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P20226 (TBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TBP
Synonyms:GTF2D1, TF2D, TFIID
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Subcellular location

Nucleus HAMAP-Rule MF_00408.

Tissue specificity

Widely expressed, with levels highest in the testis and ovary. Ref.14

Polymorphism

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. HAMAP-Rule MF_00408

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30 Ref.31 Ref.32

Sequence similarities

Belongs to the TBP family.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   DomainRepeat
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred by curator PubMed 7729427. Source: UniProtKB

transcription from RNA polymerase III promoter

Inferred from direct assay PubMed 9027316. Source: MGI

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Inferred by curator PubMed 7729427. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

female pronucleus

Inferred from electronic annotation. Source: Ensembl

male pronucleus

Inferred from electronic annotation. Source: Ensembl

nuclear euchromatin

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor TFIIA complex

Inferred from direct assay PubMed 7724559. Source: BHF-UCL

transcription factor TFIID complex

Inferred from direct assay PubMed 7729427. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.17Ref.19PubMed 12040021Ref.20PubMed 1465435PubMed 7667268PubMed 7680771PubMed 7729427PubMed 8006019PubMed 9045704Ref.11. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 18838386. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 11005381PubMed 12676957PubMed 9722567. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 16540471PubMed 7933101. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20226-1)

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.
Isoform 2 (identifier: P20226-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339TATA-box-binding protein HAMAP-Rule MF_00408
PRO_0000153956

Regions

Repeat165 – 241771 HAMAP-Rule MF_00408
Repeat255 – 332782 HAMAP-Rule MF_00408
Compositional bias55 – 9541Poly-Gln HAMAP-Rule MF_00408

Natural variations

Alternative sequence1 – 2020Missing in isoform 2.
VSP_045488
Natural variant92 – 954Missing.
VAR_016987

Experimental info

Sequence conflict951Missing in BAG65425. Ref.4
Sequence conflict1491I → T in BAG65425. Ref.4
Sequence conflict1871A → R in AAC03409. Ref.3

Secondary structure

................................ 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: A61A578D972B970B

FASTA33937,698
        10         20         30         40         50         60 
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ 

        70         80         90        100        110        120 
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQAVAAA AVQQSTSQQA TQGTSGQAPQ 

       130        140        150        160        170        180 
LFHSQTLTTA PLPGTTPLYP SPMTPMTPIT PATPASESSG IVPQLQNIVS TVNLGCKLDL 

       190        200        210        220        230        240 
KTIALRARNA EYNPKRFAAV IMRIREPRTT ALIFSSGKMV CTGAKSEEQS RLAARKYARV 

       250        260        270        280        290        300 
VQKLGFPAKF LDFKIQNMVG SCDVKFPIRL EGLVLTHQQF SSYEPELFPG LIYRMIKPRI 

       310        320        330 
VLLIFVSGKV VLTGAKVRAE IYEAFENIYP ILKGFRKTT 

« Hide

Isoform 2 [UniParc].

Checksum: 18CF7E0A7240DC5D
Show »

FASTA31935,657

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Genomics, evolution, and expression of TBPL2, a member of the TBP family."
Di Pietro C., Ragusa M., Duro L., Guglielmino M.R., Barbagallo D., Carnemolla A., Lagana A., Buffa P., Angelica R., Rinaldi A., Calafato M.S., Milicia I., Caserta C., Giugno R., Pulvirenti A., Giunta V., Rapisarda A., Di Pietro V. expand/collapse author list , Grillo A., Messina A., Ferro A., Grzeschik K.H., Purrello M.
DNA Cell Biol. 26:369-385(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"How proteins recognize the TATA box."
Juo Z.S., Chiu T.K., Leiberman P.M., Baikalov I., Berk A.J., Dickerson R.E.
J. Mol. Biol. 261:239-254(1996) [PubMed] [Europe PMC] [Abstract]
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]"Trinucleotide repeats in 202 families with ataxia: a small expanded (CAG)n allele at the SCA17 locus."
Silveira I., Miranda C., Guimaraes L., Moreira M.-C., Alonso I., Mendonca P., Ferro A., Pinto-Basto J., Coelho J., Ferreirinha F., Poirier J., Parreira E., Vale J., Januario C., Barbot C., Tuna A., Barros J., Koide R. expand/collapse author list , Tsuji S., Holmes S.E., Margolis R.L., Jardim L., Pandolfo M., Coutinho P., Sequeiros J.
Arch. Neurol. 59:623-629(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5315.1. [P20226-1]
CCDS55077.1. [P20226-2]
PIRTWHU2D. A34830.
RefSeqNP_001165556.1. NM_001172085.1. [P20226-2]
NP_003185.1. NM_003194.4. [P20226-1]
UniGeneHs.590872.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP20226.
SMRP20226. Positions 159-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112771. 139 interactions.
DIPDIP-1078N.
IntActP20226. 42 interactions.
MINTMINT-156456.
STRING9606.ENSP00000230354.

PTM databases

PhosphoSiteP20226.

Polymorphism databases

DMDM1351223.

Proteomic databases

MaxQBP20226.
PaxDbP20226.
PRIDEP20226.

Protocols and materials databases

DNASU6908.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230354; ENSP00000230354; ENSG00000112592. [P20226-1]
ENST00000392092; ENSP00000375942; ENSG00000112592. [P20226-1]
ENST00000540980; ENSP00000442132; ENSG00000112592. [P20226-2]
GeneID6908.
KEGGhsa:6908.
UCSCuc003qxt.3. human. [P20226-1]

Organism-specific databases

CTD6908.
GeneCardsGC06P170863.
GeneReviewsTBP.
HGNCHGNC:11588. TBP.
HPACAB009442.
MIM600075. gene.
607136. phenotype.
neXtProtNX_P20226.
Orphanet98759. Spinocerebellar ataxia type 17.
PharmGKBPA36352.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2101.
HOGENOMHOG000105164.
HOVERGENHBG044997.
InParanoidP20226.
KOK03120.
OMAGQAPQLF.
PhylomeDBP20226.
TreeFamTF300102.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.
SignaLinkP20226.

Gene expression databases

ArrayExpressP20226.
BgeeP20226.
CleanExHS_TBP.
GenevestigatorP20226.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
3.30.310.10. 2 hits.
HAMAPMF_00408. TATA_bind_prot_arch.
InterProIPR011989. ARM-like.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
[Graphical view]
PANTHERPTHR10126. PTHR10126. 1 hit.
PfamPF00352. TBP. 2 hits.
[Graphical view]
PRINTSPR00686. TIFACTORIID.
PROSITEPS00351. TFIID. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20226.
GeneWikiTATA-binding_protein.
GenomeRNAi6908.
NextBio27015.
PROP20226.
SOURCESearch...

Entry information

Entry nameTBP_HUMAN
AccessionPrimary (citable) accession number: P20226
Secondary accession number(s): B4E3B3 expand/collapse secondary AC list , F5H869, Q16845, Q6IBM6, Q9UC02
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM