TBP_HUMAN
ID TBP_HUMAN Reviewed; 339 AA.
AC P20226; B4E3B3; F5H869; Q16845; Q6IBM6; Q9UC02;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 240.
DE RecName: Full=TATA-box-binding protein;
DE AltName: Full=TATA sequence-binding protein;
DE AltName: Full=TATA-binding factor {ECO:0000303|PubMed:2194289, ECO:0000303|PubMed:2374612};
DE AltName: Full=TATA-box factor;
DE AltName: Full=Transcription initiation factor TFIID TBP subunit;
GN Name=TBP; Synonyms=GTF2D1, TF2D, TFIID {ECO:0000303|PubMed:2374612};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND VARIANT
RP 92-GLN--GLN-95 DEL.
RX PubMed=2374612; DOI=10.1038/346387a0;
RA Hoffmann A., Sinn E., Yamamoto T., Wang J., Roy A., Horikoshi M.,
RA Roeder R.G.;
RT "Highly conserved core domain and unique N-terminus with presumptive
RT regulatory motifs in a human TATA factor (TFIID).";
RL Nature 346:387-390(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND DOMAINS.
RX PubMed=2363050; DOI=10.1126/science.2363050;
RA Peterson M.G., Tanese N., Pugh B.F., Tjian R.;
RT "Functional domains and upstream activation properties of cloned human TATA
RT binding protein.";
RL Science 248:1625-1630(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBUNIT.
RC TISSUE=Fibroblast;
RX PubMed=2194289; DOI=10.1126/science.2194289;
RA Kao C.C., Lieberman P.M., Schmidt M.C., Zhou Q., Pei R., Berk A.J.;
RT "Cloning of a transcriptionally active human TATA binding factor.";
RL Science 248:1646-1650(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP INTERACTION WITH GTF2B.
RX PubMed=8504927; DOI=10.1101/gad.7.6.1021;
RA Ha I., Roberts S., Maldonado E., Sun X., Kim L.U., Green M., Reinberg D.;
RT "Multiple functional domains of human transcription factor IIB: distinct
RT interactions with two general transcription factors and RNA polymerase
RT II.";
RL Genes Dev. 7:1021-1032(1993).
RN [8]
RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 ICP4 (MICROBIAL INFECTION).
RX PubMed=8392607; DOI=10.1128/jvi.67.8.4676-4687.1993;
RA Smith C.A., Bates P., Rivera-Gonzalez R., Gu B., DeLuca N.A.;
RT "ICP4, the major transcriptional regulatory protein of herpes simplex virus
RT type 1, forms a tripartite complex with TATA-binding protein and TFIIB.";
RL J. Virol. 67:4676-4687(1993).
RN [9]
RP INTERACTION WITH UBTF.
RX PubMed=7982918; DOI=10.1016/s0021-9258(18)43788-x;
RA Kwon H., Green M.R.;
RT "The RNA polymerase I transcription factor, upstream binding factor,
RT interacts directly with the TATA box-binding protein.";
RL J. Biol. Chem. 269:30140-30146(1994).
RN [10]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=8121496; DOI=10.1038/367295a0;
RA Kashanchi F., Piras G., Radonovich M.F., Duvall J.F., Fattaey A.,
RA Chiang C.M., Roeder R.G., Brady J.N.;
RT "Direct interaction of human TFIID with the HIV-1 transactivator tat.";
RL Nature 367:295-299(1994).
RN [11]
RP INTERACTION WITH HADV E1A PROTEIN (MICROBIAL INFECTION).
RX PubMed=8146144; DOI=10.1073/pnas.91.7.2488;
RA Geisberg J.V., Lee W.S., Berk A.J., Ricciardi R.P.;
RT "The zinc finger region of the adenovirus E1A transactivating domain
RT complexes with the TATA box binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2488-2492(1994).
RN [12]
RP INTERACTION WITH TAF1A; TAF1B AND TAF1C.
RX PubMed=7801123; DOI=10.1126/science.7801123;
RA Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.;
RT "Reconstitution of transcription factor SL1: exclusive binding of TBP by
RT SL1 or TFIID subunits.";
RL Science 266:1966-1972(1994).
