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TATA-box-binding protein (TATA sequence-binding protein) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit)

 TBP_HUMAN               Reviewed;         339 AA.
P20226; B4E3B3; F5H869; Q16845; Q6IBM6; Q9UC02;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 208.
RecName: Full=TATA-box-binding protein;
AltName: Full=TATA sequence-binding protein;
AltName: Full=TATA-binding factor {ECO:0000303|PubMed:2194289, ECO:0000303|PubMed:2374612};
AltName: Full=TATA-box factor;
AltName: Full=Transcription initiation factor TFIID TBP subunit;
Name=TBP; Synonyms=GTF2D1, TF2D, TFIID {ECO:0000303|PubMed:2374612};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND VARIANT
92-GLN--GLN-95 DEL.
PubMed=2374612; DOI=10.1038/346387a0;
Hoffmann A., Sinn E., Yamamoto T., Wang J., Roy A., Horikoshi M.,
Roeder R.G.;
"Highly conserved core domain and unique N-terminus with presumptive
regulatory motifs in a human TATA factor (TFIID).";
Nature 346:387-390(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND
DOMAINS.
PubMed=2363050; DOI=10.1126/science.2363050;
Peterson M.G., Tanese N., Pugh B.F., Tjian R.;
"Functional domains and upstream activation properties of cloned human
TATA binding protein.";
Science 248:1625-1630(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBUNIT.
TISSUE=Fibroblast;
PubMed=2194289; DOI=10.1126/science.2194289;
Kao C.C., Lieberman P.M., Schmidt M.C., Zhou Q., Pei R., Berk A.J.;
"Cloning of a transcriptionally active human TATA binding factor.";
Science 248:1646-1650(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 ICP4.
PubMed=8392607;
Smith C.A., Bates P., Rivera-Gonzalez R., Gu B., DeLuca N.A.;
"ICP4, the major transcriptional regulatory protein of herpes simplex
virus type 1, forms a tripartite complex with TATA-binding protein and
TFIIB.";
J. Virol. 67:4676-4687(1993).
[8]
INTERACTION WITH UBTF.
PubMed=7982918;
Kwon H., Green M.R.;
"The RNA polymerase I transcription factor, upstream binding factor,
interacts directly with the TATA box-binding protein.";
J. Biol. Chem. 269:30140-30146(1994).
[9]
INTERACTION WITH HIV-1 TAT.
PubMed=8121496; DOI=10.1038/367295a0;
Kashanchi F., Piras G., Radonovich M.F., Duvall J.F., Fattaey A.,
Chiang C.M., Roeder R.G., Brady J.N.;
"Direct interaction of human TFIID with the HIV-1 transactivator
tat.";
Nature 367:295-299(1994).
[10]
INTERACTION WITH HADV E1A PROTEIN.
PubMed=8146144; DOI=10.1073/pnas.91.7.2488;
Geisberg J.V., Lee W.S., Berk A.J., Ricciardi R.P.;
"The zinc finger region of the adenovirus E1A transactivating domain
complexes with the TATA box binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 91:2488-2492(1994).
[11]
INTERACTION WITH TAF1A; TAF1B AND TAF1C.
PubMed=7801123; DOI=10.1126/science.7801123;
Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A.,
Tjian R.;
"Reconstitution of transcription factor SL1: exclusive binding of TBP
by SL1 or TFIID subunits.";
Science 266:1966-1972(1994).
[12]
INTERACTION WITH HIV-1 TAT.
PubMed=7608968; DOI=10.1006/jmbi.1995.0368;
Veschambre P., Simard P., Jalinot P.;
"Evidence for functional interaction between the HIV-1 Tat
transactivator and the TATA box binding protein in vivo.";
J. Mol. Biol. 250:169-180(1995).
[13]
INTERACTION WITH UTF1.
PubMed=9748258; DOI=10.1074/jbc.273.40.25840;
Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A.,
Muramatsu M.;
"Characterization of functional domains of an embryonic stem cell
coactivator UTF1 which are conserved and essential for potentiation of
ATF-2 activity.";
J. Biol. Chem. 273:25840-25849(1998).
[14]
IDENTIFICATION IN THE TFIID COMPLEX, AND FUNCTION.
PubMed=9836642; DOI=10.1126/science.282.5395.1900;
LeRoy G., Orphanides G., Lane W.S., Reinberg D.;
"Requirement of RSF and FACT for transcription of chromatin templates
in vitro.";
Science 282:1900-1904(1998).
