TBP_DROME
ID TBP_DROME Reviewed; 353 AA.
AC P20227; Q9W2D8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=TATA-box-binding protein;
DE AltName: Full=TATA sequence-binding protein;
DE AltName: Full=TATA-binding factor;
DE AltName: Full=TATA-box factor;
DE AltName: Full=Transcription initiation factor TFIID TBP subunit;
GN Name=Tbp; Synonyms=BTF1, TFIID; ORFNames=CG9874;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=2194666; DOI=10.1016/0092-8674(90)90682-5;
RA Hoey T., Dynlacht B.D., Peterson M.G., Pugh B.F., Tjian R.;
RT "Isolation and characterization of the Drosophila gene encoding the TATA
RT box binding protein, TFIID.";
RL Cell 61:1179-1186(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=2123550; DOI=10.1073/pnas.87.23.9148;
RA Muhich M., Iida C.T., Horikoshi M., Roeder R.G., Parker C.S.;
RT "cDNA clone encoding Drosophila transcription factor TFIID.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9148-9152(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7875589; DOI=10.1016/0378-1119(94)00764-j;
RA Lira-DeVito L.M., Burke T.W., Kadonaga J.T.;
RT "Structure of the genes encoding transcription factor IIB and TATA box-
RT binding protein from Drosophila melanogaster.";
RL Gene 153:203-207(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RA Lee K., Oh Y., Yoon J., Cho N., Baek K.;
RT "Molecular characterization of the Drosophila gene encoding the TATA-box
RT binding protein (TBP).";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH TFIIA-L.
RC TISSUE=Embryo;
RX PubMed=8224849; DOI=10.1101/gad.7.11.2235;
RA Yokomori K., Admon A., Goodrich J.A., Chen J.-L., Tjian R.;
RT "Drosophila TFIIA-L is processed into two subunits that are associated with
RT the TBP/TAF complex.";
RL Genes Dev. 7:2235-2245(1993).
RN [9]
RP INTERACTION WITH TAF12.
RX PubMed=8276241; DOI=10.1101/gad.7.12b.2587;
RA Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.;
RT "Molecular cloning and characterization of dTAFII30 alpha and dTAFII30
RT beta: two small subunits of Drosophila TFIID.";
RL Genes Dev. 7:2587-2597(1993).
RN [10]
RP INTERACTION WITH TAF5.
RC TISSUE=Embryo;
RX PubMed=8247000; DOI=10.1128/mcb.13.12.7859-7863.1993;
RA Kokubo T., Gong D.-W., Yamashita S., Takada R., Roeder R.G., Horikoshi M.,
RA Nakatani Y.;
RT "Molecular cloning, expression, and characterization of the Drosophila 85-
RT kilodalton TFIID subunit.";
RL Mol. Cell. Biol. 13:7859-7863(1993).
RN [11]
RP INTERACTION WITH TAF1.
RX PubMed=8464492; DOI=10.1038/362511a0;
RA Weinzierl R.O., Dynlacht B.D., Tjian R.;
RT "Largest subunit of Drosophila transcription factor IID directs assembly of
RT a complex containing TBP and a coactivator.";
RL Nature 362:511-517(1993).
RN [12]
RP INTERACTION WITH TAF2.
RC TISSUE=Embryo;
RX PubMed=8178153; DOI=10.1126/science.8178153;
RA Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.;
RT "Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding
RT to core promoter DNA.";
RL Science 264:933-941(1994).
CC -!- FUNCTION: General transcription factor that functions at the core of
CC the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA
CC box is the initial transcriptional step of the pre-initiation complex
CC (PIC), playing a role in the activation of eukaryotic genes transcribed
CC by RNA polymerase II. {ECO:0000269|PubMed:2123550,
CC ECO:0000269|PubMed:2194666, ECO:0000269|PubMed:8224849}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (Tafs). Binds DNA
CC as monomer. Interacts with TFIIA-L heterotrimer. Interacts with Taf1,
CC Taf2, Taf5 and Taf12. {ECO:0000269|PubMed:8178153,
CC ECO:0000269|PubMed:8224849, ECO:0000269|PubMed:8247000,
CC ECO:0000269|PubMed:8276241, ECO:0000269|PubMed:8464492}.
