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Search results 501 to 600 out of 924 for Tbp

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0.034s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Transgene
MGI:3772770 | Tg(Prnp-TBP*)71-16Xjl
Type: transgene
Organism: mouse, laboratory
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Transgene
MGI:3772769 | Tg(Prnp-TBP*)71-27Xjl
Type: transgene
Organism: mouse, laboratory
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Transgene
MGI:5142232 | Tg(Pcp2-TBP*)69Hmhl
Type: transgene
Organism: mouse, laboratory
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Genotype
Genotype
Symbol: Tg(Prnp-TBP*)105Xjl/?
Background: FVB/N-Tg(Prnp-TBP*)105Xjl
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(Prnp-TBP*)71-16Xjl/?
Background: FVB/N-Tg(Prnp-TBP*)71-16Xjl
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(Prnp-TBP*)71-27Xjl/?
Background: FVB/N-Tg(Prnp-TBP*)71-27Xjl
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(Pcp2-TBP*)69Hmhl/?
Background: involves: FVB/N
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tbp/Tbp<+> Tg(CAG-cre/Esr1*)5Amc/?
Background: involves: 129S/SvEv * C57BL/6 * CBA
Zygosity: cn
Has Mutant Allele: true
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DO Term
DOID:0050967 | spinocerebellar ataxia type 17
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Protein
A0A140LIG7
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: true
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Protein
P17427
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
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Protein
P17426
Organism: Mus musculus/domesticus
Length: 977  
Fragment?: false
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Protein
Q69ZW4
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: true
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Protein
Q6PEE6
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
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Protein
Q3U7X9
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
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Strain
MGI:5502192 | B6CBA-Tg(Prnp-TBP*)13Xjl/J
Attribute String: transgenic, mutant stock
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Strain
MGI:3772913 | FVB/N-Tg(Prnp-TBP*)13Xjl
Attribute String: transgenic, mutant strain, coisogenic
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Publication
10470030 | J:57525
First Author: Dantonel JC
Year: 1999
Journal: Trends Biochem Sci
Title: The TBP-like factor: an alternative transcription factor in metazoa?
Volume: 24
Issue: 9
Pages: 335-9
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Publication
17994014 | J:130775
First Author: Friedman MJ
Year: 2007
Journal: Nat Neurosci
Title: Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration.
Volume: 10
Issue: 12
Pages: 1519-28
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Publication
12621023 | J:83601
First Author: Hinkley CS
Year: 2003
Journal: J Biol Chem
Title: The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition.
Volume: 278
Issue: 20
Pages: 18649-57
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Protein
Q9QXK3
Organism: Mus musculus/domesticus
Length: 871  
Fragment?: false
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Protein
O35643
Organism: Mus musculus/domesticus
Length: 943  
Fragment?: false
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Protein
Q9DBG3
Organism: Mus musculus/domesticus
Length: 937  
Fragment?: false
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Protein
Q9QZE5
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
Q3TVN4
Organism: Mus musculus/domesticus
Length: 943  
Fragment?: false
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Protein
Q8CC13
Organism: Mus musculus/domesticus
Length: 953  
Fragment?: false
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Protein
H3BKM0
Organism: Mus musculus/domesticus
Length: 913  
Fragment?: false
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Protein
Q5SVG5
Organism: Mus musculus/domesticus
Length: 916  
Fragment?: false
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Protein
Q6NXY3
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: true
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Protein
Q922G9
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: true
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Protein
Q5SWR1
Organism: Mus musculus/domesticus
Length: 951  
Fragment?: false
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Protein
H3BIY9
Organism: Mus musculus/domesticus
Length: 942  
Fragment?: false
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Protein
Q5SVG4
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
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Protein
Q3U1K9
Organism: Mus musculus/domesticus
Length: 943  
Fragment?: false
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Publication
15767669 | J:97580
First Author: Chong JA
Year: 2005
Journal: Mol Cell Biol
Title: 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.
Volume: 25
Issue: 7
Pages: 2632-43
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GO Term
GO:0001188 | RNA polymerase I preinitiation complex assembly
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Publication
7698028 | J:28900
First Author: Rosen DR
Year: 1995
Journal: Cytogenet Cell Genet
Title: Mapping of the human TATA-binding protein gene (TBP) to chromosome 6qter.
Volume: 69
Issue: 3-4
Pages: 279-80
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Publication
10224042 | J:54525
First Author: Maldonado E
Year: 1999
Journal: J Biol Chem
Title: Transcriptional functions of a new mammalian TATA-binding protein-related factor.