[15]
INTERACTION WITH HSF1.
PubMed=11005381; DOI=10.1379/1466-1268(2000)005<0229:PTFHWT>2.0.CO;2;
Yuan C.X., Gurley W.B.;
"Potential targets for HSF1 within the preinitiation complex.";
Cell Stress Chaperones 5:229-242(2000).
[16]
FUNCTION OF THE SL1/TIF-IB COMPLEX.
PubMed=15970593; DOI=10.1074/jbc.M501595200;
Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.;
"TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex
formation and stabilizes upstream binding factor at the rDNA
promoter.";
J. Biol. Chem. 280:29551-29558(2005).
[17]
TISSUE SPECIFICITY.
PubMed=17570761; DOI=10.1089/dna.2006.0527;
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., Grillo A., Messina A.,
Ferro A., Grzeschik K.H., Purrello M.;
"Genomics, evolution, and expression of TBPL2, a member of the TBP
family.";
DNA Cell Biol. 26:369-385(2007).
[18]
INTERACTION WITH SPIB.
PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
Rao S., Matsumura A., Yoon J., Simon M.C.;
"SPI-B activates transcription via a unique proline, serine, and
threonine domain and exhibits DNA binding affinity differences from
PU.1.";
J. Biol. Chem. 274:11115-11124(1999).
[19]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
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.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional
coactivator essential for ligand-dependent transactivation by nuclear
receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[20]
INTERACTION WITH ELF3.
PubMed=10391676; DOI=10.1038/sj.onc.1202674;
Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C.;
"Exon 4-encoded acidic domain in the epithelium-restricted Ets factor,
ESX, confers potent transactivating capacity and binds to TATA-binding
protein (TBP).";
Oncogene 18:3682-3695(1999).
[21]
INTERACTION WITH BRF2.
PubMed=11564744; DOI=10.1074/jbc.M108515200;
Cabart P., Murphy S.;
"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.";
J. Biol. Chem. 276:43056-43064(2001).
[22]
INTERACTION WITH TAF3.
PubMed=11438666; DOI=10.1128/MCB.21.15.5109-5121.2001;
Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155)
are novel metazoan homologues of yeast TAFII47 containing a histone
fold and a PHD finger.";
Mol. Cell. Biol. 21:5109-5121(2001).
[23]
INTERACTION WITH TAF1L.
PubMed=12217962; DOI=10.1093/hmg/11.19.2341;
Wang P.J., Page D.C.;
"Functional substitution for TAF(II)250 by a retroposed homolog that
is expressed in human spermatogenesis.";
Hum. Mol. Genet. 11:2341-2346(2002).
[24]
INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC4, AND FUNCTION.
PubMed=12621023; DOI=10.1074/jbc.M204247200;
Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.;
"The small nuclear RNA-activating protein 190 Myb DNA binding domain
stimulates TATA box-binding protein-TATA box recognition.";
J. Biol. Chem. 278:18649-18657(2003).
[25]
INTERACTION WITH HIV-1 TAT.
PubMed=15719058; DOI=10.1371/journal.pbio.0030044;
Raha T., Cheng S.W.G., Green M.R.;
"HIV-1 Tat stimulates transcription complex assembly through
recruitment of TBP in the absence of TAFs.";
PLoS Biol. 3:221-230(2005).
[26]
INTERACTION WITH SP1.
PubMed=19106100; DOI=10.1074/jbc.M807098200;
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
Watanabe S., Saitoh N., Ito T., Nakao M.;
"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
telomerase activity.";
J. Biol. Chem. 284:5165-5174(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 159-337 IN COMPLEX WITH DNA.
PubMed=8643494; DOI=10.1073/pnas.93.10.4862;
Nikolov D.B., Chen H., Halay E.D., Hoffmann A., Roeder R.G.,
Burley S.K.;
"Crystal structure of a human TATA box-binding protein/TATA element
complex.";
Proc. Natl. Acad. Sci. U.S.A. 93:4862-4867(1996).
[29]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 159-339 IN COMPLEX WITH DNA.
PubMed=8757291; DOI=10.1006/jmbi.1996.0456;
Juo Z.S., Chiu T.K., Leiberman P.M., Baikalov I., Berk A.J.,
Dickerson R.E.;
"How proteins recognize the TATA box.";
J. Mol. Biol. 261:239-254(1996).
[30]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-337 IN COMPLEX WITH
GTF2B AND DNA.
