AC T00818
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ID T00818
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DT 20.11.1992 (created); ewi.
DT 26.08.2014 (updated); hna.
CO Copyright (C), QIAGEN.
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FA TFIIB
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SY alpha (rat); CB; CI; FA; factor e; GTF2B; TF2B; TFIIB; transcription initiation factor IIB.
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OS human, Homo sapiens
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
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GE G005158 GTF2B; HGNC: GTF2B.
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CL C0030; histone fold.
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SF pI(calc.) = 8.32 [19];
SF resembling the overall structure of TBP in exhibiting also two direct repeats, basic regions, and sigma homology regions [14] [15];
SF forms a protease-resistant core with a structure similar to that of cyclin A [3] [8] [9] [23];
SF the direct repeats (112-316) are alpha-helically folded and impose a pseudo-twofold symmetry [3] [9];
SF formation of the ternary complex with TBP and the TATA box depends on a basic cluster;
SF in the ternary complex TBP-TFIIB-DNA, TFIIB performs DNA contacts on either side of the TATA box [3] [4] [8] [24];
SF it constitutes the downstream surface of the basal transcription complex [3];
SF binds to the stirrup of TBP [3] [4];
SF interacts directly with acidic activating regions of upstream activators [17] [18] [21];
SF the first direct repeat and the C-terminal part of the molecule (273-316) are required for interactions with upstream activators [21];
SF interactions with upstream activators disrupt an intramolecular contact between N- and C-terminal parts of TFIIB thus exposing the latter as contact interface to RNA polymerase II [22] [26];
SF interaction with 14-3-3 proteins is mediated by direct repeat 1, and also by direct repeat 2 [29];
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CP SK-N-SH cells, HeLa cells, HEK293 cells [37].
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FF binding to (TATA-DNA)+TFIID(+TFIIA);
FF enhances affinity of TBP to DNA [7];
FF anchors pol II to the initial transcription complex [16];
FF may fix the transcription start site [3];
FF exerts similar functionality in conjunction with YY1 instead of TBP [25];
FF target of certain autoantibodies [27];
FF interacts directly with acidic transactivations domains of transcription factors, for example VP16, NF1/CTF1, CIITA [31];
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IN T04133 14-3-3GF14-Mu; thale cress, Arabidopsis thaliana.
IN T00018 AhR; mouse, Mus musculus.
IN T01346 arnt-isoform1; human, Homo sapiens.
IN T08574 C/EBPalpha; rat, Rattus norvegicus.
IN T08664 C/EBPalpha; Mammalia.
IN T05450 C2TA; human, Homo sapiens.
IN T01318 CBP; mouse, Mus musculus.
IN T00176 CTF-1; human, Homo sapiens.
IN T04134 GF14-12; maize, Zea mays.
IN T04365 GF14; thale cress, Arabidopsis thaliana.
IN T14816 IRF-1; Mammalia.
IN T14446 IRF-2; Mammalia.
IN T00456 Kr; fruit fly, Drosophila melanogaster.
IN T01427 p300; human, Homo sapiens.
IN T01384 pX; HBV, human hepatitis B virus.
IN T01345 RXR-alpha; human, Homo sapiens.
IN T01152 T3R-alpha1; human, Homo sapiens.
IN T08264 T3R-beta; human, Homo sapiens.
IN T02113 TAFII31; human, Homo sapiens.
IN T00794 TBP; human, Homo sapiens.
IN T00822 TFIIE; human, Homo sapiens.
IN T02168 TFIIF-alpha; human, Homo sapiens.
IN T02169 TFIIF-beta; human, Homo sapiens.
IN T01038 TFIIF; human, Homo sapiens.
IN T08928 VDR-M4; human, Homo sapiens.
IN T00885 VDR; human, Homo sapiens.
IN T00894 Vmw65; HSV-1, herpes simplex virus type 1.
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MX M01739 V$TFIIB_Q6.
MX M08904 V$TFIIB_Q6_02.
XX
BS R00996.
BS R01002.
BS R01016.
BS R01017.
BS R01018.
BS R03170.
BS R04803.
BS R00705.
BS R29191.
BS R63526.
BS R63600.
BS R63628.
XX
DR TRANSPATH: MO000013528.
DR UniProtKB: Q00403;
DR PDB: 1TFB.
DR PDB: 1VOL.
XX
RN [1]; RE0001533.
RX PUBMED: 2398901.
RA Buratowski S., Sharp Ph. A.
RT Transcription initiation complexes and upstream activation with RNA polymerase II lacking the C-terminal domain of the largest subunit
RL Mol. Cell. Biol. 10:5562-5564 (1990).
RN [2]; RE0005257.
RX PUBMED: 7913207.
RA Kwok R. P., Lundblad J. R., Chrivia J. C., Richards J. P., Baechinger H. P., Brennan R. G., Roberts S. G., Green M. R., Goodman R. H.
RT Nuclear protein CBP is a coactivator for the transcription factor CREB
RL Nature 370:223-226 (1994).
RN [3]; RE0005519.