Volume: 274
Issue: 19
Pages: 12963-6
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Publication
18418073 | J:151987
First Author: Brancorsini S
Year: 2008
Journal: Cell Cycle
Title: TIPT, a male germ cell-specific partner of TRF2, is chromatin-associated and interacts with HP1.
Volume: 7
Issue: 10
Pages: 1415-22
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Protein
Q6P926
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
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Protein
A0A494B8X0
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
A0A494BAA1
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
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Protein
A0A494B9K0
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
A0A494B9A8
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: false
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Protein
A0A494B928
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: true
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Protein Domain
IPR023484 | TFIIB_arc
Type: Family
Description: Transcription initiation factor IIB stabilises the TBP (TATA-binding protein) binding to an archaeal box-A promoter. It is also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).
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Protein Domain
IPR033710 | TBP_eukaryotic
Type: Family
Description: The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box [, ]. TBP associates with a host of factors, including the general transcription factors SL1, TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core promoter. Through its association with different transcription factors, TBP can initiate transcription from different RNA polymerases. There are several related TBPs, including TBP-like (TBPL) proteins []. TBP binds directly to the TATA box promoter element, where it nucleates polymerase assembly, thus defining the transcription start site.The C-terminal core of TBP (~180 residues) is highly conserved and contains two 77-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; this region binds to the TATA box and interacts with transcription factors and regulatory proteins []. By contrast, the N-terminal region varies in both length and sequence.This entry refers to TBPs found in eukaryotes.
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Protein Domain
IPR033711 | TBP_archaea
Type: Family
Description: This entry refers to TBPs found in archaea.The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box [, ]. TBP associates with a host of factors, including the general transcription factors SL1, TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core promoter. Through its association with different transcription factors, TBP can initiate transcription from different RNA polymerases. There are several related TBPs, including TBP-like (TBPL) proteins []. TBP binds directly to the TATA box promoter element, where it nucleates polymerase assembly, thus defining the transcription start site.The C-terminal core of TBP (~180 residues) is highly conserved and contains two 77-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; this region binds to the TATA box and interacts with transcription factors and regulatory proteins []. By contrast, the N-terminal region varies in both length and sequence.
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Protein Domain
IPR029176 | SPATA24
Type: Family
Description: This family of proteins bind to DNA and to TBP (TATA box binding protein), TATA-binding protein (TBP)-related protein 2 (TRF2) and several polycomb factors. It is likely to function as a transcription regulator [, ].
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Protein Domain
IPR043112 | TIP_C
Type: Homologous_superfamily
Description: This superfamily represents the C-terminal of the TBP-interacting proteins (TIPs), which includes several newly discovered transcription factors that could interact with TBP (TATA-box binding protein). This interaction would in turn prevent interaction between TBP and TATA-DNA, required for basal transcription in eukaryotic and archaeal cells. The C-terminal domain comprises three α-helices, six β-strands, and two 3(10)-helices; however, the specific function of this domain is yet to be elucidated [].
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Publication
21658482 | -
First Author: Viswanathan R
Year: 2011
Journal: Biochim Biophys Acta
Title: One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?
Volume: 1809
Issue: 9
Pages: 488-96
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Publication
30289385 | -
   
First Author: Butryn A
Year: 2018
Journal: Elife
Title: Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state.
Volume: 7
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GO Term
GO:0005669 | transcription factor TFIID complex
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Protein Domain
IPR036741 | TAFII-230_TBP-bd_sf
Type: Homologous_superfamily
Description: In eukaryotes, the general transcription factor TFIID helps to regulate transcription by RNA polymerase II from class II promoters. TFIID consists of TATA-box-binding proteins (TBP) and TBP-associated factors (TAFIIs), which together mediate both activation and inhibition of transcription. In Drosophila, the N-terminal region of TAFII-230 (the TFIID 230kDa subunit) binds directly to TBP, thereby inhibiting the binding of TBP to the TATA box. The N-terminal domain is comprised of three alpha helices and a beta hairpin, which forms the core that occupies the DNA-binding surface of TBP [].
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Protein Domain
IPR009067 | TAF_II_230-bd
Type: Domain
Description: In eukaryotes, the general transcription factor TFIID helps to regulate transcription by RNA polymerase II from class II promoters. TFIID consists of TATA-box-binding proteins (TBP) and TBP-associated factors (TAFIIs), which together mediate both activation and inhibition of transcription. In Drosophila, the N-terminal region of TAFII-230 (the TFIID 230kDa subunit) binds directly to TBP, thereby inhibiting the binding of TBP to the TATA box. The N-terminal domain is comprised of three alpha helices and a beta hairpin, which forms the core that occupies the DNA-binding surface of TBP [].