PubMed=10619841; DOI=10.1093/emboj/19.1.25;
Tsai F.T.F., Sigler P.B.;
"Structural basis of preinitiation complex assembly on human pol II
promoters.";
EMBO J. 19:25-36(2000).
[31]
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 159-339 IN COMPLEX WITH DR1;
DRAP1 AND DNA.
PubMed=11461703; DOI=10.1016/S0092-8674(01)00417-2;
Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G.,
Meisterernst M., Burley S.K.;
"Crystal structure of negative cofactor 2 recognizing the TBP-DNA
transcription complex.";
Cell 106:71-81(2001).
[32]
POLYMORPHISM OF POLY-GLN REGION.
PubMed=10484774; DOI=10.1093/hmg/8.11.2047;
Koide R., Kobayashi S., Shimohata T., Ikeuchi T., Maruyama M.,
Saito M., Yamada M., Takahashi H., Tsuji S.;
"A neurological disease caused by an expanded CAG trinucleotide repeat
in the TATA-binding protein gene: a new polyglutamine disease?";
Hum. Mol. Genet. 8:2047-2053(1999).
[33]
POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17.
PubMed=11313753; DOI=10.1038/sj.ejhg.5200617;
Zuhlke C., Hellenbroich Y., Dalski A., Kononowa N., Hagenah J.,
Vieregge P., Riess O., Klein C., Schwinger E.;
"Different types of repeat expansion in the TATA-binding protein gene
are associated with a new form of inherited ataxia.";
Eur. J. Hum. Genet. 9:160-164(2001).
[34]
POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17.
PubMed=11448935; DOI=10.1093/hmg/10.14.1441;
Nakamura K., Jeong S.-Y., Uchihara T., Anno M., Nagashima K.,
Nagashima T., Ikeda S., Tsuji S., Kanazawa I.;
"SCA17, a novel autosomal dominant cerebellar ataxia caused by an
expanded polyglutamine in TATA-binding protein.";
Hum. Mol. Genet. 10:1441-1448(2001).
[35]
POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17.
PubMed=11939898; DOI=10.1001/archneur.59.4.623;
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., Tsuji S., Holmes S.E., Margolis R.L., Jardim L.,
Pandolfo M., Coutinho P., Sequeiros J.;
"Trinucleotide repeats in 202 families with ataxia: a small expanded
(CAG)n allele at the SCA17 locus.";
Arch. Neurol. 59:623-629(2002).
[36]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 159-339 IN COMPLEX WITH BRF2
AND DNA, FUNCTION, AND SUBUNIT.
PubMed=26638071; DOI=10.1016/j.cell.2015.11.005;
Gouge J., Satia K., Guthertz N., Widya M., Thompson A.J., Cousin P.,
Dergai O., Hernandez N., Vannini A.;
"Redox signaling by the RNA polymerase III TFIIB-related factor
Brf2.";
Cell 163:1375-1387(2015).
[37]
STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, AND
SUBUNIT.
PubMed=27193682; DOI=10.1038/nature17970;
He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.;
"Near-atomic resolution visualization of human transcription promoter
opening.";
Nature 533:359-365(2016).
[38]
STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=27007846; DOI=10.1038/nature17394;
Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.;
"Structure of promoter-bound TFIID and model of human pre-initiation
complex assembly.";
Nature 531:604-609(2016).
-!- FUNCTION: General transcription factor that functions at the core
of the DNA-binding multiprotein factor TFIID (PubMed:2374612,
PubMed:2363050, PubMed:2194289, PubMed:9836642, PubMed:27193682).
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
(PubMed:2374612, PubMed:2363050, PubMed:2194289, PubMed:9836642,
PubMed:27193682). Component of a BRF2-containing transcription
factor complex that regulates transcription mediated by RNA
polymerase III (PubMed:26638071). Component of the transcription
factor SL1/TIF-IB complex, which is involved in the assembly of
the PIC (pre-initiation complex) during RNA polymerase I-dependent
transcription (PubMed:15970593). 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.
{ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:2194289,
ECO:0000269|PubMed:2363050, ECO:0000269|PubMed:2374612,
ECO:0000269|PubMed:26638071, ECO:0000269|PubMed:27193682,
ECO:0000269|PubMed:9836642, ECO:0000305}.
-!- SUBUNIT: Binds DNA as monomer (PubMed:2374612, PubMed:2194289).
