GTF2B

Functionⁱ

General transcription factor that plays a role in transcription initiation by RNA polymerase II (Pol II). Involved in the pre-initiation complex (PIC) formation and Pol II recruitment at promoter DNA (PubMed:1876184, PubMed:1946368, PubMed:1517211, PubMed:3818643, PubMed:3029109, PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:7601352, PubMed:9420329, PubMed:12931194, PubMed:27193682). Together with the TATA box-bound TBP forms the core initiation complex and provides a bridge between TBP and the Pol II-TFIIF complex (PubMed:8504927, PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312). Released from the PIC early following the onset of transcription during the initiation and elongation transition and reassociates with TBP during the next transcription cycle (PubMed:7601352). Associates with chromatin to core promoter-specific regions (PubMed:12931194, PubMed:24441171). Binds to two distinct DNA core promoter consensus sequence elements in a TBP-independent manner; these IIB-recognition elements (BREs) are localized immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element (PubMed:9420329, PubMed:16230532, PubMed:7675079, PubMed:10619841). Modulates transcription start site selection (PubMed:10318856). Exhibits also autoacetyltransferase activity that contributes to the activated transcription (PubMed:12931194).19 Publications

Manual assertion based on experiment inⁱ

Ref.1
"Cloning of a human gene encoding the general transcription initiation factor IIB."
Ha I., Lane W.S., Reinberg D.
Nature 352:689-695(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ASSOCIATION WITH THE TFIID-TFIIA COMPLEX.
Ref.2
"Sequence of general transcription factor TFIIB and relationships to other initiation factors."
Malik S., Hisatake K., Sumimoto H., Horikoshi M., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 88:9553-9557(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Ref.7
"Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II)."
Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.
J. Biol. Chem. 267:17617-17623(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-316, FUNCTION, INTERACTION WITH ESR1; NR2F1 AND PGR.
Ref.8
"Factors involved in specific transcription in mammalian RNA polymerase II. Functional analysis of initiation factors IIA and IID and identification of a new factor operating at sequences downstream of the initiation site."
Reinberg D., Horikoshi M., Roeder R.G.
J. Biol. Chem. 262:3322-3330(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX.
Ref.9
"Factors involved in specific transcription by mammalian RNA polymerase II. Purification and functional analysis of initiation factors IIB and IIE."
Reinberg D., Roeder R.G.
J. Biol. Chem. 262:3310-3321(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX.
Ref.11
"Multiple functional domains of human transcription factor IIB: distinct interactions with two general transcription factors and RNA polymerase II."
Ha I., Roberts S., Maldonado E., Sun X., Kim L.U., Green M., Reinberg D.
Genes Dev. 7:1021-1032(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GTF2F2; RNA POLYMERASE II AND TBP, MUTAGENESIS OF ARG-286; ARG-290 AND ARG-295.
Ref.13
"Potential RNA polymerase II-induced interactions of transcription factor TFIIB."
Malik S., Lee D.K., Roeder R.G.
Mol. Cell. Biol. 13:6253-6259(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX, INTERACTION WITH RNA POLYMERASE II, DOMAIN.
Ref.15
"Functional dissection of TFIIB domains required for TFIIB-TFIID-promoter complex formation and basal transcription activity."
Hisatake K., Roeder R.G., Horikoshi M.
Nature 363:744-747(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, DOMAINS.
Ref.16
"Delineation of two functional regions of transcription factor TFIIB."
Barberis A., Mueller C.W., Harrison S.C., Ptashne M.
Proc. Natl. Acad. Sci. U.S.A. 90:5628-5632(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, DOMAINS.
Ref.17
"Functional domains of transcription factor TFIIB."
Buratowski S., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 90:5633-5637(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX, DOMAIN, MUTAGENESIS OF CYS-37 AND GLY-247.
Ref.19
"Recycling of the general transcription factors during RNA polymerase II transcription."
Zawel L., Kumar K.P., Reinberg D.
Genes Dev. 9:1479-1490(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX.
Ref.23
"New core promoter element in RNA polymerase II-dependent transcription: sequence-specific DNA binding by transcription factor IIB."
Lagrange T., Kapanidis A.N., Tang H., Reinberg D., Ebright R.H.
Genes Dev. 12:34-44(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF VAL-283 AND ARG-286.
Ref.25
"The role of human TFIIB in transcription start site selection in vitro and in vivo."
Hawkes N.A., Roberts S.G.
J. Biol. Chem. 274:14337-14343(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-51 AND ARG-66.
Ref.27
"Transcription factor IIB acetylates itself to regulate transcription."
Choi C.H., Hiromura M., Usheva A.
Nature 424:965-969(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-238, AUTOACETYLATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-238, CHROMATIN-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
Ref.28
"A core promoter element downstream of the TATA box that is recognized by TFIIB."
Deng W., Roberts S.G.
Genes Dev. 19:2418-2423(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-153.
Ref.33
"A new paradigm for transcription factor TFIIB functionality."
Gelev V., Zabolotny J.M., Lange M., Hiromura M., Yoo S.W., Orlando J.S., Kushnir A., Horikoshi N., Paquet E., Bachvarov D., Schaffer P.A., Usheva A.
Sci. Rep. 4:3664-3664(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FUNCTION IN HSV-1 TRANSCRIPTION AND REPLICATION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, CHROMATIN-BINDING, ACETYLATION, TISSUE SPECIFICITY.
Ref.35
"Crystal structure of a TFIIB-TBP-TATA-element ternary complex."
Nikolov D.B., Chen H., Halay E.D., Usheva A.A., Hisatake K., Lee D.K., Roeder R.G., Burley S.K.
Nature 377:119-128(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 113-316 IN COMPLEX WITH PLANT TATA BOX-BINDING PROTEIN AND DNA, DNA-BINDING.
Ref.37
"Structural basis of preinitiation complex assembly on human pol II promoters."
Tsai F.T.F., Sigler P.B.
EMBO J. 19:25-36(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 110-316 IN COMPLEX WITH TBP AND DNA, INTERACTION WITH TBP, DNA-BINDING.
Ref.41
"Near-atomic resolution visualization of human transcription promoter opening."
He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.
Nature 533:359-365(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, SUBUNIT.

