ID TF2B_HUMAN Reviewed; 316 AA. AC Q00403; A8K1A7; Q5JS30; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 27-MAR-2024, entry version 235. DE RecName: Full=Transcription initiation factor IIB {ECO:0000303|PubMed:1876184}; DE EC=2.3.1.48 {ECO:0000269|PubMed:12931194}; DE AltName: Full=General transcription factor TFIIB {ECO:0000303|PubMed:1946368}; DE AltName: Full=S300-II {ECO:0000303|PubMed:1517211}; GN Name=GTF2B; Synonyms=TF2B, TFIIB; 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], FUNCTION, AND ASSOCIATION WITH THE TFIID-TFIIA RP COMPLEX. RX PubMed=1876184; DOI=10.1038/352689a0; RA Ha I., Lane W.S., Reinberg D.; RT "Cloning of a human gene encoding the general transcription initiation RT factor IIB."; RL Nature 352:689-695(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=1946368; DOI=10.1073/pnas.88.21.9553; RA Malik S., Hisatake K., Sumimoto H., Horikoshi M., Roeder R.G.; RT "Sequence of general transcription factor TFIIB and relationships to other RT initiation factors."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9553-9557(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-316, FUNCTION, AND INTERACTION WITH ESR1; RP NR2F1 AND PGR. RX PubMed=1517211; DOI=10.1016/s0021-9258(19)37087-5; RA Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.; RT "Members of the steroid hormone receptor superfamily interact with TFIIB RT (S300-II)."; RL J. Biol. Chem. 267:17617-17623(1992). RN [8] RP FUNCTION, AND IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX. RX PubMed=3818643; DOI=10.1016/s0021-9258(18)61506-6; RA Reinberg D., Horikoshi M., Roeder R.G.; RT "Factors involved in specific transcription in mammalian RNA polymerase II. RT Functional analysis of initiation factors IIA and IID and identification of RT a new factor operating at sequences downstream of the initiation site."; RL J. Biol. Chem. 262:3322-3330(1987). RN [9] RP FUNCTION, AND IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX. RX PubMed=3029109; DOI=10.1016/s0021-9258(18)61505-4; RA Reinberg D., Roeder R.G.; RT "Factors involved in specific transcription by mammalian RNA polymerase II. RT Purification and functional analysis of initiation factors IIB and IIE."; RL J. Biol. Chem. 262:3310-3321(1987). RN [10] RP ASSOCIATION WITH THE TFIID-TFIIA COMPLEX. RX PubMed=2247058; DOI=10.1128/mcb.10.12.6335-6347.1990; RA Maldonado E., Ha I., Cortes P., Weis L., Reinberg D.; RT "Factors involved in specific transcription by mammalian RNA polymerase II: RT role of transcription factors IIA, IID, and IIB during formation of a RT transcription-competent complex."; RL Mol. Cell. Biol. 10:6335-6347(1990). RN [11] RP FUNCTION, INTERACTION WITH GTF2F2; RNA POLYMERASE II AND TBP, AND RP MUTAGENESIS OF ARG-286; ARG-290 AND ARG-295. 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 [12] 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 [13] RP FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX, RP INTERACTION WITH RNA POLYMERASE II, AND DOMAIN. RX PubMed=8413225; DOI=10.1128/mcb.13.10.6253-6259.1993; RA Malik S., Lee D.K., Roeder R.G.; RT "Potential RNA polymerase II-induced interactions of transcription factor RT TFIIB."; RL Mol. Cell. Biol. 13:6253-6259(1993). RN [14] RP INTERACTION WITH HERPES VIRUS ACTIVATOR PROTEIN VP16 (MICROBIAL INFECTION), RP AND MUTAGENESIS OF ARG-185; LYS-189; ARG-193; LYS-196 AND LYS-200. RX PubMed=8515819; DOI=10.1038/363741a0; RA Roberts S.G., Ha I., Maldonado E., Reinberg D., Green M.R.; RT "Interaction between an acidic activator and transcription factor TFIIB is RT required for transcriptional activation."; RL Nature 363:741-744(1993). RN [15] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, AND DOMAINS. RX PubMed=8515820; DOI=10.1038/363744a08316289; RA Hisatake K., Roeder R.G., Horikoshi M.; RT "Functional dissection of TFIIB domains required for TFIIB-TFIID-promoter RT complex formation and basal transcription activity."; RL Nature 363:744-747(1993). RN [16] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, AND DOMAINS. RX PubMed=8516311; DOI=10.1073/pnas.90.12.5628; RA Barberis A., Mueller C.W., Harrison S.C., Ptashne M.; RT "Delineation of two functional regions of transcription factor TFIIB."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5628-5632(1993). RN [17] RP FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX, DOMAIN, RP AND MUTAGENESIS OF CYS-37 AND GLY-247. RX PubMed=8516312; DOI=10.1073/pnas.90.12.5633; RA Buratowski S., Zhou H.; RT "Functional domains of transcription factor TFIIB."