Belongs to the TFIID complex together with the TBP-associated
factors (TAFs) (PubMed:9836642, PubMed:27007846). Part of a TFIID-
containing RNA polymerase II pre-initiation complex that is
composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2,
GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2,
ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9,
TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846). Component of the
transcription factor SL1/TIF-IB complex, composed of TBP and at
least TAF1A, TAF1B, TAF1C and TAF1D (PubMed:7801123). Association
of TBP to form either TFIID or SL1/TIF-IB appears to be mutually
exclusive (PubMed:7801123). Interacts with TAF1A, TAF1B and TAF1C
(PubMed:7801123). Interacts with TFIIB, NCOA6, DRAP1, DR1 and ELF3
(PubMed:10567404, PubMed:10391676, PubMed:11461703). Interacts
with SPIB, SNAPC1, SNAPC2 and SNAPC4 (PubMed:10196196,
PubMed:12621023). Interacts with UTF1 (PubMed:9748258). Interacts
with BRF2; this interaction promotes recruitment of BRF2 to TATA
box-containing promoters (PubMed:11564744, PubMed:26638071).
Interacts with UBTF (PubMed:7982918). Interacts with GPBP1 (By
similarity). Interacts with CITED2 (By similarity). Interacts with
ATF7IP (Probable). Interacts with HIV-1 Tat (PubMed:8121496,
PubMed:7608968, PubMed:15719058). Interacts with herpes simplex
virus 1 ICP4 (PubMed:8392607). Interacts with human adenovirus E1A
protein; this interaction probably disrupts the TBP-TATA complex
(PubMed:8146144). Interacts with LLPH (By similarity). Interacts
with HSF1 (via transactivation domain) (PubMed:11005381).
{ECO:0000250|UniProtKB:P29037, ECO:0000269|PubMed:10196196,
ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:10567404,
ECO:0000269|PubMed:10619841, ECO:0000269|PubMed:11005381,
ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:11461703,
ECO:0000269|PubMed:11564744, ECO:0000269|PubMed:12217962,
ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:15719058,
ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:26638071,
ECO:0000269|PubMed:7608968, ECO:0000269|PubMed:7801123,
ECO:0000269|PubMed:7982918, ECO:0000269|PubMed:8121496,
ECO:0000269|PubMed:8146144, ECO:0000269|PubMed:8392607,
ECO:0000269|PubMed:8643494, ECO:0000269|PubMed:8757291,
ECO:0000269|PubMed:9748258, ECO:0000269|PubMed:9836642}.
-!- INTERACTION:
O60869-1:EDF1; NbExp=2; IntAct=EBI-355371, EBI-781310;
P52657:GTF2A2; NbExp=2; IntAct=EBI-355371, EBI-1045262;
Q00403:GTF2B; NbExp=2; IntAct=EBI-355371, EBI-389564;
P87662:ICP0 (xeno); NbExp=2; IntAct=EBI-355371, EBI-11712595;
P17473:IE (xeno); NbExp=2; IntAct=EBI-12516310, EBI-11702772;
L8B1Q7:ORF6 (xeno); NbExp=3; IntAct=EBI-355371, EBI-11712334;
P20265:POU3F2; NbExp=2; IntAct=EBI-355371, EBI-1167176;
Q01105:SET; NbExp=4; IntAct=EBI-355371, EBI-1053182;
P21675:TAF1; NbExp=10; IntAct=EBI-355371, EBI-491289;
Q16514:TAF12; NbExp=2; IntAct=EBI-355371, EBI-1034238;
Q15573:TAF1A; NbExp=2; IntAct=EBI-355371, EBI-2510647;
Q53T94:TAF1B; NbExp=4; IntAct=EBI-355371, EBI-1560239;
Q15572:TAF1C; NbExp=3; IntAct=EBI-355371, EBI-2510659;
P04637:TP53; NbExp=2; IntAct=EBI-355371, EBI-366083;
Q05906:UL3 (xeno); NbExp=4; IntAct=EBI-355371, EBI-11702805;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27007846}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P20226-1; Sequence=Displayed;
Name=2;
IsoId=P20226-2; Sequence=VSP_045488;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, with levels highest in the
testis and ovary. {ECO:0000269|PubMed:17570761}.
-!- 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.
-!- 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. {ECO:0000269|PubMed:11313753,
ECO:0000269|PubMed:11448935, ECO:0000269|PubMed:11939898}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X54993; CAA38736.1; -; mRNA.