RN [13]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=7608968; DOI=10.1006/jmbi.1995.0368;
RA Veschambre P., Simard P., Jalinot P.;
RT "Evidence for functional interaction between the HIV-1 Tat transactivator
RT and the TATA box binding protein in vivo.";
RL J. Mol. Biol. 250:169-180(1995).
RN [14]
RP INTERACTION WITH UTF1.
RX PubMed=9748258; DOI=10.1074/jbc.273.40.25840;
RA Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M.;
RT "Characterization of functional domains of an embryonic stem cell
RT coactivator UTF1 which are conserved and essential for potentiation of ATF-
RT 2 activity.";
RL J. Biol. Chem. 273:25840-25849(1998).
RN [15]
RP IDENTIFICATION IN THE TFIID COMPLEX, AND FUNCTION.
RX PubMed=9836642; DOI=10.1126/science.282.5395.1900;
RA LeRoy G., Orphanides G., Lane W.S., Reinberg D.;
RT "Requirement of RSF and FACT for transcription of chromatin templates in
RT vitro.";
RL Science 282:1900-1904(1998).
RN [16]
RP INTERACTION WITH PAX5.
RX PubMed=10197586;
RA Eberhard D., Busslinger M.;
RT "The partial homeodomain of the transcription factor Pax-5 (BSAP) is an
RT interaction motif for the retinoblastoma and TATA-binding proteins.";
RL Cancer Res. 59:1716-1724(1999).
RN [17]
RP INTERACTION WITH HSF1.
RX PubMed=11005381; DOI=10.1379/1466-1268(2000)005<0229:ptfhwt>2.0.co;2;
RA Yuan C.X., Gurley W.B.;
RT "Potential targets for HSF1 within the preinitiation complex.";
RL Cell Stress Chaperones 5:229-242(2000).
RN [18]
RP FUNCTION OF THE SL1/TIF-IB COMPLEX.
RX PubMed=15970593; DOI=10.1074/jbc.m501595200;
RA Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.;
RT "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex
RT formation and stabilizes upstream binding factor at the rDNA promoter.";
RL J. Biol. Chem. 280:29551-29558(2005).
RN [19]
RP TISSUE SPECIFICITY.
RX PubMed=17570761; DOI=10.1089/dna.2006.0527;
RA Di Pietro C., Ragusa M., Duro L., Guglielmino M.R., Barbagallo D.,
RA Carnemolla A., Lagana A., Buffa P., Angelica R., Rinaldi A., Calafato M.S.,
RA Milicia I., Caserta C., Giugno R., Pulvirenti A., Giunta V., Rapisarda A.,
RA Di Pietro V., Grillo A., Messina A., Ferro A., Grzeschik K.H., Purrello M.;
RT "Genomics, evolution, and expression of TBPL2, a member of the TBP
RT family.";
RL DNA Cell Biol. 26:369-385(2007).
RN [20]
RP INTERACTION WITH SPIB.
RX PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
RA Rao S., Matsumura A., Yoon J., Simon M.C.;
RT "SPI-B activates transcription via a unique proline, serine, and threonine
RT domain and exhibits DNA binding affinity differences from PU.1.";
RL J. Biol. Chem. 274:11115-11124(1999).
RN [21]
RP INTERACTION WITH NCOA6.
RX PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
RA Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K.,
RA Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H.,
RA Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
RT essential for ligand-dependent transactivation by nuclear receptors in
RT vivo.";
RL J. Biol. Chem. 274:34283-34293(1999).
RN [22]
RP INTERACTION WITH ELF3.
RX PubMed=10391676; DOI=10.1038/sj.onc.1202674;
RA Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C.;
RT "Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX,
RT confers potent transactivating capacity and binds to TATA-binding protein
RT (TBP).";
RL Oncogene 18:3682-3695(1999).
RN [23]
RP INTERACTION WITH BRF2.
RX PubMed=11564744; DOI=10.1074/jbc.m108515200;
RA Cabart P., Murphy S.;
RT "BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of
RT polymerase III small nuclear RNA gene promoters through its interaction
RT with TATA-binding protein.";
RL J. Biol. Chem. 276:43056-43064(2001).
RN [24]
RP INTERACTION WITH TAF3.
RX PubMed=11438666; DOI=10.1128/mcb.21.15.5109-5121.2001;
RA Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are
RT novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT PHD finger.";
RL Mol. Cell. Biol. 21:5109-5121(2001).