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Protein
Q91XA5
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
A0A140LID1
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
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Protein
A0A140LHV3
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: true
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Publication
9741622 | -
First Author: Liu D
Year: 1998
Journal: Cell
Title: Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP.
Volume: 94
Issue: 5
Pages: 573-83
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Publication
16603380 | -
First Author: Hanzlowsky A
Year: 2006
Journal: Protein Expr Purif
Title: Co-expression of multiple subunits enables recombinant SNAPC assembly and function for transcription by human RNA polymerases II and III.
Volume: 48
Issue: 2
Pages: 215-23
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Publication
8633057 | -
First Author: Sadowski CL
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: The SNAP45 subunit of the small nuclear RNA (snRNA) activating protein complex is required for RNA polymerase II and III snRNA gene transcription and interacts with the TATA box binding protein.
Volume: 93
Issue: 9
Pages: 4289-93
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Protein Domain
IPR044078 | Mot1_ATP-bd
Type: Domain
Description: The TATA-binding protein (TBP) is a major target for transcriptional regulation. Mot1, a Swi2/Snf2-related ATPase, dissociates TBP from DNA in an ATP dependent process []. The N-terminal domain of Mot1 has been shown to bind TBP, NC2 and DNA. Its ATPase domain is at the C terminus [].This domain contains the ATP-binding region found in Mot1.
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Protein Domain
IPR022707 | Mot1_central_dom
Type: Domain
Description: This domain is found in Mot1 and related proteins. The TATA-binding protein (TBP) is a major target for transcriptional regulation. Mot1, a Swi2/Snf2-related ATPase, dissociates TBP from DNA in an ATP dependent process []. The N-terminal domain of Mot1 has been shown to bind TBP, NC2 and DNA. Its ATPase domain is at the C terminus [].
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Protein Domain
IPR044972 | Mot1
Type: Family
Description: The TATA-binding protein (TBP) is a major target for transcriptional regulation. Mot1, a Swi2/Snf2-related ATPase, dissociates TBP from DNA in an ATP dependent process []. The N-terminal domain of Mot1 has been shown to bind TBP, NC2 and DNA. Its ATPase domain is at the C terminus [].
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Protein Domain
IPR021281 | SNAPC2
Type: Family
Description: The SNAPc complex allows the transcription of human small nuclear RNA genes to occur by recognition of the proximal sequence element, the TATA box []. SNAPC2 functions both to specifically recognise the proximal sequence element present in the core promoters of human snRNA genes and to stimulate TBP recognition of the neighbouring TATA box present in human U6 snRNA promoters [, ].
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Protein
D6RIQ7
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
D3Z7C2
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Protein
Q3UT44
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
Q05C74
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: false
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Publication
12818428 | -
First Author: Dasgupta A
Year: 2003
Journal: Biochim Biophys Acta
Title: TFIIA abrogates the effects of inhibition by HMGB1 but not E1A during the early stages of assembly of the transcriptional preinitiation complex.
Volume: 1627
Issue: 2-3
Pages: 101-10
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Publication
8610010 | -
First Author: Tan S
Year: 1996
Journal: Nature
Title: Crystal structure of a yeast TFIIA/TBP/DNA complex.
Volume: 381
Issue: 6578
Pages: 127-51
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Publication
7491500 | -
First Author: Beckmann H
Year: 1995
Journal: Science
Title: Coactivator and promoter-selective properties of RNA polymerase I TAFs.
Volume: 270
Issue: 5241
Pages: 1506-9
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Protein Domain
IPR016629 | RNA_pol_I_TAF1A/TAFI48_chr
Type: Family
Description: This entry represents subunit A (TATA-binding protein-associated factor TAFI48 or TAF1A) of RNA polymerase I. It is a component of the transcription factor SL1/TIFIB complex involved in the assembly of the pre-initiation complex (PIC). The SL1/TIFIB complex is composed of TBP (TATA-binding protein) and TAF1A (TAFI48), TAF1B (TAFI63) and TAF1C (TAFI110) []. Human ribosomal RNA synthesis by RNA polymerase I requires the activator UBF and the promoter selectivity factor SL1/TIFIB. Both TAF1B/TAFI63 and TAF1C/TAFI110 contact the promoter, whereas TAF1A/TAFI48 serves as a target for interaction with UBF and is required to form a transcriptionally active SL1/TIFIB complex responsive to UBF []. Interaction of the SL1/TIFIB subunits with TBP excluded interaction with the transcription factor IID (TFIID) subunits []. This mutually exclusive binding directs the formation of promoter- and RNA polymerase-selective TBP-TAF complexes. Therefore, TAF1A/TAFI48 may function both as a target to mediate UBF activation and as a class-specific promoter selectivity factor.