RX PUBMED: 7675079.
RA Nikolov D. B., Chen H., Halay E. D., Usheva A. A., Hisatake K., Lee D. K., Roeder R. G., Burley S. K.
RT Crystal structure of a TFIIB-TBP-TATA-element ternary complex
RL Nature 377:119-128 (1995).
RN [4]; RE0005520.
RX PUBMED: 7637813.
RA Lee S., Hahn S.
RT Model for binding of transcription factor TFIIB to the TBP-DNA complex
RL Nature 376:609-612 (1995).
RN [5]; RE0005527.
RX PUBMED: 7597030.
RA Klemm R. D., Goodrich J. A., Zhou S., Tjian R.
RT Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation
RL Proc. Natl. Acad. Sci. USA 92:5788-5792 (1995).
RN [6]; RE0005607.
RX PUBMED: 8221891.
RA Goodrich J. A., Hoey T., Thut C. J., Admon A., Tjian R.
RT Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB
RL Cell 75:519-530 (1993).
RN [7]; RE0005671.
RX PUBMED: 8132551.
RA Imbalzano A. N., Zaret K. S., Kingston R. E.
RT Transcription factor (TF) IIB and TFIIA can independently increase the affinity of the TATA-binding protein for DNA
RL J. Biol. Chem. 269:8280-8286 (1994).
RN [8]; RE0005673.
RX PUBMED: 8413225.
RA Malik S., Lee D. K., Roeder R. G.
RT Potential RNA polymerase II-induced interactions of transcription factor TFIIB
RL Mol. Cell. Biol. 13:6253-6259 (1993).
RN [9]; RE0005674.
RX PUBMED: 7671313.
RA Babgy S., Kim S., Maldonado E., Tong K. I., Reinberg D., Ikura M.
RT Solution structure of the C-terminal core domain of human TFIIB: similarity to Cyclin A and interaction with TATA -binding protein
RL Cell 82:857-867 (1995).
RN [10]; RE0005675.
RX PUBMED: 7675113.
RA Chi T., Lieberman P., Ellwood K., Carey M.
RT A general mechanism for transcriptional synergy by eukaryotic activators
RL Nature 377:254-257 (1995).
RN [11]; RE0005676.
RX PUBMED: 7753175.
RA Sauer F., Fondell J. D., Ohkuma Y., Roeder R. G., Jaeckle H.
RT Control of transcription by Krueppel through interactions with TFIIB and TFIIEbeta
RL Nature 375:162-164 (1995).
RN [12]; RE0005678.
RX PUBMED: 7623841.
RA Hadzic E., Desai-Yajnik V., Helmer E., Guo S., Wu S., Koudinova N., Casanova J., Raaka B. M., Samuels H. H.
RT A 10-amino acid sequence in the N-terminal A/B Domain of thyroid hormone receptor alpha is essential for transcriptional activation and interaction with the general transcription factor TFIIB
RL Mol. Cell. Biol. 15:4507-4517 (1995).
RN [13]; RE0005679.
RX PUBMED: 8670843.
RA Haviv I., Vaizel D., Shaul Y.
RT pX, the HBV-encoded coactivator, interacts with components of the transcription machinery and stimulates transcription in a TAF-independent manner
RL EMBO J. 15:3413-3420 (1996).
RN [14]; RE0005680.
RX PUBMED: 1876184.
RA Ha I., Lane W. S., Reinberg D.
RT Cloning of a human gene encoding the general transcription initiation factor IIB
RL Nature 352:689-695 (1991).
RN [15]; RE0005681.
RX PUBMED: 1946368.
RA Malik S., Hisatake K., Sumimoto H., Horikoshi M., Roeder R. G.
RT Sequence of general transcription factor TFIIB and relationships to other initiation factors
RL Proc. Natl. Acad. Sci. USA 88:9553-9557 (1991).
RN [16]; RE0005686.
RX PUBMED: 2027376.
RA Sharp P.
RT TFIIB or not TFIIB
RL Nature 351:16-18 (1991).
RN [17]; RE0005689.
RX PUBMED: 1922364.
RA Lin Y.-S., Ha I., Maldonado E., Reinberg D., Green M. R.
RT Binding of general transcription factor TFIIB to an acidic activating region
RL Nature 353:569-571 (1991).
RN [18]; RE0005690.
RX PUBMED: 2001592.
RA Lin Y.-S., Green M. R.
RT Mechanism of action of an acidic transcriptional activator in vitro
RL Cell 64:971-981 (1991).
RN [19]; RE0005692.
RX PUBMED: 1547497.
RA Pinto I., Ware D. E., Hampsey M.
RT The yeast SUA7 gene encodes a homolog of human transcription factor TFIIB and is required for normal start site selection in vivo
RL Cell 68:977-988 (1992).
RN [20]; RE0005693.
RX PUBMED: 8515820.
RA Hisatake K., Roeder R. G., Horikoshi M.
RT Functional dissection of TFIIB domains required for TFIIB-TFIID-promoter complex formation and basal transcription activity
RL Nature 363:744-747 (1993).