Catalytic activityⁱ

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N₆-acetyl-L-lysine.1 Publication

Kineticsⁱ

K_M=
0.117 mM for acetyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.27
  "Transcription factor IIB acetylates itself to regulate transcription."
  Choi C.H., Hiromura M., Usheva A.
  Nature 424:965-969(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, ACETYLATION AT LYS-238, AUTOACETYLATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-238, CHROMATIN-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	15	ZincCombined sources2 Publications	1
Metal bindingⁱ	18	Zinc; via tele nitrogenCombined sources2 Publications	1
Metal bindingⁱ	34	ZincCombined sources2 Publications	1
Metal bindingⁱ	37	ZincCombined sources2 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	11 – 42	TFIIB-typePROSITE-ProRule annotationAdd BLAST		32

GO - Molecular functionⁱ

acetyltransferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 12931194
core promoter binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10619841
- 7675079
promoter-specific chromatin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12931194
- 24441171
RNA polymerase II core binding
Source: UniProtKB
Inferred from direct assayⁱ
- 8413225
- 8504927
RNA polymerase II core promoter sequence-specific DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 16230532
- 9420329
TBP-class protein binding
Source: CAFA
Inferred from physical interactionⁱ
- 9841876
thyroid hormone receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 8524305
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 9722567
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11045620

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

positive regulation by host of viral transcription
Source: UniProtKB
Inferred from direct assayⁱ
- 24441171
positive regulation of core promoter binding
Source: CAFA
Inferred from direct assayⁱ
- 9841876
positive regulation of transcription initiation from RNA polymerase II promoter
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 12931194
- 9420329
positive regulation of viral transcription
Source: AgBase
Inferred from mutant phenotypeⁱ
- 14644612
protein acetylation
Source: UniProtKB
Inferred from direct assayⁱ
- 12931194
RNA polymerase II core complex assembly
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 8515820
- 8516312
RNA polymerase II transcriptional preinitiation complex assembly
Source: UniProtKB
Inferred from direct assayⁱ
- 3029109
snRNA transcription by RNA polymerase II Source: Reactome
transcriptional start site selection at RNA polymerase II promoter
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10318856
transcription by RNA polymerase II
Source: UniProtKB
Inferred from mutant phenotypeⁱ
transcription initiation from RNA polymerase II promoter
Source: UniProtKB
Inferred from direct assayⁱ
- 3029109
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, DNA-binding, Transferase
Biological process	Host-virus interaction, Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-167161 HIV Transcription Initiation R-HSA-167162 RNA Polymerase II HIV Promoter Escape R-HSA-167172 Transcription of the HIV genome R-HSA-674695 RNA Polymerase II Pre-transcription Events R-HSA-6807505 RNA polymerase II transcribes snRNA genes R-HSA-73776 RNA Polymerase II Promoter Escape R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening R-HSA-75953 RNA Polymerase II Transcription Initiation R-HSA-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
SIGNORⁱ	Q00403

