TF2B_HUMAN
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 03-AUG-2022, entry version 226.
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), 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 [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). Associates with TFIID-TFIIA (DA complex) to form
CC TFIID-TFIIA-TFIIB (DAB complex), which is then recognized by RNA
CC polymerase II (Pol II) (PubMed:1876184, PubMed:2247058). Found in a RNA
CC polymerase II initiation complex (PubMed:3818643, PubMed:3029109,
CC PubMed:8413225, PubMed:8516312, PubMed:7601352). Interacts (via C-
CC terminus) with TBP; this interaction with TATA box-bound TBP guides Pol
CC II into the PIC (PubMed:8504927, PubMed:10619841). Interacts (via N-
CC terminus) with Pol II (PubMed:8504927, PubMed:8413225). Interacts (via
CC C-terminus) with SSU72; this interaction is inhibited by SYMPK
CC (PubMed:29158257). Interacts with NR2F1; this interaction is direct
CC (PubMed:1517211). Interacts with PGR (PubMed:1517211). Interacts with
CC ESR1 (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}.
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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 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 AlphaFoldDB; Q00403; -.
DR SMR; Q00403; -.
DR BioGRID; 109214; 118.
DR CORUM; Q00403; -.
DR DIP; DIP-1077N; -.
DR IntAct; Q00403; 97.
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; Q00403; -.
DR PeptideAtlas; Q00403; -.
DR PRIDE; Q00403; -.
DR ProteomicsDB; 57846; -.
DR Antibodypedia; 19819; 457 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 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; 729732at2759; -.
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; 815 hits in 1094 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 202 other tissues.
DR ExpressionAtlas; Q00403; baseline and differential.
DR Genevisible; Q00403; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
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; IDA:CAFA.
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:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
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:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0006367; P:transcription initiation from 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; cd00043; CYCLIN; 2.
DR IDEAL; IID00314; -.
DR InterPro; IPR013763; Cyclin-like.
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; PTHR11618; 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; SSF47954; 2.
DR PROSITE; PS00782; TFIIB; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
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:0007744|PDB:1DL6, ECO:0007744|PDB:1RLY"
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:0007744|PDB:1DL6, ECO:0007744|PDB:1RLY"
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:0007744|PDB:1DL6, ECO:0007744|PDB:1RLY"
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 box-
FT 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 promoter-
FT 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