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Protein
E0CYD4
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: true
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Protein
Q3USX2
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: true
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Publication
11089979 | -
First Author: Yudkovsky N
Year: 2000
Journal: Nature
Title: A transcription reinitiation intermediate that is stabilized by activator.
Volume: 408
Issue: 6809
Pages: 225-9
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Protein Domain
IPR004855 | TFIIA_asu/bsu
Type: Family
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the precursor that yields both the alpha and beta subunits of TFIIA. The TFIIA heterotrimer is an essential general transcription initiation factor for the expression of genes transcribed by RNA polymerase II [].
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Protein Domain
IPR009083 | TFIIA_a-hlx
Type: Homologous_superfamily
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcriptionpre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This superfamily represents the α-helical domain found at the N-terminal of the gamma subunit of transcription factor TFIIA.
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Protein Domain
IPR009088 | TFIIA_b-brl
Type: Homologous_superfamily
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This superfamily represents the β-barrel domain found at the C-terminal of both TOA1 (or alpha/beta) and TOA2 (or gamma) subunits of TFIIA, and their homologues.
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Protein Domain
IPR003194 | TFIIA_gsu
Type: Family
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the gamma subunit of transcription factor TFIIA.
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Protein Domain
IPR015871 | TFIIA_gsu_C
Type: Domain
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the β-barrel domain found at the C-terminal of the gamma subunit of transcription factor TFIIA.
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Protein Domain
IPR015872 | TFIIA_gsu_N
Type: Domain
Description: Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [], and can dissociate HMGB1 already bound to TBP/TATA-box.Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a β-barrel (β-barrel domain) composed of β-sheets from the C-terminal regions of TOA1 and TOA2 [].This entry represents the α-helical domain found at the N-terminal of the gamma subunit of transcription factor TFIIA.
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Protein
Q80ZM7
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
D3Z7S8
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
Q3TN86
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
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Protein
D3Z793
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
Q3TE88
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Publication
11463376 | J:68789
First Author: Martianov I
Year: 2001
Journal: Mol Cell
Title: Late arrest of spermiogenesis and germ cell apoptosis in mice lacking the TBP-like TLF/TRF2 gene.
Volume: 7
Issue: 3
Pages: 509-15
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Publication
23326641 | J:197870
 
First Author: Zhou H
Year: 2013
Journal: Elife
Title: Dual functions of TAF7L in adipocyte differentiation.
Volume: 2
Pages: e00170
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Publication
17109819 | J:116631
First Author: Tanaka Y
Year: 2007
Journal: Biochem Biophys Res Commun
Title: Transcriptional repression of the mouse wee1 gene by TBP-related factor 2.
Volume: 352
Issue: 1
Pages: 21-8
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Publication
9040789 | J:38336
First Author: Purrello M
Year: 1996
Journal: Cytogenet Cell Genet
Title: Genomic localization of the human gene encoding Dr1, a negative modulator of transcription of class II and class III genes.
Volume: 75
Issue: 2-3
Pages: 186-9
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Publication
9048943 | J:38493
First Author: Diagana TT
Year: 1997
Journal: J Mol Biol
Title: The transcriptional activity of a muscle-specific promoter depends critically on the structure of the TATA element and its binding protein.
Volume: 265
Issue: 5
Pages: 480-93
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Publication
28689656 | J:256789
First Author: Preußner M
Year: 2017
Journal: Mol Cell
Title: Body Temperature Cycles Control Rhythmic Alternative Splicing in Mammals.
Volume: 67
Issue: 3
Pages: 433-446.e4
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HT Experiment
E-GEOD-26743 | An ENU-induced point mutation in the mouse Btaf1 gene causes post-gastrulation embryonic lethality and protein instability
Series Id: GSE26743
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
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Protein
Q99PM3
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Protein
Q8R4I4
Organism: Mus musculus/domesticus
Length: 468  
Fragment?: false
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Protein
Q149E9
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
Q0VGZ0
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Protein
Q8K0S9
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
A0A1Y7VJQ2
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: false
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