CC -!- INTERACTION:
CC P20227; P40791: Mef2; NbExp=2; IntAct=EBI-169179, EBI-235994;
CC P20227; P51123: Taf1; NbExp=3; IntAct=EBI-169179, EBI-499582;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P20226}.
CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
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DR EMBL; M38388; AAA28926.1; -; mRNA.
DR EMBL; M38082; AAA28931.1; -; mRNA.
DR EMBL; U11718; AAA68629.1; -; Genomic_DNA.
DR EMBL; U35147; AAA79092.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46754.1; -; Genomic_DNA.
DR EMBL; AY069663; AAL39808.1; -; mRNA.
DR PIR; A35615; A35615.
DR RefSeq; NP_523805.1; NM_079081.4.
DR AlphaFoldDB; P20227; -.
DR SMR; P20227; -.
DR BioGRID; 63101; 37.
DR DIP; DIP-80N; -.
DR IntAct; P20227; 13.
DR STRING; 7227.FBpp0071596; -.
DR PaxDb; P20227; -.
DR PRIDE; P20227; -.
DR DNASU; 37476; -.
DR EnsemblMetazoa; FBtr0071679; FBpp0071596; FBgn0003687.
DR GeneID; 37476; -.
DR KEGG; dme:Dmel_CG9874; -.
DR CTD; 6908; -.
DR FlyBase; FBgn0003687; Tbp.
DR VEuPathDB; VectorBase:FBgn0003687; -.
DR eggNOG; KOG3302; Eukaryota.
DR GeneTree; ENSGT00940000167740; -.
DR HOGENOM; CLU_060161_1_3_1; -.
DR InParanoid; P20227; -.
DR OMA; HMMPMSE; -.
DR OrthoDB; 1219067at2759; -.
DR PhylomeDB; P20227; -.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-DME-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-DME-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 37476; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37476; -.
DR PRO; PR:P20227; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003687; Expressed in egg cell and 23 other tissues.
DR Genevisible; P20227; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IPI:FlyBase.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IDA:FlyBase.
DR GO; GO:0140223; F:general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0140296; F:general transcription initiation factor binding; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:BHF-UCL.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0001092; F:TFIIA-class transcription factor complex binding; IPI:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:BHF-UCL.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:BHF-UCL.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IDA:FlyBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:FlyBase.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:FlyBase.
DR CDD; cd04516; TBP_eukaryotes; 1.
DR Gene3D; 3.30.310.10; -; 2.
DR HAMAP; MF_00408; TATA_bind_prot_arch; 1.
DR InterPro; IPR000814; TBP.
DR InterPro; IPR030491; TBP_CS.
DR InterPro; IPR012295; TBP_dom_sf.
DR InterPro; IPR033710; TBP_eukaryotic.
DR PANTHER; PTHR10126; PTHR10126; 1.
DR Pfam; PF00352; TBP; 2.
DR PRINTS; PR00686; TIFACTORIID.
DR PROSITE; PS00351; TFIID; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Transcription.
FT CHAIN 1..353
FT /note="TATA-box-binding protein"
FT /id="PRO_0000153964"
FT REPEAT 179..255
FT /note="1"
FT REPEAT 269..346
FT /note="2"
FT REGION 20..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 101
FT /note="Q -> QQ (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="G -> A (in Ref. 4; AAA79092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38451 MW; 7B079BC01BAF69BC CRC64;
MDQMLSPNFS IPSIGTPLHQ MEADQQIVAN PVYHPPAVSQ PDSLMPAPGS SSVQHQQQQQ
QSDASGGSGL FGHEPSLPLA HKQMQSYQPS ASYQQQQQQQ QLQSQAPGGG GSTPQSMMQP
QTPQSMMAHM MPMSERSVGG SGAGGGGDAL SNIHQTMGPS TPMTPATPGS ADPGIVPQLQ
NIVSTVNLCC KLDLKKIALH ARNAEYNPKR FAAVIMRIRE PRTTALIFSS GKMVCTGAKS
EDDSRLAARK YARIIQKLGF PAKFLDFKIQ NMVGSCDVKF PIRLEGLVLT HCNFSSYEPE
LFPGLIYRMV RPRIVLLIFV SGKVVLTGAK VRQEIYDAFD KIFPILKKFK KQS