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5633-5637(1993). RN [18] RP INTERACTION WITH TCEA2. RX PubMed=8566795; DOI=10.1016/0378-1119(95)00634-6; RA Umehara T., Kida S., Yamamoto T., Horikoshi M.; RT "Isolation and characterization of a cDNA encoding a new type of human RT transcription elongation factor S-II."; RL Gene 167:297-302(1995). RN [19] RP FUNCTION, AND IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX. RX PubMed=7601352; DOI=10.1101/gad.9.12.1479; RA Zawel L., Kumar K.P., Reinberg D.; RT "Recycling of the general transcription factors during RNA polymerase II RT transcription."; RL Genes Dev. 9:1479-1490(1995). RN [20] RP INTERACTION WITH EBV EBNA2 (MICROBIAL INFECTION). RX PubMed=7983760; DOI=10.1128/jvi.69.1.585-588.1995; RA Tong X., Wang F., Thut C.J., Kieff E.; RT "The Epstein-Barr virus nuclear protein 2 acidic domain can interact with RT TFIIB, TAF40, and RPA70 but not with TATA-binding protein."; RL J. Virol. 69:585-588(1995). RN [21] RP INTERACTION WITH GTF2F1 AND GTF2F2, AND REGION. RX PubMed=8662660; DOI=10.1074/jbc.271.20.11703; RA Fang S.M., Burton Z.F.; RT "RNA polymerase II-associated protein (RAP) 74 binds transcription factor RT (TF) IIB and blocks TFIIB-RAP30 binding."; RL J. Biol. Chem. 271:11703-11709(1996). RN [22] RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION). RX PubMed=8800208; DOI=10.1006/jmbi.1996.0485; RA Agostini I., Navarro J.-M., Rey F., Bouhamdan M., Spire B., Vigne R., RA Sire J.; RT "The human immunodeficiency virus type 1 Vpr transactivator: cooperation RT with promoter-bound activator domains and binding to TFIIB."; RL J. Mol. Biol. 261:599-606(1996). RN [23] RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF VAL-283 AND ARG-286. RX PubMed=9420329; DOI=10.1101/gad.12.1.34; RA Lagrange T., Kapanidis A.N., Tang H., Reinberg D., Ebright R.H.; RT "New core promoter element in RNA polymerase II-dependent transcription: RT sequence-specific DNA binding by transcription factor IIB."; RL Genes Dev. 12:34-44(1998). RN [24] RP MUTAGENESIS OF 52-GLU--SER-56. RX PubMed=10359081; DOI=10.1016/s0014-5793(99)00501-3; RA Agostini I., Navarro J.M., Bouhamdan M., Willetts K., Rey F., Spire B., RA Vigne R., Pomerantz R., Sire J.; RT "The HIV-1 Vpr co-activator induces a conformational change in TFIIB."; RL FEBS Lett. 450:235-239(1999). RN [25] RP FUNCTION, AND MUTAGENESIS OF GLU-51 AND ARG-66. RX PubMed=10318856; DOI=10.1074/jbc.274.20.14337; RA Hawkes N.A., Roberts S.G.; RT "The role of human TFIIB in transcription start site selection in vitro and RT in vivo."; RL J. Biol. Chem. 274:14337-14343(1999). RN [26] 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 [27] RP FUNCTION, ACETYLATION AT LYS-238, AUTOACETYLATION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR RP LOCATION, MUTAGENESIS OF LYS-238, CHROMATIN-BINDING, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=12931194; DOI=10.1038/nature01899; RA Choi C.H., Hiromura M., Usheva A.; RT "Transcription factor IIB acetylates itself to regulate transcription."; RL Nature 424:965-969(2003). RN [28] RP FUNCTION, AND MUTAGENESIS OF GLY-153. RX PubMed=16230532; DOI=10.1101/gad.342405; RA Deng W., Roberts S.G.; RT "A core promoter element downstream of the TATA box that is recognized by RT TFIIB."; RL Genes Dev. 19:2418-2423(2005). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [31] 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 [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-76 AND SER-92, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [33] RP FUNCTION, FUNCTION IN HSV-1 TRANSCRIPTION AND REPLICATION (MICROBIAL RP INFECTION), SUBCELLULAR LOCATION, CHROMATIN-BINDING, ACETYLATION, AND RP TISSUE SPECIFICITY. RX PubMed=24441171; DOI=10.1038/srep03664; RA Gelev V., Zabolotny J.M., Lange M., Hiromura M., Yoo S.W., Orlando J.S., RA Kushnir A., Horikoshi N., Paquet E., Bachvarov D., Schaffer P.A., RA Usheva A.; RT "A new paradigm for transcription factor TFIIB functionality."; RL Sci. Rep. 4:3664-3664(2014). RN [34] RP STRUCTURE BY NMR OF 111-316. RX PubMed=7671313; DOI=10.1016/0092-8674(95)90483-2; RA Bagby S., Kim S., Maldonado E., Tong K.I., Reinberg D., Ikura M.; RT "Solution structure of the C-terminal core domain of human TFIIB: RT similarity to cyclin A and interaction with TATA-binding protein."; RL Cell 82:857-867(1995). RN [35] {ECO:0007744|PDB:1VOL} RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 113-316 IN COMPLEX WITH PLANT TATA RP BOX-BINDING PROTEIN AND DNA, AND DNA-BINDING. RX PubMed=7675079; DOI=10.1038/377119a0; RA Nikolov D.B., Chen H., Halay E.D., Usheva A.A., Hisatake K., Lee D.K., RA Roeder R.G., Burley S.K.; RT "Crystal structure of a TFIIB-TBP-TATA-element ternary complex."; RL Nature 377:119-128(1995). RN [36] {ECO:0007744|PDB:1TFB} RP STRUCTURE BY NMR OF 112-316. RX PubMed=9609687; DOI=10.1021/bi9801098; RA Hayashi F., Ishima R., Liu D., Tong K.I., Kim S., Reinberg D., Bagby S., RA Ikura M.; RT "Human general transcription factor TFIIB: conformational variability and RT interaction with VP16 activation domain."; RL Biochemistry 37:7941-7951(1998). RN [37] {ECO:0007744|PDB:1C9B} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 110-316 IN COMPLEX WITH TBP AND RP DNA, INTERACTION WITH TBP, AND DNA-BINDING. 