RN [25]
RP INTERACTION WITH TAF1L.
RX PubMed=12217962; DOI=10.1093/hmg/11.19.2341;
RA Wang P.J., Page D.C.;
RT "Functional substitution for TAF(II)250 by a retroposed homolog that is
RT expressed in human spermatogenesis.";
RL Hum. Mol. Genet. 11:2341-2346(2002).
RN [26]
RP INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC4, AND FUNCTION.
RX PubMed=12621023; DOI=10.1074/jbc.m204247200;
RA Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.;
RT "The small nuclear RNA-activating protein 190 Myb DNA binding domain
RT stimulates TATA box-binding protein-TATA box recognition.";
RL J. Biol. Chem. 278:18649-18657(2003).
RN [27]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=15719058; DOI=10.1371/journal.pbio.0030044;
RA Raha T., Cheng S.W.G., Green M.R.;
RT "HIV-1 Tat stimulates transcription complex assembly through recruitment of
RT TBP in the absence of TAFs.";
RL PLoS Biol. 3:221-230(2005).
RN [28]
RP INTERACTION WITH SP1.
RX PubMed=19106100; DOI=10.1074/jbc.m807098200;
RA Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
RA Watanabe S., Saitoh N., Ito T., Nakao M.;
RT "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
RT telomerase activity.";
RL J. Biol. Chem. 284:5165-5174(2009).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP INTERACTION WITH HERPES SIMPLEX VIRUS 2 PROTEIN ICP4 (MICROBIAL INFECTION).
RX PubMed=30619292; DOI=10.3389/fimmu.2018.02932;
RA Zhang M., Deng X., Guan X., Geng L., Fu M., Zhang B., Chen R., Hu H.,
RA Hu K., Zhang D., Li M., Liu Y., Gong S., Hu Q.;
RT "Herpes Simplex Virus Type 2 Infection-Induced Expression of CXCR3 Ligands
RT Promotes CD4+ T Cell Migration and Is Regulated by the Viral Immediate-
RT Early Protein ICP4.";
RL Front. Immunol. 9:2932-2932(2018).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 159-337 IN COMPLEX WITH DNA.
RX PubMed=8643494; DOI=10.1073/pnas.93.10.4862;
RA Nikolov D.B., Chen H., Halay E.D., Hoffmann A., Roeder R.G., Burley S.K.;
RT "Crystal structure of a human TATA box-binding protein/TATA element
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4862-4867(1996).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 159-339 IN COMPLEX WITH DNA.
RX PubMed=8757291; DOI=10.1006/jmbi.1996.0456;
RA Juo Z.S., Chiu T.K., Leiberman P.M., Baikalov I., Berk A.J.,
RA Dickerson R.E.;
RT "How proteins recognize the TATA box.";
RL J. Mol. Biol. 261:239-254(1996).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-337 IN COMPLEX WITH GTF2B AND
RP DNA.
RX PubMed=10619841; DOI=10.1093/emboj/19.1.25;
RA Tsai F.T.F., Sigler P.B.;
RT "Structural basis of preinitiation complex assembly on human pol II
RT promoters.";
RL EMBO J. 19:25-36(2000).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 159-339 IN COMPLEX WITH DR1;
RP DRAP1 AND DNA.
RX PubMed=11461703; DOI=10.1016/s0092-8674(01)00417-2;
RA Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G.,
RA Meisterernst M., Burley S.K.;
RT "Crystal structure of negative cofactor 2 recognizing the TBP-DNA
RT transcription complex.";
RL Cell 106:71-81(2001).
RN [35]
RP POLYMORPHISM OF POLY-GLN REGION.
RX PubMed=10484774; DOI=10.1093/hmg/8.11.2047;
RA Koide R., Kobayashi S., Shimohata T., Ikeuchi T., Maruyama M., Saito M.,
RA Yamada M., Takahashi H., Tsuji S.;
RT "A neurological disease caused by an expanded CAG trinucleotide repeat in
RT the TATA-binding protein gene: a new polyglutamine disease?";
RL Hum. Mol. Genet. 8:2047-2053(1999).
RN [36]
RP POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17.