Reactomeⁱ

R-HSA-167161 HIV Transcription Initiation
R-HSA-167162 RNA Polymerase II HIV Promoter Escape
R-HSA-167172 Transcription of the HIV genome
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-73776 RNA Polymerase II Promoter Escape
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-75953 RNA Polymerase II Transcription Initiation
R-HSA-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance

SIGNORⁱ

Q00403

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Transcription initiation factor IIB1 Publication (EC:2.3.1.481 Publication) Alternative name(s): General transcription factor TFIIB1 Publication S300-II1 Publication
Gene namesⁱ	Name:GTF2B Synonyms:TF2B, TFIIB
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000137947.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4648 GTF2B
MIMⁱ	189963 gene
neXtProtⁱ	NX_Q00403

Keywords - Cellular componentⁱ

Chromosome, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	37	C → S: Does not inhibit interaction with TBP. Inhibits the recruitment of RNA polymerase II into the initiation complex. 1 Publication	1
Mutagenesisⁱ	51 – 56	EWRTFS → AWRTFA: Partial loss of HIV-1 Vpr binding. 1 Publication	6
Mutagenesisⁱ	51	E → R, A or D: Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type. 1 Publication	1
Mutagenesisⁱ	52	W → A: Partial loss of HIV-1 Vpr binding. 1 Publication	1
Mutagenesisⁱ	53 – 54	RT → AA: Partial loss of HIV-1 Vpr binding. 1 Publication	2
Mutagenesisⁱ	55	F → A: Partial loss of HIV-1 Vpr binding. 1 Publication	1
Mutagenesisⁱ	66	R → A, E or K: Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type. 1 Publication	1
Mutagenesisⁱ	153	G → Q: Decreases BREd-dependent pre-initiation complex formation. 1 Publication	1
Mutagenesisⁱ	185	R → E: Reduces interaction with SSU72; when associated with E-193 or E-200. Inhibits interaction with VP16; when associated with E-193. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-193. 2 Publications	1
Mutagenesisⁱ	185	R → L: Reduces interaction with VP16; when associated with L-189. 1 Publication	1
Mutagenesisⁱ	189	K → E: Inhibits interaction with SSU72; when associated with E-193. Reduces interaction with SSU72; when associated with E-200. Inhibits interaction with VP16; when associated with E-200. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-200. 2 Publications	1
Mutagenesisⁱ	189	K → L: Reduces interaction with VP16; when associated with L-185. 1 Publication	1
Mutagenesisⁱ	193	R → E: Inhibits interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-185. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-185. 2 Publications	1
Mutagenesisⁱ	196	K → L: Reduces interaction with VP16; when associated with L-200. 1 Publication	1
Mutagenesisⁱ	200 – 208	KALETSVDL → GSGS: Reduces the formation of the TATA box-bound TBP ternary complex. 1 Publication	9
Mutagenesisⁱ	200	K → E: Reduces interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-189. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-189. 2 Publications	1
Mutagenesisⁱ	200	K → KGSGS: Reduces the formation of the TATA box-bound TBP ternary complex. 1 Publication	1
Mutagenesisⁱ	200	K → L: Reduces interaction with VP16; when associated with L-196. 1 Publication	1
Mutagenesisⁱ	208	L → LGSGS: Does not inhibit the formation of the TATA box-bound TBP ternary complex. 1 Publication	1
Mutagenesisⁱ	238	K → A: Abolishes autoacetylation, represses transcription activity, does not inhibit its association with chromatin to promoter-specific regions and decreases the association of GTF2F1 with chromatin to promoter-specific regions. 1 Publication	1
Mutagenesisⁱ	247	G → V: Inhibits interaction with TBP. 1 Publication	1
Mutagenesisⁱ	283	V → A: Reduces DNA-binding. 1 Publication	1
Mutagenesisⁱ	286	R → A: Reduces DNA-binding. 1 Publication	1
Mutagenesisⁱ	286	R → E: Inhibits interaction with RNA polymerase II; when associated with E-290 and E-295. 1 Publication	1
Mutagenesisⁱ	290	R → E: Inhibits interaction with RNA polymerase II; when associated with E-286 and E-295. 1 Publication	1
Mutagenesisⁱ	295	R → E: Inhibits interaction with RNA polymerase II; when associated with E-286 and E-290. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2959
Open Targets More...OpenTargetsⁱ	ENSG00000137947
PharmGKBⁱ	PA29035

