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Protein

TATA-box-binding protein

Gene

Tbp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.3 Publications

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • core promoter binding Source: FlyBase
  • DNA binding Source: FlyBase
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: FlyBase
  • RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly Source: FlyBase
  • TFIIA-class transcription factor binding Source: FlyBase
  • transcription factor binding Source: FlyBase
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  • DNA-templated transcription, initiation Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: BHF-UCL
  • regulation of transcription from RNA polymerase III promoter Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • RNA polymerase II transcriptional preinitiation complex assembly Source: BHF-UCL
  • snRNA transcription from RNA polymerase III promoter Source: FlyBase
  • transcription initiation from RNA polymerase II promoter Source: FlyBase
  • tRNA transcription from RNA polymerase III promoter Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-6807505. RNA polymerase II transcribes snRNA genes.
R-DME-73772. RNA Polymerase I Promoter Escape.
R-DME-73776. RNA Polymerase II Promoter Escape.
R-DME-73777. RNA Polymerase I Chain Elongation.
R-DME-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-DME-75953. RNA Polymerase II Transcription Initiation.
R-DME-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended name:
TATA-box-binding protein
Alternative name(s):
TATA sequence-binding protein
TATA-binding factor
TATA-box factor
Transcription initiation factor TFIID TBP subunit
Gene namesi
Name:Tbp
Synonyms:BTF1, TFIID
ORF Names:CG9874
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003687. Tbp.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase III complex Source: FlyBase
  • nucleus Source: FlyBase
  • transcription factor TFIID complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353TATA-box-binding proteinPRO_0000153964Add
BLAST

Proteomic databases

PaxDbiP20227.
PRIDEiP20227.

Expressioni

Gene expression databases

BgeeiP20227.
GenevisibleiP20227. DM.

Interactioni

Subunit structurei

Belongs to the TFIID complex which is composed of TATA binding protein (Tbp) and a number of TBP-associated factors (Tafs). Binds DNA as monomer. Interacts with TFIIA-L heterotrimer. Interacts with Taf1, Taf2, Taf5 and Taf12.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Mef2P407912EBI-169179,EBI-235994

GO - Molecular functioni

  • TFIIA-class transcription factor binding Source: FlyBase
  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi63101. 9 interactions.
DIPiDIP-80N.
IntActiP20227. 7 interactions.
MINTiMINT-945188.
STRINGi7227.FBpp0071596.

Structurei

3D structure databases

ProteinModelPortaliP20227.
SMRiP20227. Positions 174-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati179 – 255771Add
BLAST
Repeati269 – 346782Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 618Poly-Gln
Compositional biasi94 – 10310Poly-Gln

Sequence similaritiesi

Belongs to the TBP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3302. Eukaryota.
COG2101. LUCA.
GeneTreeiENSGT00410000025389.
InParanoidiP20227.
KOiK03120.
OMAiMDQMLPS.
OrthoDBiEOG7XWPPF.
PhylomeDBiP20227.

Family and domain databases

Gene3Di3.30.310.10. 2 hits.
HAMAPiMF_00408. TATA_bind_prot_arch.
InterProiIPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
IPR030491. TBP_CS.
[Graphical view]
PANTHERiPTHR10126. PTHR10126. 1 hit.
PfamiPF00352. TBP. 2 hits.
[Graphical view]
PRINTSiPR00686. TIFACTORIID.
PROSITEiPS00351. TFIID. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20227-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQMLSPNFS IPSIGTPLHQ MEADQQIVAN PVYHPPAVSQ PDSLMPAPGS
60 70 80 90 100
SSVQHQQQQQ QSDASGGSGL FGHEPSLPLA HKQMQSYQPS ASYQQQQQQQ
110 120 130 140 150
QLQSQAPGGG GSTPQSMMQP QTPQSMMAHM MPMSERSVGG SGAGGGGDAL
160 170 180 190 200
SNIHQTMGPS TPMTPATPGS ADPGIVPQLQ NIVSTVNLCC KLDLKKIALH
210 220 230 240 250
ARNAEYNPKR FAAVIMRIRE PRTTALIFSS GKMVCTGAKS EDDSRLAARK
260 270 280 290 300
YARIIQKLGF PAKFLDFKIQ NMVGSCDVKF PIRLEGLVLT HCNFSSYEPE
310 320 330 340 350
LFPGLIYRMV RPRIVLLIFV SGKVVLTGAK VRQEIYDAFD KIFPILKKFK

KQS
Length:353
Mass (Da):38,451
Last modified:February 1, 1991 - v1
Checksum:i7B079BC01BAF69BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011Q → QQ (Ref. 4) Curated
Sequence conflicti146 – 1461G → A in AAA79092 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38388 mRNA. Translation: AAA28926.1.
M38082 mRNA. Translation: AAA28931.1.
U11718 Genomic DNA. Translation: AAA68629.1.
U35147 Genomic DNA. Translation: AAA79092.1.
AE013599 Genomic DNA. Translation: AAF46754.1.
AY069663 mRNA. Translation: AAL39808.1.
PIRiA35615.
RefSeqiNP_523805.1. NM_079081.4.
UniGeneiDm.4490.