RX PubMed=11313753; DOI=10.1038/sj.ejhg.5200617;
RA Zuhlke C., Hellenbroich Y., Dalski A., Kononowa N., Hagenah J.,
RA Vieregge P., Riess O., Klein C., Schwinger E.;
RT "Different types of repeat expansion in the TATA-binding protein gene are
RT associated with a new form of inherited ataxia.";
RL Eur. J. Hum. Genet. 9:160-164(2001).
RN [37]
RP POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17.
RX PubMed=11448935; DOI=10.1093/hmg/10.14.1441;
RA Nakamura K., Jeong S.-Y., Uchihara T., Anno M., Nagashima K., Nagashima T.,
RA Ikeda S., Tsuji S., Kanazawa I.;
RT "SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded
RT polyglutamine in TATA-binding protein.";
RL Hum. Mol. Genet. 10:1441-1448(2001).
RN [38]
RP POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17.
RX PubMed=11939898; DOI=10.1001/archneur.59.4.623;
RA Silveira I., Miranda C., Guimaraes L., Moreira M.-C., Alonso I.,
RA Mendonca P., Ferro A., Pinto-Basto J., Coelho J., Ferreirinha F.,
RA Poirier J., Parreira E., Vale J., Januario C., Barbot C., Tuna A.,
RA Barros J., Koide R., Tsuji S., Holmes S.E., Margolis R.L., Jardim L.,
RA Pandolfo M., Coutinho P., Sequeiros J.;
RT "Trinucleotide repeats in 202 families with ataxia: a small expanded (CAG)n
RT allele at the SCA17 locus.";
RL Arch. Neurol. 59:623-629(2002).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 159-339 IN COMPLEX WITH BRF2 AND
RP DNA, FUNCTION, AND SUBUNIT.
RX PubMed=26638071; DOI=10.1016/j.cell.2015.11.005;
RA Gouge J., Satia K., Guthertz N., Widya M., Thompson A.J., Cousin P.,
RA Dergai O., Hernandez N., Vannini A.;
RT "Redox signaling by the RNA polymerase III TFIIB-related factor Brf2.";
RL Cell 163:1375-1387(2015).
RN [40]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=27193682; DOI=10.1038/nature17970;
RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.;
RT "Near-atomic resolution visualization of human transcription promoter
RT opening.";
RL Nature 533:359-365(2016).
RN [41]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27007846; DOI=10.1038/nature17394;
RA Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.;
RT "Structure of promoter-bound TFIID and model of human pre-initiation
RT complex assembly.";
RL Nature 531:604-609(2016).
RN [42] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGF}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.16 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE TFIID COMPLEX, AND SUBUNIT.
RX PubMed=33795473; DOI=10.1126/science.aba8490;
RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z.,
RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.;
RT "Structural insights into preinitiation complex assembly on core
RT promoters.";
RL Science 372:0-0(2021).
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription (PubMed:33795473). TFIID recognizes and binds promoters
CC with or without a TATA box via its subunit TBP, a TATA-box-binding
CC protein, and promotes assembly of the pre-initiation complex (PIC)
CC (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050,
CC PubMed:2374612). The TFIID complex consists of TBP and TBP-associated
CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7,
CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473,
CC PubMed:27007846). The TFIID complex structure can be divided into 3
CC modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TBP forms the
CC TFIID-A module together with TAF3 and TAF5 (PubMed:33795473). TBP is a
CC general transcription factor that functions at the core of the TFIID
CC complex (PubMed:33795473, PubMed:27193682, PubMed:2194289,
CC PubMed:2363050, PubMed:2374612, PubMed:9836642). During assembly of the
CC core PIC on the promoter, as part of TFIID, TBP binds to and also bends
CC promoter DNA, irrespective of whether the promoter contains a TATA box
CC (PubMed:33795473). Component of a BRF2-containing transcription factor
CC complex that regulates transcription mediated by RNA polymerase III
CC (PubMed:26638071). Component of the transcription factor SL1/TIF-IB
CC complex, which is involved in the assembly of the PIC during RNA
CC polymerase I-dependent transcription (PubMed:15970593). The rate of PIC
CC formation probably is primarily dependent on the rate of association of
CC SL1 with the rDNA promoter (PubMed:15970593). SL1 is involved in
CC stabilization of nucleolar transcription factor 1/UBTF on rDNA
CC (PubMed:15970593). {ECO:0000269|PubMed:15970593,
CC ECO:0000269|PubMed:2194289, ECO:0000269|PubMed:2363050,
CC ECO:0000269|PubMed:2374612, ECO:0000269|PubMed:26638071,
CC ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:27193682,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:9836642}.
