Property Summary

NCBI Gene PubMed Count 11
Grant Count 64
R01 Count 4
Funding $10,217,674.15
PubMed Score 120.13
PubTator Score 142.67

Knowledge Summary

Patent

No data available

TINX Plot

Expression

  Differential Expression (2)

Disease log2 FC p
ependymoma -1.100 0.008
osteosarcoma -1.758 0.000

Synonym

Accession Q7Z7C8 Q5T0K1 Q8N4R9 Q96M52
Symbols II
TAF
TBN
TAFII43
TAFII-43

Gene

PDB

4WV6   5FUR   4WV4  

Gene RIF (11)

PMID Text
25586196 the TAF2-TAF8-TAF10 complex demonstrates that there is a stepwise assembly pathway of nuclear holo-TFIID, regulated by nuclear import of preformed cytoplasmic submodules
19204726 Observational study of gene-disease association. (HuGE Navigator)
9054383 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
8849451 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
8764062 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
8764009 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
8680883 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
8121496 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
7933101 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
7836461 Interaction of TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat protein, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47
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AA Sequence

MADAAATAGAGGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYIS      1 - 70
EIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNR     71 - 140
PHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDVST    141 - 210
FPLIAARPFTIPYLTALLPSELEMQQMEETDSSEQDEQTDTENLALHISMEDSGAEKENTSVLQQNPSLS    211 - 280
GSRNGEENIIDNPYLRPVKKPKIRRKKSLS                                            281 - 310
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Text Mined References (18)

PMID Year Title
27007846 2016 Structure of promoter-bound TFIID and model of human pre-initiation complex assembly.
25586196 2015 Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.
23186163 2013 Toward a comprehensive characterization of a human cancer cell phosphoproteome.
22814378 2012 N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
19413330 2009 Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
19204726 2009 Transcriptomic and genetic studies identify IL-33 as a candidate gene for Alzheimer's disease.
18669648 2008 A quantitative atlas of mitotic phosphorylation.
18029348 2008 Toward a confocal subcellular atlas of the human proteome.
17375202 2007 Identification of a small TAF complex and its role in the assembly of TAF-containing complexes.
15870280 2005 The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners.
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