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 [38] {ECO:0007744|PDB:1DL6} RP STRUCTURE BY NMR OF 2-59 IN COMPLEX WITH ZINC. RX PubMed=11045620; DOI=10.1110/ps.9.9.1743; RA Chen H.T., Legault P., Glushka J., Omichinski J.G., Scott R.A.; RT "Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and RT eucaryal transcription."; RL Protein Sci. 9:1743-1752(2000). RN [39] {ECO:0007744|PDB:1RLY, ECO:0007744|PDB:1RO4} RP STRUCTURE BY NMR OF 1-60 IN APO AND -BOUND FORMS IN COMPLEX WITH ZINC. RX PubMed=14641108; DOI=10.1042/bj20031706; RA Ghosh M., Elsby L.M., Mal T.K., Gooding J.M., Roberts S.G., Ikura M.; RT "Probing Zn2+-binding effects on the zinc-ribbon domain of human general RT transcription factor TFIIB."; RL Biochem. J. 378:317-324(2004). RN [40] {ECO:0007744|PDB:2PHG} RP STRUCTURE BY NMR OF 111-316 IN COMPLEX WITH HERPES VIRUS ACTIVATOR PROTEIN RP VP16, AND INTERACTION WITH VP16 (MICROBIAL INFECTION). RX PubMed=15654739; DOI=10.1021/bi0482912; RA Jonker H.R., Wechselberger R.W., Boelens R., Folkers G.E., Kaptein R.; RT "Structural properties of the promiscuous VP16 activation domain."; RL Biochemistry 44:827-839(2005). RN [41] {ECO:0007744|PDB:5IY6, ECO:0007744|PDB:5IY7, ECO:0007744|PDB:5IY8, ECO:0007744|PDB:5IY9, ECO:0007744|PDB:5IYA, ECO:0007744|PDB:5IYB, ECO:0007744|PDB:5IYC, ECO:0007744|PDB:5IYD} RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH PROMOTER RP DNA AND ZN(2+), IDENTIFICATION IN A COMPLEX WITH TBP-BASED PIC, FUNCTION, RP 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 [42] {ECO:0007744|PDB:5WH1} RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 107-316 OF APOPROTEIN, RP IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, INTERACTION WITH RP SSU72, AND MUTAGENESIS OF ARG-185; LYS-189; ARG-193; 200-LYS--LEU-208; RP LYS-200 AND LEU-208. RX PubMed=29158257; DOI=10.1074/jbc.m117.811521; RA Bratkowski M., Unarta I.C., Zhu L., Shubbar M., Huang X., Liu X.; RT "Structural dissection of an interaction between transcription initiation RT and termination factors implicated in promoter-terminator cross-talk."; RL J. Biol. Chem. 293:1651-1665(2018). RN [43] RP VARIANT [LARGE SCALE ANALYSIS] GLN-132. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: General transcription factor that plays a role in CC transcription initiation by RNA polymerase II (Pol II). Involved in the CC pre-initiation complex (PIC) formation and Pol II recruitment at CC promoter DNA (PubMed:1876184, PubMed:1946368, PubMed:1517211, CC PubMed:3818643, PubMed:3029109, PubMed:8413225, PubMed:8515820, CC PubMed:8516311, PubMed:8516312, PubMed:7601352, PubMed:9420329, CC PubMed:12931194, PubMed:27193682). Together with the TATA box-bound TBP CC forms the core initiation complex and provides a bridge between TBP and CC the Pol II-TFIIF complex (PubMed:8504927, PubMed:8413225, CC PubMed:8515820, PubMed:8516311, PubMed:8516312). Released from the PIC CC early following the onset of transcription during the initiation and CC elongation transition and reassociates with TBP during the next CC transcription cycle (PubMed:7601352). Associates with chromatin to core CC promoter-specific regions (PubMed:12931194, PubMed:24441171). Binds to CC two distinct DNA core promoter consensus sequence elements in a TBP- CC independent manner; these IIB-recognition elements (BREs) are localized CC immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream CC (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element CC (PubMed:9420329, PubMed:16230532, PubMed:7675079, PubMed:10619841). CC Modulates transcription start site selection (PubMed:10318856). CC Exhibits also autoacetyltransferase activity that contributes to the CC activated transcription (PubMed:12931194). CC {ECO:0000269|PubMed:10318856, ECO:0000269|PubMed:10619841, CC ECO:0000269|PubMed:12931194, ECO:0000269|PubMed:1517211, CC ECO:0000269|PubMed:16230532, ECO:0000269|PubMed:1876184, CC ECO:0000269|PubMed:1946368, ECO:0000269|PubMed:24441171, CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:3029109, CC ECO:0000269|PubMed:3818643, ECO:0000269|PubMed:7601352, CC ECO:0000269|PubMed:7675079, ECO:0000269|PubMed:8413225, CC ECO:0000269|PubMed:8504927, ECO:0000269|PubMed:8515820, CC ECO:0000269|PubMed:8516311, ECO:0000269|PubMed:8516312, CC ECO:0000269|PubMed:9420329}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000269|PubMed:12931194}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.117 mM for acetyl-CoA {ECO:0000269|PubMed:12931194}; CC -!