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Protein

TATA-box-binding protein

Gene

TBP

Organism
Homo sapiens (Human)
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. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
SignaLinkiP20226.
SIGNORiP20226.

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:GTF2D1, TF2D, TFIID
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11588. TBP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • female pronucleus Source: Ensembl
  • male pronucleus Source: Ensembl
  • nuclear euchromatin Source: BHF-UCL
  • nucleoplasm Source: HPA
  • transcription factor TFIIA complex Source: BHF-UCL
  • transcription factor TFIID complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 17 (SCA17)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
See also OMIM:607136

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MalaCardsiTBP.
MIMi607136. phenotype.
Orphaneti98759. Spinocerebellar ataxia type 17.
PharmGKBiPA36352.

Polymorphism and mutation databases

BioMutaiTBP.
DMDMi1351223.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339TATA-box-binding proteinPRO_0000153956Add
BLAST

Proteomic databases

EPDiP20226.
MaxQBiP20226.
PaxDbiP20226.
PeptideAtlasiP20226.
PRIDEiP20226.

PTM databases

iPTMnetiP20226.
PhosphoSiteiP20226.
SwissPalmiP20226.

Expressioni

Tissue specificityi

Widely expressed, with levels highest in the testis and ovary.1 Publication

Gene expression databases

BgeeiENSG00000112592.
CleanExiHS_TBP.
ExpressionAtlasiP20226. baseline and differential.
GenevisibleiP20226. HS.

Organism-specific databases

HPAiCAB009442.
HPA049805.

Interactioni

Subunit structurei

Binds DNA as monomer. Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B TAF1C and TAF1D. Association of TBP to form either TFIID or SL1/TIF-IB appears to be mutually exclusive. Interacts with TAF1A, TAF1B and TAF1C. Interacts with TFIIB, NCOA6, DRAP1, DR1 and ELF3. Interacts with SPIB, SNAPC1, SNAPC2 and SNAPC4. Interacts with UTF1. Interacts with BRF2. Interacts with UBTF. Interacts with GPBP1. Interacts with CITED2 (By similarity). Interacts with ATF7IP. Interacts with HIV-1 Tat. Interacts with herpes simplex virus 1 ICP4. Interacts with human adenovirus E1A protein; this interaction probably disrupts the TBP-TATA complex.By similarity21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EDF1O60869-12EBI-355371,EBI-781310
GTF2A2P526572EBI-355371,EBI-1045262
GTF2BQ004032EBI-355371,EBI-389564
POU3F2P202652EBI-355371,EBI-1167176
SETQ011054EBI-355371,EBI-1053182
TAF1P216755EBI-355371,EBI-491289
TAF12Q165142EBI-355371,EBI-1034238
TAF1AQ155732EBI-355371,EBI-2510647
TAF1BQ53T944EBI-355371,EBI-1560239
TAF1CQ155723EBI-355371,EBI-2510659
TP53P046372EBI-355371,EBI-366083
UL3Q059064EBI-355371,EBI-11702805From a different organism.

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • repressing transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112771. 167 interactions.
DIPiDIP-1078N.
IntActiP20226. 58 interactions.
MINTiMINT-156456.
STRINGi9606.ENSP00000230354.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi164 – 17310Combined sources
Helixi180 – 1867Combined sources
Beta strandi190 – 1923Combined sources
Turni194 – 1963Combined sources
Beta strandi198 – 2047Combined sources
Turni205 – 2084Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi217 – 2226Combined sources
Helixi227 – 24418Combined sources
Beta strandi251 – 26313Combined sources
Helixi270 – 2767Combined sources
Turni277 – 2804Combined sources
Turni285 – 2873Combined sources
Beta strandi289 – 2957Combined sources
Turni296 – 2994Combined sources
Beta strandi300 – 3045Combined sources
Beta strandi308 – 3136Combined sources
Helixi318 – 33316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9BX-ray2.65B/F/J/N/R159-337[»]
1CDWX-ray1.90A159-337[»]
1JFIX-ray2.62C159-339[»]
1NVPX-ray2.10A159-339[»]
1TGHX-ray2.90A156-339[»]
4ROCX-ray1.90B159-339[»]
4RODX-ray2.70B159-339[»]
4ROEX-ray2.20B159-339[»]
5FURelectron microscopy8.50A1-339[»]
5IY6electron microscopy7.20P1-339[»]
5IY7electron microscopy8.60P1-339[»]
5IY8electron microscopy7.90P1-339[»]
5IY9electron microscopy6.30P1-339[»]
5IYAelectron microscopy5.40P1-339[»]
5IYBelectron microscopy3.90P1-339[»]
5IYCelectron microscopy3.90P1-339[»]
5IYDelectron microscopy3.90P1-339[»]
ProteinModelPortaliP20226.
SMRiP20226. Positions 159-337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20226.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati165 – 241771Add
BLAST
Repeati255 – 332782Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 9541Poly-GlnAdd
BLAST