RN [21]; RE0005695.
RX PUBMED: 8515819.
RA Roberts S. G. E., Ha I., Maldonado E., Reinberg D., Green M. R.
RT Interaction between an acidic activator and transcription factor IIB is required for transcriptional activation
RL Nature 363:741-744 (1993).
RN [22]; RE0005697.
RX PUBMED: 8504927.
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 interactions with two general transcription factors
RL Genes Dev. 7:1021-1032 (1993).
RN [23]; RE0005698.
RX PUBMED: 8516311.
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. USA 90:5628-5632 (1993).
RN [24]; RE0005699.
RX PUBMED: 8516312.
RA Buratowski S., Zhou H.
RT Functional domains of transcription factor TFIIB
RL Proc. Natl. Acad. Sci. USA 90:5633-5637 (1993).
RN [25]; RE0005700.
RX PUBMED: 8137426.
RA Usheva A., Shenk T.
RT TATA-binding protein-independent initiation: YY1, TFIIB, and RNA polymerase II direct basal transcription on supercoiled template DNA
RL Cell 76:1115-1121 (1994).
RN [26]; RE0005701.
RX PUBMED: 7935820.
RA Roberts S. G. E., Green M. R.
RT Activator-induced conformational change in general transcription factor TFIIB
RL Nature 371:717-720 (1994).
RN [27]; RE0005702.
RX PUBMED: 7651839.
RA Abendroth F. D., Peterson S. R., Galman M., Suwa A., Hardin J. A., Dynan W. S.
RT Identification of human autoantibodies to transcription factor IIB
RL Nucleic Acids Res. 23:2770-2774 (1995).
RN [28]; RE0006251.
RX PUBMED: 7556073.
RA Nerlov C., Ziff E. B.
RT CCAAT/enhancer binding protein-alpha amino acid motifs with dual TBP and TFIIB binding ability co-operate to activate transcription in both yeast and mammalian cells
RL EMBO J. 14:4318-4328 (1995).
RN [29]; RE0017024.
RX PUBMED: 10449590.
RA Pan S., Sehnke P. C., Ferl R. J., Gurley W. B.
RT Specific interactions with TBP and TFIIB in vitro suggest that 14-3-3 proteins may participate in the regulation of transcription when part of a DNA binding complex
RL Plant Cell 11:1591-1602 (1999).
RN [30]; RE0018012.
RX PUBMED: 8887661.
RA Wang I. M., Blanco J. C., Tsai S. Y., Tsai M. J., Ozato K.
RT Interferon regulatory factors and TFIIB cooperatively regulate interferon-responsive promoter activity in vivo and in vitro.
RL Mol. Cell. Biol. 16:6313-6324 (1996).
RN [31]; RE0022568.
RX PUBMED: 9177216.
RA Mahanta S. K., Scholl T., Yang F. C., Strominger J. L.
RT Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein.
RL Proc. Natl. Acad. Sci. USA 94:6324-6329 (1997).
RN [32]; RE0035551.
RX PUBMED: 12931194.
RA Choi C. H., Hiromura M., Usheva A.
RT Transcription factor IIB acetylates itself to regulate transcription.
RL Nature 424:965-969 (2003).
RN [33]; RE0047272.
RX PUBMED: 14729958.
RA Forget D., Langelier M. F., Therien C., Trinh V., Coulombe B.
RT Photo-cross-linking of a purified preinitiation complex reveals central roles for the RNA polymerase II mobile clamp and TFIIE in initiation mechanisms
RL Mol. Cell. Biol. 24:1122-31 (2004).
RN [34]; RE0047287.
RX PUBMED: 10707958.
RA Jurutka P. W., Remus L. S., Whitfield G. K., Thompson P. D., Hsieh J. C., Zitzer H., Tavakkoli P., Galligan M. A., Dang H. T., Haussler C. A., Haussler M. R.
RT The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB
RL Mol. Endocrinol. 14:401-20 (2000).
RN [35]; RE0047290.
RX PUBMED: 7876247.
RA MacDonald P. N., Sherman D. R., Dowd D. R., Jefcoat S. C. Jr, DeLisle R. K.
RT The vitamin D receptor interacts with general transcription factor IIB
RL J. Biol. Chem. 270:4748-52 (1995).
RN [36]; RE0047297.
RX PUBMED: 8415616.
RA Baniahmad A., Ha I., Reinberg D., Tsai S., Tsai M. J., O'Malley B. W.
RT Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone
RL Proc. Natl. Acad. Sci. USA 90:8832-6 (1993).
RN [37]; RE0050400.
RX PUBMED: 15767669.
RA Chong J. A., Moran M. M., Teichmann M., Kaczmarek J. S., Roeder R., Clapham D. E.
RT TATA-binding protein (TBP)-like factor (TLF) is a functional regulator of transcription: reciprocal regulation of the neurofibromatosis type 1 and c-fos genes by TLF/TRF2 and TBP.
RL Mol. Cell. Biol. 25:2632-2643 (2005).
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