- SUBUNIT: Found in a ternary complex with TATA box-bound TBP CC (PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, CC PubMed:10619841, PubMed:29158257). Part of a TFIID-containing RNA CC polymerase II pre-initiation complex (PIC) that is composed of TBP and CC at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, CC GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, CC TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 CC (PubMed:27193682, PubMed:27193682). Associates with TFIID-TFIIA (DA CC complex) to form TFIID-TFIIA-TFIIB (DAB complex), which is then CC recognized by RNA polymerase II (Pol II) (PubMed:1876184, CC PubMed:2247058). Found in a RNA polymerase II initiation complex CC (PubMed:3818643, PubMed:3029109, PubMed:8413225, PubMed:8516312, CC PubMed:7601352). Interacts (via C-terminus) with TBP; this interaction CC with TATA box-bound TBP guides Pol II into the PIC (PubMed:8504927, CC PubMed:10619841). Interacts (via N-terminus) with Pol II CC (PubMed:8504927, PubMed:8413225). Interacts (via C-terminus) with CC SSU72; this interaction is inhibited by SYMPK (PubMed:29158257). CC Interacts with NR2F1; this interaction is direct (PubMed:1517211). CC Interacts with PGR (PubMed:1517211). Interacts with ESR1 CC (PubMed:1517211). Interacts with GTF2F1 (via C-terminus and CC preferentially via acetylated form); this interaction prevents binding CC of GTF2B to GTF2F2 (PubMed:8662660, PubMed:12931194). Interacts with CC GTF2F2 (via N-terminus); this interaction is inhibited in presence of CC GTF2F1 (PubMed:8504927, PubMed:8662660). Interacts with the CC transcription elongation factor TCEA2 (PubMed:8566795). Interacts with CC HSF1 (via transactivation domain) (PubMed:11005381). Interacts with CC GPBP1 (By similarity). {ECO:0000250|UniProtKB:P62915, CC ECO:0000269|PubMed:10619841, ECO:0000269|PubMed:11005381, CC ECO:0000269|PubMed:12931194, ECO:0000269|PubMed:1517211, CC ECO:0000269|PubMed:1876184, ECO:0000269|PubMed:2247058, CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:29158257, CC ECO:0000269|PubMed:3029109, ECO:0000269|PubMed:3818643, CC ECO:0000269|PubMed:7601352, ECO:0000269|PubMed:8413225, CC ECO:0000269|PubMed:8504927, ECO:0000269|PubMed:8515820, CC ECO:0000269|PubMed:8516311, ECO:0000269|PubMed:8516312, CC ECO:0000269|PubMed:8566795, ECO:0000269|PubMed:8662660}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr. CC {ECO:0000269|PubMed:8800208}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA2. CC {ECO:0000269|PubMed:7983760}. CC -!- SUBUNIT: (Microbial infection) Interacts with Herpes simplex virus 1 CC protein ICP4. {ECO:0000269|PubMed:8392607}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with the CC Herpes simplex virus activator VP16; this interaction stimulates RNA CC Pol II transcription by increasing the extent of pre-initiation complex CC assembly. {ECO:0000269|PubMed:15654739, ECO:0000269|PubMed:8515819}. CC -!- INTERACTION: CC Q00403; P13928: ANXA8; NbExp=3; IntAct=EBI-389564, EBI-2556915; CC Q00403; P05067: APP; NbExp=3; IntAct=EBI-389564, EBI-77613; CC Q00403; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-389564, EBI-10254793; CC Q00403; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-389564, EBI-742750; CC Q00403; Q9H972-2: C14orf93; NbExp=3; IntAct=EBI-389564, EBI-11524174; CC Q00403; Q13191: CBLB; NbExp=3; IntAct=EBI-389564, EBI-744027; CC Q00403; Q14781-2: CBX2; NbExp=3; IntAct=EBI-389564, EBI-11974585; CC Q00403; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-389564, EBI-9087876; CC Q00403; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-389564, EBI-25842815; CC Q00403; Q14919: DRAP1; NbExp=6; IntAct=EBI-389564, EBI-712941; CC Q00403; Q09472: EP300; NbExp=2; IntAct=EBI-389564, EBI-447295; CC Q00403; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-389564, EBI-5461838; CC Q00403; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-389564, EBI-8468186; CC Q00403; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-389564, EBI-5916454; CC Q00403; Q9HCC6: HES4; NbExp=3; IntAct=EBI-389564, EBI-2680288; CC Q00403; Q13123: IK; NbExp=3; IntAct=EBI-389564, EBI-713456; CC Q00403; Q92613: JADE3; NbExp=3; IntAct=EBI-389564, EBI-10278909; CC Q00403; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-389564, EBI-2796400; CC Q00403; Q14693: LPIN1; NbExp=3; IntAct=EBI-389564, EBI-5278370; CC Q00403; Q15049: MLC1; NbExp=3; IntAct=EBI-389564, EBI-8475277; CC Q00403; P01106: MYC; NbExp=3; IntAct=EBI-389564, EBI-447544; CC Q00403; O15381-5: NVL; NbExp=3; IntAct=EBI-389564, EBI-18577082; CC Q00403; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-389564, EBI-10302990; CC Q00403; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-389564, EBI-2339674; CC Q00403; P19388: POLR2E; NbExp=5; IntAct=EBI-389564, EBI-395189; CC Q00403; Q96D59: RNF183; NbExp=3; IntAct=EBI-389564, EBI-743938; CC Q00403; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-389564, EBI-366570; CC Q00403; P62701: RPS4X; NbExp=3; IntAct=EBI-389564, EBI-354303; CC Q00403; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-389564, EBI-6257312; CC Q00403; Q8N488: RYBP; NbExp=3; IntAct=EBI-389564, EBI-752324; CC Q00403; O75446: SAP30; NbExp=3; IntAct=EBI-389564, EBI-632609; CC Q00403; P60896: SEM1; NbExp=3; IntAct=EBI-389564, EBI-79819; CC Q00403; Q8NHS9: SPATA22; NbExp=3; IntAct=EBI-389564, EBI-7067260; CC Q00403; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-389564, EBI-8345366; CC Q00403; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-389564, EBI-11123832; CC Q00403; P20226: TBP; NbExp=2; IntAct=EBI-389564, EBI-355371; CC Q00403; O43615: TIMM44; NbExp=3; IntAct=EBI-389564, EBI-861737; CC Q00403; Q15025: TNIP1; NbExp=7; IntAct=EBI-389564, EBI-357849; CC Q00403; Q7Z2T5: TRMT1L; NbExp=3; IntAct=EBI-389564, EBI-1237316; CC Q00403; O75604-3: USP2; NbExp=3; IntAct=EBI-389564, EBI-10696113; CC Q00403; P58304: VSX2; NbExp=3; IntAct=EBI-389564, EBI-6427899; CC Q00403; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-389564, EBI-25831733; CC Q00403; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-389564, EBI-18036029; CC Q00403; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-389564, EBI-12021938; CC Q00403; P10073: ZSCAN22; NbExp=3; IntAct=EBI-389564, EBI-10178224; CC Q00403; P46077: GRF4; Xeno; NbExp=2; IntAct=EBI-389564, EBI-637479; CC Q00403; P87662: ICP0; Xeno; NbExp=3; IntAct=EBI-389564, EBI-11712595; CC Q00403; P17473: IE; Xeno; NbExp=4; IntAct=EBI-389564, EBI-11702772; CC Q00403; P48281: Vdr; Xeno; NbExp=2; IntAct=EBI-389564, EBI-346797; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12931194}. Chromosome CC {ECO:0000269|PubMed:24441171}. Note=Non-acetylated form colocalizes CC with DNA in the G0/1, S and G2 phases of the cell cycle, but not during CC mitosis (PubMed:24441171). Acetylated form colocalizes at CC transcriptionally silent mitotic chromatids during mitosis at CC metaphase, anaphase, and telophase phases of the cell cycle CC (PubMed:24441171). {ECO:0000269|PubMed:24441171}. CC -!- TISSUE SPECIFICITY: Expressed in the inner cell mass forming the CC embryoblast (PubMed:24441171). Not detected in cells from the outer CC thin layer trophoblast (at protein level) (PubMed:24441171). CC {ECO:0000269|PubMed:24441171}. CC -!- DOMAIN: The TFIIB-type zinc-binding domain is necessary for the CC interaction and recruitment of RNA polymerase II to the core promoter, CC the formation of a fully competent pre-initiation complex (PIC) CC assembly and basal transcription initiation (PubMed:8515820, CC PubMed:8516311, PubMed:8516312, PubMed:8413225). The C-terminus is CC necessary and sufficient for interaction with the TATA box-bound TBP CC complex and for the formation of PIC (PubMed:8515820, PubMed:8516311, CC PubMed:8413225). {ECO:0000269|PubMed:8413225, CC ECO:0000269|PubMed:8515820, ECO:0000269|PubMed:8516311, CC ECO:0000269|PubMed:8516312}. CC -!- PTM: Acetylated (PubMed:24441171). Autoacetylated; autoacetylation at CC Lys-238 stimulates transcription activation (PubMed:12931194). CC {ECO:0000269|PubMed:12931194, ECO:0000269|PubMed:24441171}. CC -!- SIMILARITY: Belongs to the TFIIB 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; X59268; CAA41958.1; -; mRNA. DR EMBL; M76766; AAA61149.1; -; mRNA. DR EMBL; AK289822; BAF82511.1; -; mRNA. DR EMBL; AB451296; BAG70110.1; -; mRNA. DR EMBL; AL445991; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020597; AAH20597.1; -; mRNA. DR EMBL; S44184; AAB23144.1; -; mRNA. DR CCDS; CCDS715.1; -. DR PIR; S17654; TWHU2B. DR RefSeq; NP_001505.1; NM_001514.5. DR PDB; 1C9B; X-ray; 2.65 A; A/E/I/M/Q=110-316. DR PDB; 1DL6; NMR; -; A=2-59. DR PDB; 1RLY; NMR; -; A=1-60. DR PDB; 1RO4; NMR; -; A=1-60. DR PDB; 1TFB; NMR; -; A=112-316. DR PDB; 1VOL; X-ray; 2.70 A; A=113-316. DR PDB; 2PHG; NMR; -; A=112-316. DR PDB; 5IY6; EM; 7.20 A; M=1-316. DR PDB; 5IY7; EM; 8.60 A; M=1-316. DR PDB; 5IY8; EM; 7.90 A; M=1-316. DR PDB; 5IY9; EM; 6.30 A; M=1-316. DR PDB; 5IYA; EM; 5.40 A; M=1-316. DR PDB; 5IYB; EM; 3.90 A; M=1-316. DR PDB; 5IYC; EM; 3.90 A; M=1-316. DR PDB; 5IYD; EM; 3.90 A; M=1-316. DR PDB; 5WH1; X-ray; 3.39 A; A/B/C/D=107-316. DR PDB; 6O9L; EM; 7.20 A; M=1-316. DR PDB; 7EDX; EM; 4.50 A; R=1-316. DR PDB; 7EG7; EM; 6.20 A; R=1-316. DR PDB; 7EG8; EM; 7.40 A; R=1-316. DR PDB; 7EG9; EM; 3.70 A; R=1-316. DR PDB; 7EGA; EM; 4.10 A; R=1-316. DR PDB; 7EGB; EM; 3.30 A; R=1-316. DR PDB; 7EGC; EM; 3.90 A; R=1-316. DR PDB; 7ENA; EM; 4.07 A; BA=1-316. DR PDB; 7ENC; EM; 4.13 A; BA=1-316. DR PDB; 7LBM; EM; 4.80 