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P20226

- TBP_HUMAN

UniProt

P20226 - TBP_HUMAN

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Protein

TATA-box-binding protein

Gene

TBP

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. repressing transcription factor binding Source: BHF-UCL
  2. transcription factor binding Source: UniProtKB
  3. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. positive regulation of transcription, DNA-templated Source: Ensembl
  4. spermatogenesis Source: Ensembl
  5. termination of RNA polymerase I transcription Source: Reactome
  6. transcription elongation from RNA polymerase II promoter Source: Reactome
  7. transcription elongation from RNA polymerase I promoter Source: Reactome
  8. transcription from RNA polymerase III promoter Source: MGI
  9. transcription from RNA polymerase II promoter Source: UniProtKB
  10. transcription from RNA polymerase I promoter Source: Reactome
  11. transcription initiation from RNA polymerase II promoter Source: UniProtKB
  12. transcription initiation from RNA polymerase I promoter Source: Reactome
  13. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_1074. RNA Polymerase I Transcription Termination.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_953. RNA Polymerase I Transcription Initiation.
SignaLinkiP20226.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11588. TBP.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. female pronucleus Source: Ensembl
  3. male pronucleus Source: Ensembl
  4. nuclear euchromatin Source: BHF-UCL
  5. nucleoplasm Source: Reactome
  6. transcription factor TFIIA complex Source: BHF-UCL
  7. transcription factor TFIID complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 17 (SCA17) [MIM:607136]: Spinocerebellar 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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiP20226.
PaxDbiP20226.
PRIDEiP20226.

PTM databases

PhosphoSiteiP20226.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP20226.
CleanExiHS_TBP.
ExpressionAtlasiP20226. baseline and differential.
GenevestigatoriP20226.

Organism-specific databases

HPAiCAB009442.

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.By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EDF1O60869-12EBI-355371,EBI-781310
GTF2A2P526572EBI-355371,EBI-1045262
POU3F2P202652EBI-355371,EBI-1167176
SETQ011054EBI-355371,EBI-1053182
TAF1P216755EBI-355371,EBI-491289
TAF12Q165142EBI-355371,EBI-1034238
TAF1BQ53T943EBI-355371,EBI-1560239
TAF1CQ155723EBI-355371,EBI-2510659
TP53P046372EBI-355371,EBI-366083

Protein-protein interaction databases

BioGridi112771. 145 interactions.
DIPiDIP-1078N.
IntActiP20226. 42 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[»]
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

eggNOGiCOG2101.
GeneTreeiENSGT00410000025389.
HOGENOMiHOG000105164.
HOVERGENiHBG044997.
InParanoidiP20226.
KOiK03120.
OMAiGQAPQLF.
PhylomeDBiP20226.
TreeFamiTF300102.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
3.30.310.10. 2 hits.
HAMAPiMF_00408. TATA_bind_prot_arch.
InterProiIPR011989. ARM-like.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
[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. Align

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.3. human. [P20226-1]

Polymorphism databases

DMDMi1351223.

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 .
CCDSi CCDS5315.1. [P20226-1 ]
CCDS55077.1. [P20226-2 ]
PIRi A34830. TWHU2D.
RefSeqi NP_001165556.1. NM_001172085.1. [P20226-2 ]
NP_003185.1. NM_003194.4. [P20226-1 ]
UniGenei Hs.590872.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C9B X-ray 2.65 B/F/J/N/R 159-337 [» ]
1CDW X-ray 1.90 A 159-337 [» ]
1JFI X-ray 2.62 C 159-339 [» ]
1NVP X-ray 2.10 A 159-339 [» ]
1TGH X-ray 2.90 A 156-339 [» ]
ProteinModelPortali P20226.
SMRi P20226. Positions 159-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112771. 145 interactions.
DIPi DIP-1078N.
IntActi P20226. 42 interactions.
MINTi MINT-156456.
STRINGi 9606.ENSP00000230354.

PTM databases

PhosphoSitei P20226.

Polymorphism databases

DMDMi 1351223.

Proteomic databases

MaxQBi P20226.
PaxDbi P20226.
PRIDEi P20226.

Protocols and materials databases

DNASUi 6908.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000230354 ; ENSP00000230354 ; ENSG00000112592 . [P20226-1 ]
ENST00000392092 ; ENSP00000375942 ; ENSG00000112592 . [P20226-1 ]
ENST00000540980 ; ENSP00000442132 ; ENSG00000112592 . [P20226-2 ]
GeneIDi 6908.
KEGGi hsa:6908.
UCSCi uc003qxt.3. human. [P20226-1 ]

Organism-specific databases

CTDi 6908.
GeneCardsi GC06P170863.
GeneReviewsi TBP.
HGNCi HGNC:11588. TBP.
HPAi CAB009442.
MIMi 600075. gene.
607136. phenotype.
neXtProti NX_P20226.
Orphaneti 98759. Spinocerebellar ataxia type 17.
PharmGKBi PA36352.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2101.
GeneTreei ENSGT00410000025389.
HOGENOMi HOG000105164.
HOVERGENi HBG044997.
InParanoidi P20226.
KOi K03120.
OMAi GQAPQLF.
PhylomeDBi P20226.
TreeFami TF300102.

Enzyme and pathway databases

Reactomei REACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_1074. RNA Polymerase I Transcription Termination.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_953. RNA Polymerase I Transcription Initiation.
SignaLinki P20226.

Miscellaneous databases

EvolutionaryTracei P20226.
GeneWikii TATA-binding_protein.
GenomeRNAii 6908.
NextBioi 27015.
PROi P20226.
SOURCEi Search...