Genome annotation databases

EnsemblMetazoaiFBtr0071679; FBpp0071596; FBgn0003687.
GeneIDi37476.
KEGGidme:Dmel_CG9874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38388 mRNA. Translation: AAA28926.1.
M38082 mRNA. Translation: AAA28931.1.
U11718 Genomic DNA. Translation: AAA68629.1.
U35147 Genomic DNA. Translation: AAA79092.1.
AE013599 Genomic DNA. Translation: AAF46754.1.
AY069663 mRNA. Translation: AAL39808.1.
PIRiA35615.
RefSeqiNP_523805.1. NM_079081.4.
UniGeneiDm.4490.

3D structure databases

ProteinModelPortaliP20227.
SMRiP20227. Positions 174-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63101. 9 interactions.
DIPiDIP-80N.
IntActiP20227. 7 interactions.
MINTiMINT-945188.
STRINGi7227.FBpp0071596.

Proteomic databases

PaxDbiP20227.
PRIDEiP20227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071679; FBpp0071596; FBgn0003687.
GeneIDi37476.
KEGGidme:Dmel_CG9874.

Organism-specific databases

CTDi6908.
FlyBaseiFBgn0003687. Tbp.

Phylogenomic databases

eggNOGiKOG3302. Eukaryota.
COG2101. LUCA.
GeneTreeiENSGT00410000025389.
InParanoidiP20227.
KOiK03120.
OMAiMDQMLPS.
OrthoDBiEOG7XWPPF.
PhylomeDBiP20227.

Enzyme and pathway databases

ReactomeiR-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-6807505. RNA polymerase II transcribes snRNA genes.
R-DME-73772. RNA Polymerase I Promoter Escape.
R-DME-73776. RNA Polymerase II Promoter Escape.
R-DME-73777. RNA Polymerase I Chain Elongation.
R-DME-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-DME-75953. RNA Polymerase II Transcription Initiation.
R-DME-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

GenomeRNAii37476.
PROiP20227.

Gene expression databases

BgeeiP20227.
GenevisibleiP20227. DM.

Family and domain databases

Gene3Di3.30.310.10. 2 hits.
HAMAPiMF_00408. TATA_bind_prot_arch.
InterProiIPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
IPR030491. TBP_CS.
[Graphical view]
PANTHERiPTHR10126. PTHR10126. 1 hit.
PfamiPF00352. TBP. 2 hits.
[Graphical view]
PRINTSiPR00686. TIFACTORIID.
PROSITEiPS00351. TFIID. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the Drosophila gene encoding the TATA box binding protein, TFIID."
    Hoey T., Dynlacht B.D., Peterson M.G., Pugh B.F., Tjian R.
    Cell 61:1179-1186(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  3. "Structure of the genes encoding transcription factor IIB and TATA box-binding protein from Drosophila melanogaster."
    Lira-DeVito L.M., Burke T.W., Kadonaga J.T.
    Gene 153:203-207(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Molecular characterization of the Drosophila gene encoding the TATA-box binding protein (TBP)."
    Lee K., Oh Y., Yoon J., Cho N., Baek K.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
  5. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  6. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  7. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  8. "Drosophila TFIIA-L is processed into two subunits that are associated with the TBP/TAF complex."
    Yokomori K., Admon A., Goodrich J.A., Chen J.-L., Tjian R.
    Genes Dev. 7:2235-2245(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TFIIA-L.
    Tissue: Embryo.
  9. "Molecular cloning and characterization of dTAFII30 alpha and dTAFII30 beta: two small subunits of Drosophila TFIID."
    Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.
    Genes Dev. 7:2587-2597(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF12.
  10. "Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit."
    Kokubo T., Gong D.-W., Yamashita S., Takada R., Roeder R.G., Horikoshi M., Nakatani Y.
    Mol. Cell. Biol. 13:7859-7863(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF5.
    Tissue: Embryo.
  11. "Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator."
    Weinzierl R.O., Dynlacht B.D., Tjian R.
    Nature 362:511-517(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF1.
  12. "Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding to core promoter DNA."
    Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.
    Science 264:933-941(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF2.
    Tissue: Embryo.

Entry informationi

Entry nameiTBP_DROME
AccessioniPrimary (citable) accession number: P20227
Secondary accession number(s): Q9W2D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 8, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.