Sequence similaritiesi

Belongs to the TBP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3302. Eukaryota.
COG2101. LUCA.
GeneTreeiENSGT00410000025389.
HOGENOMiHOG000105164.
HOVERGENiHBG044997.
InParanoidiP20226.
KOiK03120.
OMAiMMPYGSG.
OrthoDBiEOG091G0ENY.
PhylomeDBiP20226.
TreeFamiTF300102.

Family and domain databases

CDDicd04516. TBP_eukaryotes. 1 hit.
Gene3Di1.25.10.10. 1 hit.
3.30.310.10. 2 hits.
HAMAPiMF_00408. TATA_bind_prot_arch. 1 hit.
InterProiIPR011989. ARM-like.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
IPR030491. TBP_CS.
IPR033710. TBP_eukaryotic.
[Graphical view]
PANTHERiPTHR10126. PTHR10126. 1 hit.
PfamiPF00352. TBP. 2 hits.
[Graphical view]
PRINTSiPR00686. TIFACTORIID.
PROSITEiPS00351. TFIID. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P20226-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS
60 70 80 90 100
ILEEQQRQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQAVAAA
110 120 130 140 150
AVQQSTSQQA TQGTSGQAPQ LFHSQTLTTA PLPGTTPLYP SPMTPMTPIT
160 170 180 190 200
PATPASESSG IVPQLQNIVS TVNLGCKLDL KTIALRARNA EYNPKRFAAV
210 220 230 240 250
IMRIREPRTT ALIFSSGKMV CTGAKSEEQS RLAARKYARV VQKLGFPAKF
260 270 280 290 300
LDFKIQNMVG SCDVKFPIRL EGLVLTHQQF SSYEPELFPG LIYRMIKPRI
310 320 330
VLLIFVSGKV VLTGAKVRAE IYEAFENIYP ILKGFRKTT
Length:339
Mass (Da):37,698
Last modified:February 1, 1996 - v2
Checksum:iA61A578D972B970B
GO
Isoform 2 (identifier: P20226-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Note: No experimental confirmation available.
Show »
Length:319
Mass (Da):35,657
Checksum:i18CF7E0A7240DC5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951Missing in BAG65425 (PubMed:14702039).Curated
Sequence conflicti149 – 1491I → T in BAG65425 (PubMed:14702039).Curated
Sequence conflicti187 – 1871A → R in AAC03409 (PubMed:2194289).Curated

Polymorphismi

The poly-Gln region of TBP is highly polymorphic (25 to 42 repeats) in normal individuals and is expanded to about 47-63 repeats in spinocerebellar ataxia 17 (SCA17) patients.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 954Missing .1 Publication
VAR_016987

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform 2. 1 PublicationVSP_045488Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54993 mRNA. Translation: CAA38736.1.
M55654 mRNA. Translation: AAA36731.1.
M34960 mRNA. Translation: AAC03409.1.
AK304648 mRNA. Translation: BAG65425.1.
CR456776 mRNA. Translation: CAG33057.1.
AL031259 Genomic DNA. Translation: CAA20286.1.
CCDSiCCDS5315.1. [P20226-1]
CCDS55077.1. [P20226-2]
PIRiA34830. TWHU2D.
RefSeqiNP_001165556.1. NM_001172085.1. [P20226-2]
NP_003185.1. NM_003194.4. [P20226-1]
UniGeneiHs.590872.