EMBL; M55654; AAA36731.1; -; mRNA.
EMBL; M34960; AAC03409.1; -; mRNA.
EMBL; AK304648; BAG65425.1; -; mRNA.
EMBL; CR456776; CAG33057.1; -; mRNA.
EMBL; AL031259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS5315.1; -. [P20226-1]
CCDS; CCDS55077.1; -. [P20226-2]
PIR; A34830; TWHU2D.
RefSeq; NP_001165556.1; NM_001172085.1. [P20226-2]
RefSeq; NP_003185.1; NM_003194.4. [P20226-1]
UniGene; Hs.590872; -.
PDB; 1C9B; X-ray; 2.65 A; B/F/J/N/R=159-337.
PDB; 1CDW; X-ray; 1.90 A; A=159-337.
PDB; 1JFI; X-ray; 2.62 A; C=159-339.
PDB; 1NVP; X-ray; 2.10 A; A=159-339.
PDB; 1TGH; X-ray; 2.90 A; A=156-339.
PDB; 4ROC; X-ray; 1.90 A; B=159-339.
PDB; 4ROD; X-ray; 2.70 A; B=159-339.
PDB; 4ROE; X-ray; 2.20 A; B=159-339.
PDB; 5FUR; EM; 8.50 A; A=1-339.
PDB; 5IY6; EM; 7.20 A; P=1-339.
PDB; 5IY7; EM; 8.60 A; P=1-339.
PDB; 5IY8; EM; 7.90 A; P=1-339.
PDB; 5IY9; EM; 6.30 A; P=1-339.
PDB; 5IYA; EM; 5.40 A; P=1-339.
PDB; 5IYB; EM; 3.90 A; P=1-339.
PDB; 5IYC; EM; 3.90 A; P=1-339.
PDB; 5IYD; EM; 3.90 A; P=1-339.
PDB; 5N9G; X-ray; 2.70 A; B/G=159-339.
PDBsum; 1C9B; -.
PDBsum; 1CDW; -.
PDBsum; 1JFI; -.
PDBsum; 1NVP; -.
PDBsum; 1TGH; -.
PDBsum; 4ROC; -.
PDBsum; 4ROD; -.
PDBsum; 4ROE; -.
PDBsum; 5FUR; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5IYA; -.
PDBsum; 5IYB; -.
PDBsum; 5IYC; -.
PDBsum; 5IYD; -.
PDBsum; 5N9G; -.
ProteinModelPortal; P20226; -.
SMR; P20226; -.
BioGrid; 112771; 171.
CORUM; P20226; -.
DIP; DIP-1078N; -.
IntAct; P20226; 79.
MINT; MINT-156456; -.
STRING; 9606.ENSP00000230354; -.
iPTMnet; P20226; -.
PhosphoSitePlus; P20226; -.
SwissPalm; P20226; -.
BioMuta; TBP; -.
DMDM; 1351223; -.
EPD; P20226; -.
MaxQB; P20226; -.
PaxDb; P20226; -.
PeptideAtlas; P20226; -.
PRIDE; P20226; -.
DNASU; 6908; -.
Ensembl; ENST00000230354; ENSP00000230354; ENSG00000112592. [P20226-1]
Ensembl; ENST00000392092; ENSP00000375942; ENSG00000112592. [P20226-1]
Ensembl; ENST00000540980; ENSP00000442132; ENSG00000112592. [P20226-2]
GeneID; 6908; -.
KEGG; hsa:6908; -.
UCSC; uc003qxt.4; human. [P20226-1]
CTD; 6908; -.
DisGeNET; 6908; -.
EuPathDB; HostDB:ENSG00000112592.12; -.
GeneCards; TBP; -.
GeneReviews; TBP; -.
HGNC; HGNC:11588; TBP.
HPA; CAB009442; -.
HPA; HPA049805; -.
MalaCards; TBP; -.
MIM; 600075; gene.
MIM; 607136; phenotype.
neXtProt; NX_P20226; -.
OpenTargets; ENSG00000112592; -.
Orphanet; 98759; Spinocerebellar ataxia type 17.
PharmGKB; PA36352; -.
eggNOG; KOG3302; Eukaryota.
eggNOG; COG2101; LUCA.
GeneTree; ENSGT00410000025389; -.
HOGENOM; HOG000105164; -.
HOVERGEN; HBG044997; -.
InParanoid; P20226; -.
KO; K03120; -.