CC -!- SUBUNIT: Binds DNA as monomer (PubMed:2194289, PubMed:2374612).
CC Component of the TFIID basal transcription factor complex, composed of
CC TATA-box-binding protein TBP, and a number of TBP-associated factors
CC (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9,
CC TAF10, TAF11, TAF12 and TAF13 (PubMed:9836642, PubMed:27007846,
CC PubMed:33795473). Part of a TFIID-containing RNA polymerase II pre-
CC initiation complex that is composed of TBP and at least GTF2A1, GTF2A2,
CC GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1,
CC ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9,
CC TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846, PubMed:33795473).
CC Component of the transcription factor SL1/TIF-IB complex, composed of
CC TBP and at least TAF1A, TAF1B, TAF1C and TAF1D (PubMed:7801123).
CC Association of TBP to form either TFIID or SL1/TIF-IB appears to be
CC mutually exclusive (PubMed:7801123). Interacts with TAF1A, TAF1B and
CC TAF1C (PubMed:7801123). Interacts with TFIIB, NCOA6, DRAP1, DR1 and
CC ELF3 (PubMed:11461703, PubMed:10391676, PubMed:10567404). Interacts
CC with SPIB, SNAPC1, SNAPC2 and SNAPC4 (PubMed:12621023,
CC PubMed:10196196). Interacts with UTF1 (PubMed:9748258). Interacts with
CC BRF2; this interaction promotes recruitment of BRF2 to TATA box-
CC containing promoters (PubMed:11564744, PubMed:26638071). Interacts with
CC UBTFD (PubMed:7982918). Interacts with GPBP1D (By similarity).
CC Interacts with CITED2 (By similarity). Interacts with ATF7IP
CC (Probable). Interacts with LLPH (By similarity). Interacts with HSF1
CC (via transactivation domain) (PubMed:11005381). Interacts with GTF2B
CC (via C-terminus); this interaction with promoter-bound TBP guides RNA
CC polymerase II into the pre-initiation complex (PIC) (PubMed:8504927).
CC Interacts with PAX5 (PubMed:10197586). {ECO:0000250|UniProtKB:P29037,
CC ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:10197586,
CC ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:10567404,
CC ECO:0000269|PubMed:11005381, ECO:0000269|PubMed:11461703,
CC ECO:0000269|PubMed:11564744, ECO:0000269|PubMed:12621023,
CC ECO:0000269|PubMed:2194289, ECO:0000269|PubMed:2374612,
CC ECO:0000269|PubMed:26638071, ECO:0000269|PubMed:27007846,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:7801123,
CC ECO:0000269|PubMed:7982918, ECO:0000269|PubMed:8504927,
CC ECO:0000269|PubMed:9748258, ECO:0000269|PubMed:9836642}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:15719058, ECO:0000269|PubMed:7608968,
CC ECO:0000269|PubMed:8121496}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC ICP4. {ECO:0000269|PubMed:8392607}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 2
CC ICP4. {ECO:0000269|PubMed:30619292}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus E1A
CC protein; this interaction probably disrupts the TBP-TATA complex.
CC {ECO:0000269|PubMed:8146144}.