Polymorphism and mutation databases

BioMutaⁱ	GTF2B
DMDMⁱ	135629

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000119293	1 – 316	Transcription initiation factor IIBAdd BLAST		316

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	70	PhosphoserineCombined sources	1
Modified residueⁱ	76	PhosphoserineCombined sources	1
Modified residueⁱ	92	PhosphoserineCombined sources	1
Modified residueⁱ	238	N6-acetyllysine; by autocatalysis1 Publication	1

Post-translational modificationⁱ

Acetylated (PubMed:24441171). Autoacetylated; autoacetylation at Lys-238 stimulates transcription activation (PubMed:12931194).2 Publications

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q00403
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q00403
PaxDbⁱ	Q00403
PeptideAtlas More...PeptideAtlasⁱ	Q00403
PRIDEⁱ	Q00403
ProteomicsDBⁱ	57846

PTM databases

iPTMnetⁱ	Q00403
PhosphoSitePlusⁱ	Q00403

Miscellaneous databases

PMAP-CutDBⁱ	Q00403

PMAP-CutDBⁱ

Q00403

Expressionⁱ

Tissue specificityⁱ

Expressed in the inner cell mass forming the embryoblast (PubMed:24441171). Not detected in cells from the outer thin layer trophoblast (at protein level) (PubMed:24441171).1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000137947 Expressed in 224 organ(s), highest expression level in oocyte
CleanExⁱ	HS_GTF2B
ExpressionAtlasⁱ	Q00403 baseline and differential
Genevisibleⁱ	Q00403 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA061626

HPAⁱ

HPA061626

Interactionⁱ

Subunit structureⁱ

Found in a ternary complex with TATA box-bound TBP (PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:10619841, PubMed:29158257). Part of a TFIID-containing RNA polymerase II pre-initiation complex (PIC) that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27193682). Associates with TFIID-TFIIA (DA complex) to form TFIID-TFIIA-TFIIB (DAB complex), which is then recognized by RNA polymerase II (Pol II) (PubMed:1876184, PubMed:2247058). Found in a RNA polymerase II initiation complex (PubMed:3818643, PubMed:3029109, PubMed:8413225, PubMed:8516312, PubMed:7601352). Interacts (via C-terminus) with TBP; this interaction with TATA box-bound TBP guides Pol II into the PIC (PubMed:8504927, PubMed:10619841). Interacts (via N-terminus) with Pol II (PubMed:8504927, PubMed:8413225). Interacts (via C-terminus) with SSU72; this interaction is inhibited by SYMPK (PubMed:29158257). Interacts with NR2F1; this interaction is direct (PubMed:1517211). Interacts with PGR (PubMed:1517211). Interacts with ESR1 (PubMed:1517211). Interacts with GTF2F1 (via C-terminus and preferentially via acetylated form); this interaction prevents binding of GTF2B to GTF2F2 (PubMed:8662660, PubMed:12931194). Interacts with GTF2F2 (via N-terminus); this interaction is inhibited in presence of GTF2F1 (PubMed:8504927, PubMed:8662660). Interacts with the transcription elongation factor TCEA2 (PubMed:8566795). Interacts with HSF1 (via transactivation domain) (PubMed:11005381). Interacts with GPBP1 (By similarity).By similarity18 Publications