Genome annotation databases

EnsembliENST00000230354; ENSP00000230354; ENSG00000112592. [P20226-1]
ENST00000392092; ENSP00000375942; ENSG00000112592. [P20226-1]
ENST00000540980; ENSP00000442132; ENSG00000112592. [P20226-2]
GeneIDi6908.
KEGGihsa:6908.
UCSCiuc003qxt.4. human. [P20226-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54993 mRNA. Translation: CAA38736.1.
M55654 mRNA. Translation: AAA36731.1.
M34960 mRNA. Translation: AAC03409.1.
AK304648 mRNA. Translation: BAG65425.1.
CR456776 mRNA. Translation: CAG33057.1.
AL031259 Genomic DNA. Translation: CAA20286.1.
CCDSiCCDS5315.1. [P20226-1]
CCDS55077.1. [P20226-2]
PIRiA34830. TWHU2D.
RefSeqiNP_001165556.1. NM_001172085.1. [P20226-2]
NP_003185.1. NM_003194.4. [P20226-1]
UniGeneiHs.590872.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9BX-ray2.65B/F/J/N/R159-337[»]
1CDWX-ray1.90A159-337[»]
1JFIX-ray2.62C159-339[»]
1NVPX-ray2.10A159-339[»]
1TGHX-ray2.90A156-339[»]
4ROCX-ray1.90B159-339[»]
4RODX-ray2.70B159-339[»]
4ROEX-ray2.20B159-339[»]
5FURelectron microscopy8.50A1-339[»]
5IY6electron microscopy7.20P1-339[»]
5IY7electron microscopy8.60P1-339[»]
5IY8electron microscopy7.90P1-339[»]
5IY9electron microscopy6.30P1-339[»]
5IYAelectron microscopy5.40P1-339[»]
5IYBelectron microscopy3.90P1-339[»]
5IYCelectron microscopy3.90P1-339[»]
5IYDelectron microscopy3.90P1-339[»]
ProteinModelPortaliP20226.
SMRiP20226. Positions 159-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112771. 167 interactions.
DIPiDIP-1078N.
IntActiP20226. 58 interactions.
MINTiMINT-156456.
STRINGi9606.ENSP00000230354.

PTM databases

iPTMnetiP20226.
PhosphoSiteiP20226.
SwissPalmiP20226.

Polymorphism and mutation databases

BioMutaiTBP.
DMDMi1351223.

Proteomic databases

EPDiP20226.
MaxQBiP20226.
PaxDbiP20226.
PeptideAtlasiP20226.
PRIDEiP20226.

Protocols and materials databases

DNASUi6908.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230354; ENSP00000230354; ENSG00000112592. [P20226-1]
ENST00000392092; ENSP00000375942; ENSG00000112592. [P20226-1]
ENST00000540980; ENSP00000442132; ENSG00000112592. [P20226-2]
GeneIDi6908.
KEGGihsa:6908.
UCSCiuc003qxt.4. human. [P20226-1]

Organism-specific databases

CTDi6908.
GeneCardsiTBP.
GeneReviewsiTBP.
HGNCiHGNC:11588. TBP.
HPAiCAB009442.
HPA049805.
MalaCardsiTBP.
MIMi600075. gene.
607136. phenotype.
neXtProtiNX_P20226.
Orphaneti98759. Spinocerebellar ataxia type 17.
PharmGKBiPA36352.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3302. Eukaryota.
COG2101. LUCA.
GeneTreeiENSGT00410000025389.
HOGENOMiHOG000105164.
HOVERGENiHBG044997.
InParanoidiP20226.
KOiK03120.
OMAiMMPYGSG.
OrthoDBiEOG091G0ENY.
PhylomeDBiP20226.
TreeFamiTF300102.

Enzyme and pathway databases

ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
SignaLinkiP20226.
SIGNORiP20226.

Miscellaneous databases

EvolutionaryTraceiP20226.
GeneWikiiTATA-binding_protein.
GenomeRNAii6908.
PROiP20226.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112592.
CleanExiHS_TBP.
ExpressionAtlasiP20226. baseline and differential.
GenevisibleiP20226. HS.

Family and domain databases

CDDicd04516. TBP_eukaryotes. 1 hit.
Gene3Di1.25.10.10. 1 hit.
3.30.310.10. 2 hits.
HAMAPiMF_00408. TATA_bind_prot_arch. 1 hit.
InterProiIPR011989. ARM-like.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
IPR030491. TBP_CS.
IPR033710. TBP_eukaryotic.
[Graphical view]
PANTHERiPTHR10126. PTHR10126. 1 hit.
PfamiPF00352. TBP. 2 hits.
[Graphical view]
PRINTSiPR00686. TIFACTORIID.
PROSITEiPS00351. TFIID. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBP_HUMAN
AccessioniPrimary (citable) accession number: P20226
Secondary accession number(s): B4E3B3
, F5H869, Q16845, Q6IBM6, Q9UC02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: September 7, 2016
This is version 196 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.