CC -!- INTERACTION:
CC P20226; P05067: APP; NbExp=3; IntAct=EBI-355371, EBI-77613;
CC P20226; Q00535: CDK5; NbExp=3; IntAct=EBI-355371, EBI-1041567;
CC P20226; O60869-1: EDF1; NbExp=2; IntAct=EBI-355371, EBI-781310;
CC P20226; P52655: GTF2A1; NbExp=2; IntAct=EBI-355371, EBI-389518;
CC P20226; P52657: GTF2A2; NbExp=2; IntAct=EBI-355371, EBI-1045262;
CC P20226; Q00403: GTF2B; NbExp=2; IntAct=EBI-355371, EBI-389564;
CC P20226; Q16236: NFE2L2; NbExp=5; IntAct=EBI-355371, EBI-2007911;
CC P20226; P20265: POU3F2; NbExp=2; IntAct=EBI-355371, EBI-1167176;
CC P20226; Q01105: SET; NbExp=4; IntAct=EBI-355371, EBI-1053182;
CC P20226; P21675: TAF1; NbExp=10; IntAct=EBI-355371, EBI-491289;
CC P20226; Q16514: TAF12; NbExp=3; IntAct=EBI-355371, EBI-1034238;
CC P20226; Q15573: TAF1A; NbExp=2; IntAct=EBI-355371, EBI-2510647;
CC P20226; Q53T94: TAF1B; NbExp=4; IntAct=EBI-355371, EBI-1560239;
CC P20226; Q15572: TAF1C; NbExp=3; IntAct=EBI-355371, EBI-2510659;
CC P20226; P04637: TP53; NbExp=2; IntAct=EBI-355371, EBI-366083;
CC P20226; P18111: Cdx1; Xeno; NbExp=5; IntAct=EBI-355371, EBI-21005290;
CC P20226; P87662: ICP0; Xeno; NbExp=2; IntAct=EBI-355371, EBI-11712595;
CC P20226; L8B1Q7: ORF6; Xeno; NbExp=3; IntAct=EBI-355371, EBI-11712334;
CC P20226; P28159: Su(H); Xeno; NbExp=2; IntAct=EBI-355371, EBI-92180;
CC P20226; Q05906: UL3; Xeno; NbExp=4; IntAct=EBI-355371, EBI-11702805;
CC P20226-1; P17473: IE; Xeno; NbExp=2; IntAct=EBI-12516310, EBI-11702772;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27007846}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20226-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20226-2; Sequence=VSP_045488;
CC -!- TISSUE SPECIFICITY: Widely expressed, with levels highest in the testis
CC and ovary. {ECO:0000269|PubMed:17570761}.
CC -!- POLYMORPHISM: The poly-Gln region of TBP is highly polymorphic (25 to
CC 42 repeats) in normal individuals and is expanded to about 47-63
CC repeats in spinocerebellar ataxia 17 (SCA17) patients.
CC -!- DISEASE: Spinocerebellar ataxia 17 (SCA17) [MIM:607136]:
CC Spinocerebellar ataxia is a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar
CC ataxia (ADCA) characterized by widespread cerebral and cerebellar
CC atrophy, dementia and extrapyramidal signs. The molecular defect in
CC SCA17 is the expansion of a CAG repeat in the coding region of TBP.
CC Longer expansions result in earlier onset and more severe clinical
CC manifestations of the disease. {ECO:0000269|PubMed:11313753,
CC ECO:0000269|PubMed:11448935, ECO:0000269|PubMed:11939898}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
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DR EMBL; X54993; CAA38736.1; -; mRNA.
DR EMBL; M55654; AAA36731.1; -; mRNA.
DR EMBL; M34960; AAC03409.1; -; mRNA.
DR EMBL; AK304648; BAG65425.1; -; mRNA.
DR EMBL; CR456776; CAG33057.1; -; mRNA.
DR EMBL; AL031259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS5315.1; -. [P20226-1]
DR CCDS; CCDS55077.1; -. [P20226-2]
DR PIR; A34830; TWHU2D.
DR RefSeq; NP_001165556.1; NM_001172085.1. [P20226-2]
DR RefSeq; NP_003185.1; NM_003194.4. [P20226-1]
DR PDB; 1C9B; X-ray; 2.65 A; B/F/J/N/R=159-337.
DR PDB; 1CDW; X-ray; 1.90 A; A=159-337.
DR PDB; 1JFI; X-ray; 2.62 A; C=159-339.
DR PDB; 1NVP; X-ray; 2.10 A; A=159-339.
DR PDB; 1TGH; X-ray; 2.90 A; A=156-339.
DR PDB; 4ROC; X-ray; 1.90 A; B=159-339.
DR PDB; 4ROD; X-ray; 2.70 A; B=159-339.
DR PDB; 4ROE; X-ray; 2.20 A; B=159-339.
DR PDB; 5FUR; EM; 8.50 A; A=1-339.