Manual assertion based on experiment inⁱ

Ref.1
"Cloning of a human gene encoding the general transcription initiation factor IIB."
Ha I., Lane W.S., Reinberg D.
Nature 352:689-695(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ASSOCIATION WITH THE TFIID-TFIIA COMPLEX.
Ref.7
"Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II)."
Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.
J. Biol. Chem. 267:17617-17623(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-316, FUNCTION, INTERACTION WITH ESR1; NR2F1 AND PGR.
Ref.8
"Factors involved in specific transcription in mammalian RNA polymerase II. Functional analysis of initiation factors IIA and IID and identification of a new factor operating at sequences downstream of the initiation site."
Reinberg D., Horikoshi M., Roeder R.G.
J. Biol. Chem. 262:3322-3330(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX.
Ref.9
"Factors involved in specific transcription by mammalian RNA polymerase II. Purification and functional analysis of initiation factors IIB and IIE."
Reinberg D., Roeder R.G.
J. Biol. Chem. 262:3310-3321(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX.
Ref.10
"Factors involved in specific transcription by mammalian RNA polymerase II: role of transcription factors IIA, IID, and IIB during formation of a transcription-competent complex."
Maldonado E., Ha I., Cortes P., Weis L., Reinberg D.
Mol. Cell. Biol. 10:6335-6347(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE TFIID-TFIIA COMPLEX.
Ref.11
"Multiple functional domains of human transcription factor IIB: distinct interactions with two general transcription factors and RNA polymerase II."
Ha I., Roberts S., Maldonado E., Sun X., Kim L.U., Green M., Reinberg D.
Genes Dev. 7:1021-1032(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GTF2F2; RNA POLYMERASE II AND TBP, MUTAGENESIS OF ARG-286; ARG-290 AND ARG-295.
Ref.13
"Potential RNA polymerase II-induced interactions of transcription factor TFIIB."
Malik S., Lee D.K., Roeder R.G.
Mol. Cell. Biol. 13:6253-6259(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX, INTERACTION WITH RNA POLYMERASE II, DOMAIN.
Ref.15
"Functional dissection of TFIIB domains required for TFIIB-TFIID-promoter complex formation and basal transcription activity."
Hisatake K., Roeder R.G., Horikoshi M.
Nature 363:744-747(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, DOMAINS.
Ref.16
"Delineation of two functional regions of transcription factor TFIIB."
Barberis A., Mueller C.W., Harrison S.C., Ptashne M.
Proc. Natl. Acad. Sci. U.S.A. 90:5628-5632(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, DOMAINS.
Ref.17
"Functional domains of transcription factor TFIIB."
Buratowski S., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 90:5633-5637(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX, DOMAIN, MUTAGENESIS OF CYS-37 AND GLY-247.
Ref.18
"Isolation and characterization of a cDNA encoding a new type of human transcription elongation factor S-II."
Umehara T., Kida S., Yamamoto T., Horikoshi M.
Gene 167:297-302(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TCEA2.
Ref.19
"Recycling of the general transcription factors during RNA polymerase II transcription."
Zawel L., Kumar K.P., Reinberg D.
Genes Dev. 9:1479-1490(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE II INITIATION COMPLEX.
Ref.21
"RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding."
Fang S.M., Burton Z.F.
J. Biol. Chem. 271:11703-11709(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTF2F1 AND GTF2F2, REGION.
Ref.26
"Potential targets for HSF1 within the preinitiation complex."
Yuan C.X., Gurley W.B.
Cell Stress Chaperones 5:229-242(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSF1.
Ref.27
"Transcription factor IIB acetylates itself to regulate transcription."
Choi C.H., Hiromura M., Usheva A.
Nature 424:965-969(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-238, AUTOACETYLATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-238, CHROMATIN-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
Ref.37
"Structural basis of preinitiation complex assembly on human pol II promoters."
Tsai F.T.F., Sigler P.B.
EMBO J. 19:25-36(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 110-316 IN COMPLEX WITH TBP AND DNA, INTERACTION WITH TBP, DNA-BINDING.
Ref.41
"Near-atomic resolution visualization of human transcription promoter opening."
He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.
Nature 533:359-365(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, SUBUNIT.
Ref.42
"Structural dissection of an interaction between transcription initiation and termination factors implicated in promoter-terminator cross-talk."
Bratkowski M., Unarta I.C., Zhu L., Shubbar M., Huang X., Liu X.
J. Biol. Chem. 293:1651-1665(2018) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 107-316 OF APOPROTEIN, IDENTIFICATION IN A COMPLEX WITH TATA BOX-BOUND TBP, INTERACTION WITH SSU72, MUTAGENESIS OF ARG-185; LYS-189; ARG-193; 200-LYS--LEU-208; LYS-200 AND LEU-208.