OMA; MMPYGSG; -.
OrthoDB; EOG091G0ENY; -.
PhylomeDB; P20226; -.
TreeFam; TF300102; -.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
SignaLink; P20226; -.
SIGNOR; P20226; -.
EvolutionaryTrace; P20226; -.
GeneWiki; TATA-binding_protein; -.
GenomeRNAi; 6908; -.
PRO; PR:P20226; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112592; -.
CleanEx; HS_TBP; -.
ExpressionAtlas; P20226; baseline and differential.
Genevisible; P20226; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0005672; C:transcription factor TFIIA complex; IDA:BHF-UCL.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0097550; C:transcriptional preinitiation complex; IDA:CAFA.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
GO; GO:0001047; F:core promoter binding; IDA:CAFA.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IEA:Ensembl.
GO; GO:0001129; F:RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly; IDA:CAFA.
GO; GO:0001034; F:RNA polymerase III transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:CAFA.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IDA:CAFA.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0006383; P:transcription from RNA polymerase III promoter; IDA:MGI.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd04516; TBP_eukaryotes; 1.
HAMAP; MF_00408; TATA_bind_prot_arch; 1.
InterPro; IPR000814; TBP.
InterPro; IPR030491; TBP_CS.
InterPro; IPR033710; TBP_eukaryotic.
PANTHER; PTHR10126; PTHR10126; 1.
Pfam; PF00352; TBP; 2.
PRINTS; PR00686; TIFACTORIID.
PROSITE; PS00351; TFIID; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; DNA-binding; Host-virus interaction;
Neurodegeneration; Nucleus; Polymorphism; Reference proteome; Repeat;
Spinocerebellar ataxia; Transcription; Transcription regulation;
Triplet repeat expansion.
CHAIN 1 339 TATA-box-binding protein.
/FTId=PRO_0000153956.
REPEAT 165 241 1.
REPEAT 255 332 2.
COMPBIAS 55 95 Poly-Gln.
VAR_SEQ 1 20 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045488.
VARIANT 92 95 Missing. {ECO:0000269|PubMed:2374612}.
/FTId=VAR_016987.
CONFLICT 95 95 Missing (in Ref. 4; BAG65425).
{ECO:0000305}.
CONFLICT 149 149 I -> T (in Ref. 4; BAG65425).
{ECO:0000305}.
CONFLICT 187 187 A -> R (in Ref. 3; AAC03409).
{ECO:0000305}.
STRAND 164 173 {ECO:0000244|PDB:1CDW}.
HELIX 180 186 {ECO:0000244|PDB:1CDW}.
STRAND 190 192 {ECO:0000244|PDB:1CDW}.
TURN 194 196 {ECO:0000244|PDB:1CDW}.
STRAND 198 204 {ECO:0000244|PDB:1CDW}.
TURN 205 208 {ECO:0000244|PDB:1CDW}.
STRAND 209 213 {ECO:0000244|PDB:1CDW}.
STRAND 217 222 {ECO:0000244|PDB:1CDW}.
HELIX 227 244 {ECO:0000244|PDB:1CDW}.
STRAND 251 263 {ECO:0000244|PDB:1CDW}.
HELIX 270 276 {ECO:0000244|PDB:1CDW}.
TURN 277 280 {ECO:0000244|PDB:1CDW}.
TURN 285 287 {ECO:0000244|PDB:1CDW}.
STRAND 289 295 {ECO:0000244|PDB:1CDW}.
TURN 296 299 {ECO:0000244|PDB:1CDW}.
STRAND 300 304 {ECO:0000244|PDB:1CDW}.
STRAND 308 313 {ECO:0000244|PDB:1CDW}.
HELIX 318 333 {ECO:0000244|PDB:1CDW}.
SEQUENCE 339 AA; 37698 MW; A61A578D972B970B CRC64;
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQAVAAA AVQQSTSQQA TQGTSGQAPQ
LFHSQTLTTA PLPGTTPLYP SPMTPMTPIT PATPASESSG IVPQLQNIVS TVNLGCKLDL
KTIALRARNA EYNPKRFAAV IMRIREPRTT ALIFSSGKMV CTGAKSEEQS RLAARKYARV
VQKLGFPAKF LDFKIQNMVG SCDVKFPIRL EGLVLTHQQF SSYEPELFPG LIYRMIKPRI
VLLIFVSGKV VLTGAKVRAE IYEAFENIYP ILKGFRKTT


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