A; O=1-316. DR PDB; 7NVR; EM; 4.50 A; M=1-316. DR PDB; 7NVS; EM; 2.80 A; M=1-316. DR PDB; 7NVT; EM; 2.90 A; M=1-316. DR PDB; 7NVU; EM; 2.50 A; M=1-316. DR PDB; 7NVY; EM; 7.30 A; M=1-316. DR PDB; 7NVZ; EM; 7.20 A; M=1-316. DR PDB; 7NW0; EM; 6.60 A; M=1-316. DR PDB; 7ZWC; EM; 3.20 A; M=1-316. DR PDB; 7ZWD; EM; 3.00 A; M=1-316. DR PDB; 7ZX7; EM; 3.40 A; M=1-316. DR PDB; 7ZX8; EM; 3.00 A; M=1-316. DR PDB; 7ZXE; EM; 3.50 A; M=1-316. DR PDB; 8BVW; EM; 4.00 A; M=1-316. DR PDB; 8BYQ; EM; 4.10 A; M=1-316. DR PDB; 8BZ1; EM; 3.80 A; M=1-316. DR PDB; 8GXQ; EM; 5.04 A; BA=1-316. DR PDB; 8GXS; EM; 4.16 A; BA=1-316. DR PDB; 8WAK; EM; 5.47 A; R=1-316. DR PDB; 8WAL; EM; 8.52 A; R=1-316. DR PDB; 8WAN; EM; 6.07 A; R=1-316. DR PDB; 8WAO; EM; 6.40 A; R=1-316. DR PDB; 8WAP; EM; 5.85 A; R=1-316. DR PDB; 8WAQ; EM; 6.29 A; R=1-316. DR PDB; 8WAR; EM; 7.20 A; R=1-316. DR PDB; 8WAS; EM; 6.13 A; R=1-316. DR PDBsum; 1C9B; -. DR PDBsum; 1DL6; -. DR PDBsum; 1RLY; -. DR PDBsum; 1RO4; -. DR PDBsum; 1TFB; -. DR PDBsum; 1VOL; -. DR PDBsum; 2PHG; -. 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; 5WH1; -. 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; 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; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; Q00403; -. 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-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. 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 SMR; Q00403; -. DR BioGRID; 109214; 137. DR ComplexPortal; CPX-2398; General transcription factor TFIIB-TBP complex. DR CORUM; Q00403; -. DR DIP; DIP-1077N; -. DR IntAct; Q00403; 99. DR MINT; Q00403; -. DR STRING; 9606.ENSP00000359531; -. DR GlyGen; Q00403; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q00403; -. DR MetOSite; Q00403; -. DR PhosphoSitePlus; Q00403; -. DR BioMuta; GTF2B; -. DR DMDM; 135629; -. DR EPD; Q00403; -. DR jPOST; Q00403; -. DR MassIVE; Q00403; -. DR MaxQB; Q00403; -. DR PaxDb; 9606-ENSP00000359531; -. DR PeptideAtlas; Q00403; -. DR ProteomicsDB; 57846; -. DR Pumba; Q00403; -. DR Antibodypedia; 19819; 518 antibodies from 36 providers. DR DNASU; 2959; -. DR Ensembl; ENST00000370500.10; ENSP00000359531.5; ENSG00000137947.12. DR GeneID; 2959; -. DR KEGG; hsa:2959; -. DR MANE-Select; ENST00000370500.10; ENSP00000359531.5; NM_001514.6; NP_001505.1. DR UCSC; uc001dmo.5; human. DR AGR; HGNC:4648; -. DR CTD; 2959; -. DR DisGeNET; 2959; -. DR GeneCards; GTF2B; -. DR HGNC; HGNC:4648; GTF2B. DR HPA; ENSG00000137947; Low tissue specificity. DR MIM; 189963; gene. DR neXtProt; NX_Q00403; -. DR OpenTargets; ENSG00000137947; -. DR PharmGKB; PA29035; -. DR VEuPathDB; HostDB:ENSG00000137947; -. DR eggNOG; KOG1597; Eukaryota. DR GeneTree; ENSGT00390000006671; -. DR InParanoid; Q00403; -. DR OMA; DHDQRMK; -. DR OrthoDB; 38673at2759; -. DR PhylomeDB; Q00403; -. DR TreeFam; TF105953; -. DR PathwayCommons; Q00403; -. 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-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. 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-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR SignaLink; Q00403; -. DR SIGNOR; Q00403; -. DR BioGRID-ORCS; 2959; 846 hits in 1175 CRISPR screens. DR ChiTaRS; GTF2B; human. DR EvolutionaryTrace; Q00403; -. DR GeneWiki; Transcription_factor_II_B; -. DR GenomeRNAi; 2959; -. DR Pharos; Q00403; Tbio. DR PRO; PR:Q00403; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q00403; Protein. DR Bgee; ENSG00000137947; Expressed in oocyte and 204 other cell types or tissues. DR ExpressionAtlas; Q00403; baseline and differential. DR GO; GO:0032153; C:cell division site; IEA:Ensembl. DR GO; GO:0005694; C:chromosome; IDA:UniProtKB. DR GO; GO:0042585; C:germinal vesicle; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:UniProtKB. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB. DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central. DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB. DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL. DR GO; GO:0017025; F:TBP-class protein binding; IPI:CAFA. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IEA:Ensembl. DR GO; GO:1904798; P:positive regulation of core promoter binding; IDA:GO_Central. DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB. DR GO; GO:1990114; P:RNA polymerase II core complex assembly; IMP:UniProtKB. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:UniProtKB. DR GO; GO:0051225; P:spindle assembly; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0019083; P:viral transcription; IDA:GO_Central. DR CDD; cd20551; CYCLIN_TFIIB_rpt1; 1. DR CDD; cd20552; CYCLIN_TFIIB_rpt2; 1. DR Gene3D; 2.20.25.10; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR IDEAL; IID00314; -. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR000812; TFIIB. DR InterPro; IPR023486; TFIIB_CS. DR InterPro; IPR013150; TFIIB_cyclin. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR11618:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1. DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1. DR Pfam; PF08271; TF_Zn_Ribbon; 1. DR Pfam; PF00382; TFIIB; 2. DR PRINTS; PR00685; TIFACTORIIB. DR SMART; SM00385; CYCLIN; 2. DR SUPFAM; SSF47954; Cyclin-like; 2. DR SUPFAM; SSF57783; Zinc beta-ribbon; 1. DR PROSITE; PS00782; TFIIB; 2. DR PROSITE; PS51134; ZF_TFIIB; 1. DR Genevisible; Q00403; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Chromosome; DNA-binding; KW Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1..316 FT /note="Transcription initiation factor IIB" FT /id="PRO_0000119293" FT REPEAT 124..200 FT /note="1" FT REPEAT 218..294 FT /note="2" FT ZN_FING 11..42 FT /note="TFIIB-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT REGION 189..193 FT /note="Core promoter DNA-binding" FT /evidence="ECO:0000269|PubMed:10619841" FT REGION 244..316 FT /note="Necessary for TATA box-bound TBP complex formation" FT /evidence="ECO:0000269|PubMed:8515820, FT ECO:0000269|PubMed:8516311" FT REGION 249..252 FT /note="Core promoter DNA-binding" FT /evidence="ECO:0000269|PubMed:7675079" FT REGION 283..286 FT /note="Core promoter DNA-binding" FT /evidence="ECO:0000269|PubMed:10619841, FT ECO:0000269|PubMed:7675079" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469, FT ECO:0000269|PubMed:11045620, ECO:0000269|PubMed:14641108, FT ECO:0000269|PubMed:27193682, ECO:0007744|PDB:1DL6, FT ECO:0007744|PDB:1RLY, ECO:0007744|PDB:5IY6" FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469, FT ECO:0000269|PubMed:11045620, ECO:0000269|PubMed:14641108, FT ECO:0007744|PDB:1DL6, ECO:0007744|PDB:1RLY" FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469, FT ECO:0000269|PubMed:11045620, ECO:0000269|PubMed:14641108, FT ECO:0000269|PubMed:27193682, ECO:0007744|PDB:1DL6, FT ECO:0007744|PDB:1RLY, ECO:0007744|PDB:5IY6" FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469, FT ECO:0000269|PubMed:11045620, ECO:0000269|PubMed:14641108, FT ECO:0000269|PubMed:27193682, ECO:0007744|PDB:1DL6, FT ECO:0007744|PDB:1RLY, ECO:0007744|PDB:5IY6" FT BINDING 53 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 61 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 152 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 154 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 189 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 196 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 248 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 272 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 281 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 284 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 286 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 290 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 238 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:12931194" FT VARIANT 19 FT /note="P -> S (in dbSNP:rs1804499)" FT /id="VAR_011977" FT VARIANT 132 FT /note="R -> Q (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs144944840)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035722" FT MUTAGEN 37 FT /note="C->S: Does not inhibit interaction with TBP. FT Inhibits the recruitment of RNA polymerase II into the FT initiation complex." FT /evidence="ECO:0000269|PubMed:8516312" FT MUTAGEN 51..56 FT /note="EWRTFS->AWRTFA: Partial loss of HIV-1 Vpr binding." FT /evidence="ECO:0000269|PubMed:10359081" FT MUTAGEN 51 FT /note="E->R,A,D: Defects in transcription start site FT selection. Supports a level of transcription equivalent to FT wild-type." FT /evidence="ECO:0000269|PubMed:10318856" FT MUTAGEN 52 FT /note="W->A: Partial loss of HIV-1 Vpr binding." FT /evidence="ECO:0000269|PubMed:10359081" FT MUTAGEN 53..54 FT /note="RT->AA: Partial loss of HIV-1 Vpr binding." FT /evidence="ECO:0000269|PubMed:10359081" FT MUTAGEN 55 FT /note="F->A: Partial loss of HIV-1 Vpr binding." FT /evidence="ECO:0000269|PubMed:10359081" FT MUTAGEN 66 FT /note="R->A,E,K: Defects in transcription start site FT selection. Supports a level of transcription equivalent to FT wild-type." FT /evidence="ECO:0000269|PubMed:10318856" FT MUTAGEN 153 FT /note="G->Q: Decreases BREd-dependent pre-initiation FT complex formation." FT /evidence="ECO:0000269|PubMed:16230532" FT MUTAGEN 185 FT /note="R->E: Reduces interaction with SSU72; when FT associated with E-193 or E-200. Inhibits interaction with FT VP16; when associated with E-193. Inhibits RNA pol II FT transcription activation induced by VP16 but does not FT affect basal transcription; when associated with E-193." FT /evidence="ECO:0000269|PubMed:29158257, FT