DR PDB; 5IY6; EM; 7.20 A; P=1-339.
DR PDB; 5IY7; EM; 8.60 A; P=1-339.
DR PDB; 5IY8; EM; 7.90 A; P=1-339.
DR PDB; 5IY9; EM; 6.30 A; P=1-339.
DR PDB; 5IYA; EM; 5.40 A; P=1-339.
DR PDB; 5IYB; EM; 3.90 A; P=1-339.
DR PDB; 5IYC; EM; 3.90 A; P=1-339.
DR PDB; 5IYD; EM; 3.90 A; P=1-339.
DR PDB; 5N9G; X-ray; 2.70 A; B/G=159-339.
DR PDB; 6MZD; EM; 9.80 A; T=1-339.
DR PDB; 6MZL; EM; 23.00 A; T=1-339.
DR PDB; 6MZM; EM; 7.50 A; T=1-339.
DR PDB; 6O9L; EM; 7.20 A; P=1-339.
DR PDB; 7EDX; EM; 4.50 A; P=1-339.
DR PDB; 7EG7; EM; 6.20 A; P=1-339.
DR PDB; 7EG8; EM; 7.40 A; P=1-339.
DR PDB; 7EG9; EM; 3.70 A; P=1-339.
DR PDB; 7EGA; EM; 4.10 A; P=1-339.
DR PDB; 7EGB; EM; 3.30 A; P=1-339.
DR PDB; 7EGC; EM; 3.90 A; P=1-339.
DR PDB; 7EGD; EM; 6.75 A; P=1-339.
DR PDB; 7EGE; EM; 9.00 A; P=1-339.
DR PDB; 7EGF; EM; 3.16 A; P=1-339.
DR PDB; 7EGI; EM; 9.82 A; P=1-339.
DR PDB; 7EGJ; EM; 8.64 A; P=1-339.
DR PDB; 7ENA; EM; 4.07 A; DP=1-339.
DR PDB; 7ENC; EM; 4.13 A; DP=1-339.
DR PDB; 7LBM; EM; 4.80 A; P=1-339.
DR PDB; 7NVR; EM; 4.50 A; O=1-339.
DR PDB; 7NVS; EM; 2.80 A; O=1-339.
DR PDB; 7NVT; EM; 2.90 A; O=1-339.
DR PDB; 7NVU; EM; 2.50 A; O=1-339.
DR PDB; 7NVY; EM; 7.30 A; O=1-339.
DR PDB; 7NVZ; EM; 7.20 A; O=1-339.
DR PDB; 7NW0; EM; 6.60 A; O=1-339.
DR PDBsum; 1C9B; -.
DR PDBsum; 1CDW; -.
DR PDBsum; 1JFI; -.
DR PDBsum; 1NVP; -.
DR PDBsum; 1TGH; -.
DR PDBsum; 4ROC; -.
DR PDBsum; 4ROD; -.
DR PDBsum; 4ROE; -.
DR PDBsum; 5FUR; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 5N9G; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
DR PDBsum; 6MZM; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7EGD; -.
DR PDBsum; 7EGE; -.
DR PDBsum; 7EGF; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVS; -.
DR PDBsum; 7NVT; -.
DR PDBsum; 7NVU; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; P20226; -.
DR SMR; P20226; -.
DR BioGRID; 112771; 234.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR CORUM; P20226; -.
DR DIP; DIP-1078N; -.
DR IntAct; P20226; 101.
DR MINT; P20226; -.
DR STRING; 9606.ENSP00000375942; -.
DR GlyGen; P20226; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P20226; -.
DR PhosphoSitePlus; P20226; -.
DR SwissPalm; P20226; -.
DR BioMuta; TBP; -.
DR DMDM; 1351223; -.
DR EPD; P20226; -.
DR jPOST; P20226; -.
DR MassIVE; P20226; -.
DR MaxQB; P20226; -.
DR PaxDb; P20226; -.
DR PeptideAtlas; P20226; -.
DR PRIDE; P20226; -.
DR ProteomicsDB; 27699; -.
DR ProteomicsDB; 53733; -. [P20226-1]
DR Antibodypedia; 4001; 619 antibodies from 45 providers.
DR DNASU; 6908; -.
