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 27-MAR-2024, entry version 249. 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) IN COMPLEX WITH PROMOTER RP DNA, 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 PubMed:27193682). Component of the transcription factor SL1/TIF-IB CC complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D CC (PubMed:7801123). Association of TBP to form either TFIID or SL1/TIF-IB CC appears to be mutually exclusive (PubMed:7801123). Interacts with CC TAF1A, TAF1B and TAF1C (PubMed:7801123). Interacts with TFIIB, NCOA6, CC DRAP1, DR1 and ELF3 (PubMed:11461703, PubMed:10391676, CC PubMed:10567404). Interacts with SPIB, SNAPC1, SNAPC2 and SNAPC4 CC (PubMed:12621023, PubMed:10196196). Interacts with UTF1 CC (PubMed:9748258). Interacts with BRF2; this interaction promotes CC recruitment of BRF2 to TATA box-containing promoters (PubMed:11564744, CC PubMed:26638071). Interacts with UBTFD (PubMed:7982918). Interacts with CC GPBP1D (By similarity). Interacts with CITED2 (By similarity). CC Interacts with ATF7IP (Probable). Interacts with LLPH (By similarity). CC Interacts with HSF1 (via transactivation domain) (PubMed:11005381). CC Interacts with GTF2B (via C-terminus); this interaction with promoter- CC bound TBP guides RNA polymerase II into the pre-initiation complex CC (PIC) (PubMed:8504927). Interacts with PAX5 (PubMed:10197586). CC Interacts with MSX1; the interaction may inhibit MSX1 autoinactivation CC (By similarity). {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:27193682, ECO:0000269|PubMed:33795473, CC ECO:0000269|PubMed:7801123, ECO:0000269|PubMed:7982918, CC ECO:0000269|PubMed:8504927, ECO:0000269|PubMed:9748258, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7ZWC; EM; 3.20 A; O=1-339. DR PDB; 7ZWD; EM; 3.00 A; O=1-339. DR PDB; 7ZX7; EM; 3.40 A; O=1-339. DR PDB; 7ZX8; EM; 3.00 A; O=1-339. DR PDB; 7ZXE; EM; 3.50 A; O=1-339. DR PDB; 8BVW; EM; 4.00 A; O=1-339. DR PDB; 8BYQ; EM; 4.10 A; O=1-339. DR PDB; 8BZ1; EM; 3.80 A; O=1-339. DR PDB; 8GXQ; EM; 5.04 A; DP=1-339. DR PDB; 8GXS; EM; 4.16 A; DP=1-339. DR PDB; 8ITY; EM; 3.90 A; U=1-339. DR PDB; 8IUE; EM; 4.10 A; U=1-339. DR PDB; 8IUH; EM; 3.40 A; U=1-339. DR PDB; 8WAK; EM; 5.47 A; P=1-339. DR PDB; 8WAL; EM; 8.52 A; P=1-339. DR PDB; 8WAN; EM; 6.07 A; P=1-339. DR PDB; 8WAO; EM; 6.40 A; P=1-339. DR PDB; 8WAP; EM; 5.85 A; P=1-339. DR PDB; 8WAQ; EM; 6.29 A; P=1-339. DR PDB; 8WAR; EM; 7.20 A; P=1-339. DR PDB; 8WAS; EM; 6.13 A; P=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 PDBsum; 7ZWC; -. DR PDBsum; 7ZWD; -. DR PDBsum; 7ZX7; -. DR PDBsum; 7ZX8; -. DR PDBsum; 7ZXE; -. DR PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8BZ1; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8ITY; -. DR PDBsum; 8IUE; -. DR PDBsum; 8IUH; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; P20226; -. DR EMDB; EMD-12610; -. DR EMDB; EMD-12611; -. DR EMDB; EMD-12612; -. DR EMDB; EMD-12613; -. DR EMDB; EMD-12617; -. DR EMDB; EMD-12618; -. DR EMDB; EMD-12619; -. DR EMDB; EMD-14996; -. DR EMDB; EMD-14997; -. DR EMDB; EMD-15006; -. DR EMDB; EMD-15007; -. DR EMDB; EMD-15009; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-16335; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-31075; -. DR EMDB; EMD-31107; -. DR EMDB; EMD-31108; -. DR EMDB; EMD-31109; -. DR EMDB; EMD-31110; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31113; -. DR EMDB; EMD-31114; -. DR EMDB; EMD-31115; -. DR EMDB; EMD-31118; -. DR EMDB; EMD-31119; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-3307; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-35712; -. DR EMDB; EMD-35719; -. DR EMDB; EMD-35722; -. DR EMDB; EMD-8132; -. DR EMDB; EMD-8133; -. DR EMDB; EMD-8134; -. DR EMDB; EMD-8135; -. DR EMDB; EMD-8136; -. DR EMDB; EMD-8137; -. DR EMDB; EMD-8138; -. DR EMDB; EMD-9302; -. DR EMDB; EMD-9305; -. DR EMDB; EMD-9306; -. DR SMR; P20226; -. DR BioGRID; 112771; 261. DR ComplexPortal; CPX-2396; General transcription factor TFIII3B complex, BRF1 variant. DR ComplexPortal; CPX-2397; General transcription factor TFIII3B complex, BRF2 variant. DR ComplexPortal; CPX-2398; General transcription factor TFIIB-TBP complex. DR ComplexPortal; CPX-7978; RNA polymerase I selectivity factor 1 compex. 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.ENSP00000230354; -. DR GlyCosmos; P20226; 1 site, 1 glycan. 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; 9606-ENSP00000375942; -. DR PeptideAtlas; P20226; -. DR ProteomicsDB; 27699; -. DR ProteomicsDB; 53733; -. [P20226-1] DR Pumba; P20226; -. DR Antibodypedia; 4001; 709 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 AGR; HGNC:11588; -. 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; NMDQNNS; -. DR OrthoDB; 996519at2759; -. 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; 356 hits in 1150 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 153 other cell types or tissues. DR ExpressionAtlas; P20226; baseline and differential. 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: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: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 by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:CAFA. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. 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 at RNA polymerase II promoter; TAS:ProtInc. DR CDD; cd04516; TBP_eukaryotes; 1. DR Gene3D; 3.30.310.10; TATA-Binding Protein; 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; TATA-BOX BINDING PROTEIN; 1. DR PANTHER; PTHR10126:SF20; TATA-BOX-BINDING PROTEIN; 1. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR SUPFAM; SSF55945; TATA-box binding protein-like; 2. DR PROSITE; PS00351; TFIID; 2. DR Genevisible; P20226; HS. 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 BINDING 167 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 203 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 218 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 257 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 294 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" 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 //