ECO:0000269|PubMed:8515819" FT MUTAGEN 185 FT /note="R->L: Reduces interaction with VP16; when associated FT with L-189." FT /evidence="ECO:0000269|PubMed:8515819" FT MUTAGEN 189 FT /note="K->E: Inhibits interaction with SSU72; when FT associated with E-193. Reduces interaction with SSU72; when FT associated with E-200. Inhibits interaction with VP16; when FT associated with E-200. Inhibits RNA pol II transcription FT activation induced by VP16 but does not affect basal FT transcription; when associated with E-200." FT /evidence="ECO:0000269|PubMed:29158257, FT ECO:0000269|PubMed:8515819" FT MUTAGEN 189 FT /note="K->L: Reduces interaction with VP16; when associated FT with L-185." FT /evidence="ECO:0000269|PubMed:8515819" FT MUTAGEN 193 FT /note="R->E: Inhibits interaction with SSU72; when FT associated with E-185 or E-189. Inhibits interaction with FT VP16; when associated with E-185. Inhibits RNA pol II FT transcription activation induced by VP16 but does not FT affect basal transcription; when associated with E-185." FT /evidence="ECO:0000269|PubMed:29158257, FT ECO:0000269|PubMed:8515819" FT MUTAGEN 196 FT /note="K->L: Reduces interaction with VP16; when associated FT with L-200." FT /evidence="ECO:0000269|PubMed:8515819" FT MUTAGEN 200..208 FT /note="KALETSVDL->GSGS: Reduces the formation of the TATA FT box-bound TBP ternary complex." FT /evidence="ECO:0000269|PubMed:29158257" FT MUTAGEN 200 FT /note="K->E: Reduces interaction with SSU72; when FT associated with E-185 or E-189. Inhibits interaction with FT VP16; when associated with E-189. Inhibits RNA pol II FT transcription activation induced by VP16 but does not FT affect basal transcription; when associated with E-189." FT /evidence="ECO:0000269|PubMed:29158257, FT ECO:0000269|PubMed:8515819" FT MUTAGEN 200 FT /note="K->KGSGS: Reduces the formation of the TATA FT box-bound TBP ternary complex." FT /evidence="ECO:0000269|PubMed:29158257" FT MUTAGEN 200 FT /note="K->L: Reduces interaction with VP16; when associated FT with L-196." FT /evidence="ECO:0000269|PubMed:8515819" FT MUTAGEN 208 FT /note="L->LGSGS: Does not inhibit the formation of the TATA FT box-bound TBP ternary complex." FT /evidence="ECO:0000269|PubMed:29158257" FT MUTAGEN 238 FT /note="K->A: Abolishes autoacetylation, represses FT transcription activity, does not inhibit its association FT with chromatin to promoter-specific regions and decreases FT the association of GTF2F1 with chromatin to FT promoter-specific regions." FT /evidence="ECO:0000269|PubMed:12931194" FT MUTAGEN 247 FT /note="G->V: Inhibits interaction with TBP." FT /evidence="ECO:0000269|PubMed:8516312" FT MUTAGEN 283 FT /note="V->A: Reduces DNA-binding." FT /evidence="ECO:0000269|PubMed:9420329" FT MUTAGEN 286 FT /note="R->A: Reduces DNA-binding." FT /evidence="ECO:0000269|PubMed:9420329" FT MUTAGEN 286 FT /note="R->E: Inhibits interaction with RNA polymerase II; FT when associated with E-290 and E-295." FT /evidence="ECO:0000269|PubMed:8504927" FT MUTAGEN 290 FT /note="R->E: Inhibits interaction with RNA polymerase II; FT when associated with E-286 and E-295." FT /evidence="ECO:0000269|PubMed:8504927" FT MUTAGEN 295 FT /note="R->E: Inhibits interaction with RNA polymerase II; FT when associated with E-286 and E-290." FT /evidence="ECO:0000269|PubMed:8504927" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:1RLY" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:7NVU" FT TURN 27..30 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:7NVU" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:7NVS" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 109..127 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 132..148 FT /evidence="ECO:0007829|PDB:7NVU" FT TURN 150..153 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 156..170 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 177..182 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 188..202 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 215..222 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 226..242 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 250..263 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 271..278 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 282..292 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:1C9B" FT HELIX 296..299 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:7NVU" SQ SEQUENCE 316 AA; 34833 MW; 9CC7E102526C2722 CRC64; MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK YQNRRTMSSS DRAMMNAFKE ITTMADRINL PRNIVDRTNN LFKQVYEQKS LKGRANDAIA SACLYIACRQ EGVPRTFKEI CAVSRISKKE IGRCFKLILK ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV ELDLVPGRSP ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF PTDFKFDTPV DKLPQL //