Gene expression databases

Bgeei P20226.
CleanExi HS_TBP.
ExpressionAtlasi P20226. baseline and differential.
Genevestigatori P20226.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
3.30.310.10. 2 hits.
HAMAPi MF_00408. TATA_bind_prot_arch.
InterProi IPR011989. ARM-like.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
[Graphical view ]
PANTHERi PTHR10126. PTHR10126. 1 hit.
Pfami PF00352. TBP. 2 hits.
[Graphical view ]
PRINTSi PR00686. TIFACTORIID.
PROSITEi PS00351. TFIID. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Highly conserved core domain and unique N-terminus with presumptive regulatory motifs in a human TATA factor (TFIID)."
    Hoffmann A., Sinn E., Yamamoto T., Wang J., Roy A., Horikoshi M., Roeder R.G.
    Nature 346:387-390(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 92-GLN--GLN-95 DEL.
  2. "Functional domains and upstream activation properties of cloned human TATA binding protein."
    Peterson M.G., Tanese N., Pugh B.F., Tjian R.
    Science 248:1625-1630(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAINS.
  3. "Cloning of a transcriptionally active human TATA binding factor."
    Kao C.C., Lieberman P.M., Schmidt M.C., Zhou Q., Pei R., Berk A.J.
    Science 248:1646-1650(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fibroblast.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The RNA polymerase I transcription factor, upstream binding factor, interacts directly with the TATA box-binding protein."
    Kwon H., Green M.R.
    J. Biol. Chem. 269:30140-30146(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBFT.
  8. "Direct interaction of human TFIID with the HIV-1 transactivator tat."
    Kashanchi F., Piras G., Radonovich M.F., Duvall J.F., Fattaey A., Chiang C.M., Roeder R.G., Brady J.N.
    Nature 367:295-299(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  9. "Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits."
    Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.
    Science 266:1966-1972(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF1A; TAF1B AND TAF1C.
  10. "Evidence for functional interaction between the HIV-1 Tat transactivator and the TATA box binding protein in vivo."
    Veschambre P., Simard P., Jalinot P.
    J. Mol. Biol. 250:169-180(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  11. "Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity."
    Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M.
    J. Biol. Chem. 273:25840-25849(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UTF1.
  12. "Requirement of RSF and FACT for transcription of chromatin templates in vitro."
    LeRoy G., Orphanides G., Lane W.S., Reinberg D.
    Science 282:1900-1904(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TFIID COMPLEX.
  13. "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex formation and stabilizes upstream binding factor at the rDNA promoter."
    Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.
    J. Biol. Chem. 280:29551-29558(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE SL1/TIF-IB COMPLEX.
  14. Cited for: TISSUE SPECIFICITY.
  15. "SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1."
    Rao S., Matsumura A., Yoon J., Simon M.C.
    J. Biol. Chem. 274:11115-11124(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPIB.
  16. "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
    Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
    J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  17. "Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX, confers potent transactivating capacity and binds to TATA-binding protein (TBP)."
    Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C.
    Oncogene 18:3682-3695(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELF3.
  18. "BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of polymerase III small nuclear RNA gene promoters through its interaction with TATA-binding protein."
    Cabart P., Murphy S.
    J. Biol. Chem. 276:43056-43064(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRF2.
  19. "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger."
    Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.
    Mol. Cell. Biol. 21:5109-5121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF3.
  20. "Functional substitution for TAF(II)250 by a retroposed homolog that is expressed in human spermatogenesis."
    Wang P.J., Page D.C.
    Hum. Mol. Genet. 11:2341-2346(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF1L.
  21. "The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition."
    Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.
    J. Biol. Chem. 278:18649-18657(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC4.
  22. "HIV-1 Tat stimulates transcription complex assembly through recruitment of TBP in the absence of TAFs."
    Raha T., Cheng S.W.G., Green M.R.
    PLoS Biol. 3:221-230(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  23. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
    Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
    J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP1.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Crystal structure of a human TATA box-binding protein/TATA element complex."
    Nikolov D.B., Chen H., Halay E.D., Hoffmann A., Roeder R.G., Burley S.K.
    Proc. Natl. Acad. Sci. U.S.A. 93:4862-4867(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 159-337 IN COMPLEX WITH DNA.
  26. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 159-339 IN COMPLEX WITH DNA.
  27. "Structural basis of preinitiation complex assembly on human pol II promoters."
    Tsai F.T.F., Sigler P.B.
    EMBO J. 19:25-36(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-337 IN COMPLEX WITH GTF2B AND DNA.
  28. "Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex."
    Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G., Meisterernst M., Burley S.K.
    Cell 106:71-81(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 159-339 IN COMPLEX WITH DR1; DRAP1 AND DNA.
  29. "A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?"
    Koide R., Kobayashi S., Shimohata T., Ikeuchi T., Maruyama M., Saito M., Yamada M., Takahashi H., Tsuji S.
    Hum. Mol. Genet. 8:2047-2053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM OF POLY-GLN REGION.
  30. "Different types of repeat expansion in the TATA-binding protein gene are associated with a new form of inherited ataxia."
    Zuhlke C., Hellenbroich Y., Dalski A., Kononowa N., Hagenah J., Vieregge P., Riess O., Klein C., Schwinger E.
    Eur. J. Hum. Genet. 9:160-164(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.
  31. "SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein."
    Nakamura K., Jeong S.-Y., Uchihara T., Anno M., Nagashima K., Nagashima T., Ikeda S., Tsuji S., Kanazawa I.
    Hum. Mol. Genet. 10:1441-1448(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.
  32. Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.

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: November 26, 2014
This is version 176 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

External Data

Dasty 3