(Microbial infection) Interacts with HIV-1 Vpr.1 Publication

(Microbial infection) Interacts with Epstein-Barr virus EBNA2.1 Publication

(Microbial infection) Interacts with Herpes simplex virus 1 protein ICP4.1 Publication

(Microbial infection) Interacts (via C-terminus) with the Herpes simplex virus activator VP16; this interaction stimulates RNA Pol II transcription by increasing the extent of pre-initiation complex assembly.2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
DRAP1	Q14919	5	EBI-389564,EBI-712941
EP300	Q09472	2	EBI-389564,EBI-447295
GRF4	P46077	2	EBI-389564,EBI-637479	From Arabidopsis thaliana.
ICP0	P87662	3	EBI-389564,EBI-11712595	From Equid alphaherpesvirus 1.
IE	P17473	4	EBI-389564,EBI-11702772	From Equine herpesvirus 1 (strain Kentucky A).
TBP	P20226	2	EBI-389564,EBI-355371
TNIP1	Q15025	5	EBI-389564,EBI-357849
Vdr	P48281	2	EBI-389564,EBI-346797	From Mus musculus.

GO - Molecular functionⁱ

RNA polymerase II core binding
Source: UniProtKB
Inferred from direct assayⁱ
- 8413225
- 8504927
TBP-class protein binding
Source: CAFA
Inferred from physical interactionⁱ
- 9841876
thyroid hormone receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 8524305
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 9722567

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109214, 90 interactors
CORUMⁱ	Q00403
Database of interacting proteins More...DIPⁱ	DIP-1077N
IntActⁱ	Q00403, 37 interactors
Molecular INTeraction database More...MINTⁱ	Q00403
STRINGⁱ	9606.ENSP00000359531

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 6	Combined sources	3
Beta strandⁱ	18 – 21	Combined sources	4
Beta strandⁱ	24 – 26	Combined sources	3
Beta strandⁱ	27 – 29	Combined sources	3
Turnⁱ	35 – 37	Combined sources	3
Helixⁱ	111 – 113	Combined sources	3
Helixⁱ	114 – 127	Combined sources	14
Helixⁱ	132 – 148	Combined sources	17
Helixⁱ	149 – 151	Combined sources	3
Beta strandⁱ	152 – 154	Combined sources	3
Helixⁱ	156 – 170	Combined sources	15
Helixⁱ	177 – 182	Combined sources	6
Beta strandⁱ	184 – 186	Combined sources	3
Helixⁱ	188 – 201	Combined sources	14
Helixⁱ	212 – 221	Combined sources	10
Helixⁱ	226 – 241	Combined sources	16
Helixⁱ	250 – 263	Combined sources	14
Beta strandⁱ	265 – 267	Combined sources	3
Helixⁱ	271 – 278	Combined sources	8
Helixⁱ	282 – 292	Combined sources	11
Helixⁱ	293 – 295	Combined sources	3
Helixⁱ	296 – 299	Combined sources	4
Helixⁱ	310 – 312	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q00403
SMRⁱ	Q00403
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q00403

EvolutionaryTraceⁱ

Q00403

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Repeatⁱ	124 – 200	1Add BLAST		77
Repeatⁱ	218 – 294	2Add BLAST		77

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	189 – 193	Core promoter DNA-binding1 Publication	5
Regionⁱ	244 – 316	Necessary for TATA box-bound TBP complex formation2 PublicationsAdd BLAST	73
Regionⁱ	249 – 252	Core promoter DNA-binding1 Publication	4
Regionⁱ	283 – 286	Core promoter DNA-binding2 Publications	4

Domainⁱ

The TFIIB-type zinc-binding domain is necessary for the interaction and recruitment of RNA polymerase II to the core promoter, the formation of a fully competent pre-initiation complex (PIC) assembly and basal transcription initiation (PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:8413225). The C-terminus is necessary and sufficient for interaction with the TATA box-bound TBP complex and for the formation of PIC (PubMed:8515820, PubMed:8516311, PubMed:8413225).4 Publications

Sequence similaritiesⁱ

Belongs to the TFIIB family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	11 – 42	TFIIB-typePROSITE-ProRule annotationAdd BLAST		32

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG1597 Eukaryota COG1405 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000006671
HOGENOMⁱ	HOG000108634
HOVERGENⁱ	HBG017914
InParanoidⁱ	Q00403
KEGG Orthology (KO) More...KOⁱ	K03124
OMAⁱ	NDDQGND
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0E7S
PhylomeDBⁱ	Q00403
TreeFamⁱ	TF105953

