV IEVNKSVDRK
NLLKTFDVSQ MLLCIRPIQE EEEVYALEAP DTEDLVVKHF EGIEDEIWEN KETFLKGYNG
APLSDMEAKH LKEIALKGYD YKHGISPPLY NVRNRRFRRK MDPNEIDYVE KVVDMLLKQD
KQAEEVSYDL VDKSELQARQ ERVSSWENFK EEPGEPLSRP ALKKEEIHTI ASAVGKQGAE
EEGEEGMEEE EEEDLDLGAA FESEEEGSGA EGDKEQQQEE VGDEVDQDTG GEDDDDDDDG
DIEAAGGESE SDDEKDENRQ HTELLADELN ELETTLAHTK HKLSKATNPL LKSRFIDSIK
KLEKEAELKR KQLQQTEDSV QKQHQHRSDA ETANNVEEEE EEEEEEEEED EVDEDEEDDE
ENDEDEDNVH EREHIQENKV VRELDEAPAE ETLDQNDLDM MMLFGAEGDE