DR Ensembl; ENST00000230354.10; ENSP00000230354.5; ENSG00000112592.15. [P20226-1]
DR Ensembl; ENST00000392092.7; ENSP00000375942.2; ENSG00000112592.15. [P20226-1]
DR Ensembl; ENST00000540980.5; ENSP00000442132.1; ENSG00000112592.15. [P20226-2]
DR GeneID; 6908; -.
DR KEGG; hsa:6908; -.
DR MANE-Select; ENST00000392092.7; ENSP00000375942.2; NM_003194.5; NP_003185.1.
DR UCSC; uc003qxt.4; human. [P20226-1]
DR CTD; 6908; -.
DR DisGeNET; 6908; -.
DR GeneCards; TBP; -.
DR GeneReviews; TBP; -.
DR HGNC; HGNC:11588; TBP.
DR HPA; ENSG00000112592; Low tissue specificity.
DR MalaCards; TBP; -.
DR MIM; 600075; gene.
DR MIM; 607136; phenotype.
DR neXtProt; NX_P20226; -.
DR OpenTargets; ENSG00000112592; -.
DR Orphanet; 98759; Spinocerebellar ataxia type 17.
DR PharmGKB; PA36352; -.
DR VEuPathDB; HostDB:ENSG00000112592; -.
DR eggNOG; KOG3302; Eukaryota.
DR GeneTree; ENSGT00940000157474; -.
DR InParanoid; P20226; -.
DR OMA; FGRTNAS; -.
DR PhylomeDB; P20226; -.
DR TreeFam; TF300102; -.
DR PathwayCommons; P20226; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P20226; -.
DR SIGNOR; P20226; -.
DR BioGRID-ORCS; 6908; 333 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; P20226; -.
DR GeneWiki; TATA-binding_protein; -.
DR GenomeRNAi; 6908; -.
DR Pharos; P20226; Tbio.
DR PRO; PR:P20226; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P20226; protein.
DR Bgee; ENSG00000112592; Expressed in left testis and 151 other tissues.
DR ExpressionAtlas; P20226; baseline and differential.
DR Genevisible; P20226; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IEA:Ensembl.
DR GO; GO:0005672; C:transcription factor TFIIA complex; IDA:BHF-UCL.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0097550; C:transcription preinitiation complex; IDA:CAFA.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0140223; F:general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:ARUK-UCL.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IMP:UniProtKB.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:CAFA.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:CAFA.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
DR CDD; cd04516; TBP_eukaryotes; 1.
DR Gene3D; 3.30.310.10; -; 2.
DR HAMAP; MF_00408; TATA_bind_prot_arch; 1.
DR IDEAL; IID00367; -.
DR InterPro; IPR000814; TBP.
DR InterPro; IPR030491; TBP_CS.
DR InterPro; IPR012295; TBP_dom_sf.
DR InterPro; IPR033710; TBP_eukaryotic.
DR PANTHER; PTHR10126; PTHR10126; 1.
DR Pfam; PF00352; TBP; 2.
DR PRINTS; PR00686; TIFACTORIID.
DR PROSITE; PS00351; TFIID; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; DNA-binding;
KW Host-virus interaction; Neurodegeneration; Nucleus; Reference proteome;
KW Repeat; Spinocerebellar ataxia; Transcription; Transcription regulation;
KW Triplet repeat expansion.
FT CHAIN 1..339
FT /note="TATA-box-binding protein"
FT /id="PRO_0000153956"
FT REPEAT 165..241
FT /note="1"
FT REPEAT 255..332
FT /note="2"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045488"
FT VARIANT 92..95
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:2374612"
FT /id="VAR_016987"
FT CONFLICT 95
FT /note="Missing (in Ref. 4; BAG65425)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="I -> T (in Ref. 4; BAG65425)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="A -> R (in Ref. 3; AAC03409)"
FT /evidence="ECO:0000305"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:1CDW"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7NVU"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1CDW"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1CDW"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1CDW"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 251..263
FT /evidence="ECO:0007829|PDB:1CDW"
FT HELIX 270..276
FT /evidence="ECO:0007829|PDB:1CDW"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:7EGF"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:1CDW"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1CDW"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:1CDW"
FT HELIX 318..333
FT /evidence="ECO:0007829|PDB:1CDW"
SQ 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