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00043 CYCLIN, 2 hits
InterProⁱ	View protein in InterPro IPR013763 Cyclin-like IPR036915 Cyclin-like_sf IPR000812 TFIIB IPR023486 TFIIB_CS IPR013150 TFIIB_cyclin IPR013137 Znf_TFIIB
PANTHERⁱ	PTHR11618 PTHR11618, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08271 TF_Zn_Ribbon, 1 hit PF00382 TFIIB, 2 hits
PRINTSⁱ	PR00685 TIFACTORIIB
SMARTⁱ	View protein in SMART SM00385 CYCLIN, 2 hits
SUPFAMⁱ	SSF47954 SSF47954, 2 hits
PROSITEⁱ	View protein in PROSITE PS00782 TFIIB, 2 hits PS51134 ZF_TFIIB, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.ⁱShow all

Q00403-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS 
        60         70         80         90        100
EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK 
       110        120        130        140        150
YQNRRTMSSS DRAMMNAFKE ITTMADRINL PRNIVDRTNN LFKQVYEQKS 
       160        170        180        190        200
LKGRANDAIA SACLYIACRQ EGVPRTFKEI CAVSRISKKE IGRCFKLILK 
       210        220        230        240        250
ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV ELDLVPGRSP 
       260        270        280        290        300
ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF 
       310 
PTDFKFDTPV DKLPQL

Length:316

Mass (Da):34,833

Last modified:December 1, 1992 - v1

Checksum:ⁱ9CC7E102526C2722

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation
	B1APE1	B1APE1_HUMAN		Transcription initiation factor IIB Transcription initiation factor IIB	GTF2B	224	Annotation score:
	B1APE2	B1APE2_HUMAN		Transcription initiation factor IIB Transcription initiation factor IIB	GTF2B	231	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_011977	19	P → S. Corresponds to variant dbSNP:rs1804499Ensembl.		1
Natural variantⁱVAR_035722	132	R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs144944840Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59268 mRNA Translation: CAA41958.1 M76766 mRNA Translation: AAA61149.1 AK289822 mRNA Translation: BAF82511.1 AB451296 mRNA Translation: BAG70110.1 AL445991 Genomic DNA No translation available. BC020597 mRNA Translation: AAH20597.1 S44184 mRNA Translation: AAB23144.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS715.1
PIRⁱ	S17654 TWHU2B
NCBI Reference Sequences More...RefSeqⁱ	NP_001505.1, NM_001514.5
UniGeneⁱ	Hs.481852

Genome annotation databases

Ensemblⁱ	ENST00000370500; ENSP00000359531; ENSG00000137947
GeneIDⁱ	2959
KEGGⁱ	hsa:2959
UCSC genome browser More...UCSCⁱ	uc001dmo.5 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q00403	Transcription initiation factor IIB		MACFA		316	UniRef100_Q00403
Transcription initiation factor IIB		PONAB		316
Transcription initiation factor IIB		MACMU		373
General transcription factor IIB		CERAT		373
GTF2B isoform 1		PANTR		316
+39

Protein	Similar proteins		Species	Score	Length	Source
Q00403	Transcription initiation factor IIB		MACFA		316	UniRef90_Q00403
Transcription initiation factor IIB		PONAB		316
Transcription initiation factor IIB		XENLA		316
Transcription initiation factor IIB		MOUSE		316
Transcription initiation factor IIB		RAT		316
+222

Protein	Similar proteins		Species	Score	Length	Source
Q00403	Transcription initiation factor IIB		MACFA		316	UniRef50_Q00403
Transcription initiation factor IIB		PONAB		316
Transcription initiation factor IIB		BOVIN		316
Transcription initiation factor IIB		XENLA		316
Transcription initiation factor IIB		MOUSE		316
+289

Entry informationⁱ

Entry nameⁱ	TF2B_HUMAN
Accessionⁱ	Q00403Primary (citable) accession number: Q00403 Secondary accession number(s): A8K1A7, Q5JS30
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
	Last sequence update:	December 1, 1992
	Last modified:	September 12, 2018
	This is version 202 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - Q00403 (TF2B_HUMAN)

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Transcription initiation factor IIB

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Computationally mapped potential isoform sequencesⁱ

Keywords - Coding sequence diversityⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