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TAF13 RNA polymerase II, TATA box binding protein

TAFII18, TAF13, hTAFII18, FUN81, hTAF(II)18, taf19, TAF(II)18
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes a small subunit associated with a subset of TFIID complexes. This subunit interacts with TBP and with two other small subunits of TFIID, TAF10 and TAF11. There is a pseudogene located on chromosome 6. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: TBP, TAF, Histone, TAFII, CAN
Papers on TAFII18
TAF13 interacts with PRC2 members and is essential for Arabidopsis seed development.
Kater et al., Milano, Italy. In Dev Biol, 2013
Here we show that in Arabidopsis TAF13 interacts with MEDEA and SWINGER, both members of a plant variant of Polycomb Repressive Complex 2 (PRC2).
Cloning and bioinformatic analysis of full-length novel pepper (Capsicum annuum) genes TAF10 and TAF13.
Deng et al., Kunming, China. In Genet Mol Res, 2012
We isolated two TATA-binding protein-associated factor (TAF) genes, TAF10 and TAF13, from pepper (Capsicum annuum).
Involvement of GTA protein NC2beta in neuroblastoma pathogenesis suggests that it physiologically participates in the regulation of cell proliferation.
Purrello et al., Catania, Italy. In Mol Cancer, 2007
Transcripts from TAF13 and TAF12 (mapping at 1p13.3 and 1p35.3,
A common cis-element in promoters of protein synthesis and cell cycle genes.
Ostrowski et al., Poznań, Poland. In Acta Biochim Pol, 2006
The motif was identified in a substantial fraction of promoters of cell cycle genes, like cyclins (CCNC, CCNG1), as well as transcription regulators (TAF7, TAF13, KLF7, NCOA2), chromatin structure modulators (HDAC2, TAF6L), translation initiation factors (EIF5, EIF2S1, EIF4G2, EIF3S8, EIF4) and previously reported 18 ribosomal protein genes.
Systematic analysis of essential yeast TAFs in genome-wide transcription and preinitiation complex assembly.
Green et al., Worcester, United States. In Embo J, 2003
Unexpectedly, these assembly experiments reveal that TAF11 and TAF13 appear to provide the critical functional contacts with TBP during PIC assembly.
NF-Y recruitment of TFIID, multiple interactions with histone fold TAF(II)s.
Mantovani et al., Modena, Italy. In J Biol Chem, 2002
hTAF(II)20, hTAF(II)28, and hTAF(II)18-hTAF(II)28 bind to the NF-Y B-NF-YC histone fold dimer; hTAF(II)80 and hTAF(II)31-hTAF(II)80 interact with the trimer but not with the NF-YB-NF-YC dimer.
The TATA-binding protein-associated factor yTafII19p functionally interacts with components of the global transcriptional regulator Ccr4-Not complex and physically interacts with the Not5 subunit.
Collart et al., Genève, Switzerland. In J Biol Chem, 2000
We isolated conditional taf19 alleles that display synthetic growth phenotypes when combined with not4 or specific not5 alleles.
Two novel Drosophila TAF(II)s have homology with human TAF(II)30 and are differentially regulated during development.
Tora et al., Strasbourg, France. In Mol Cell Biol, 2000
Biochemical studies suggested that the Drosophila (d) TFIID complexes contain only eight TAF(II)s, leaving a number of yeast and human TAF(II)s (e.g., hTAF(II)55, hTAF(II)30, and hTAF(II)18) without known Drosophila homologues.
Synergistic transcriptional activation by TATA-binding protein and hTAFII28 requires specific amino acids of the hTAFII28 histone fold.
Davidson et al., Strasbourg, France. In Mol Cell Biol, 1999
Critical amino acids are found on both the exposed hydrophilic face of this helix and the hydrophobic interface with TAFII18.
Genomics of the human genes encoding four TAFII subunits of TFIID, the three subunits of TFIIA, as well as CDK8 and SURB7.
Purrello et al., Catania, Italy. In Somat Cell Mol Genet, 1999
By in situ chromosomal hybridization, and by somatic cell and radiation hybrid analysis, we have determined the genomic position of the human genes encoding four TAFII subunits of TFIID (TAFII150, TAFII105, TAFII68, TAFII18), the three subunits of TFIIA (TFIIA35 and TFIIA19, both encoded by the same gene, and TFIIA12), CDK8, and SURB7.
CD36 antisense expression in 3T3-F442A preadipocytes.
Abumrad et al., Stony Brook, United States. In Mol Cell Biochem, 1999
Three clones, TAF13, TAF25, and TAF38 exhibited low CD36 expression and one clone TAF 18 had expression comparable to that of F442A control cells.
A human SPT3-TAFII31-GCN5-L acetylase complex distinct from transcription factor IID.
Roeder et al., New York City, United States. In J Biol Chem, 1998
Amino acid sequence comparisons between human SPT3 (hSPT3) and its counterparts in different yeast species reveal three highly conserved domains, with the most conserved 92-amino acid N-terminal domain being 25% identical with human TAFII18.
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.
Moras et al., Strasbourg, France. In Cell, 1998
Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex.
Interaction of human papillomavirus 8 regulatory proteins E2, E6 and E7 with components of the TFIID complex.
May et al., Köln, Germany. In Intervirology, 1997
Using glutathione-S-transferase (GST) pull-down experiments, we tested in vitro interactions between GST-HPV8-E1, -E2, -E6 and -E7 and 7 in-vitro-translated TAFIIs in the human (h) system (hTAFII18, hTAFII20, hTAFII28, hTAFII30, hTAFII55, hTAFII100, hTAFIIDeltaN135) or TBP.
Yeast homologues of higher eukaryotic TFIID subunits.
Buratowski et al., Boston, United States. In Proc Natl Acad Sci U S A, 1997
A sixth essential gene (FUN81) has previously been noted to be similar to human TAFII18.
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