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Small nuclear RNA activating complex, polypeptide 4, 190kDa

SNAP190, PTFalpha
Top mentioned proteins: POLYMERASE, OCT, SNAP43, SNAP50, PDEF
Papers on SNAP190
Architectural arrangement of the small nuclear RNA (snRNA)-activating protein complex 190 subunit (SNAP190) on U1 snRNA gene promoter DNA.
Stumph et al., San Diego, United States. In J Biol Chem, 2012
SNAP190, the largest subunit of SNAPc, uncharacteristically contains 4.5 tandem Myb repeats.
Mitotic functions for SNAP45, a subunit of the small nuclear RNA-activating protein complex SNAPc.
Hernandez et al., United States. In J Biol Chem, 2008
In contrast, down-regulation of SNAP190, another SNAP(c) subunit, leads to an accumulation of cells with a G(0)/G(1) DNA content.
The protein kinase CK2 phosphorylates SNAP190 to negatively regulate SNAPC DNA binding and human U6 transcription by RNA polymerase III.
GeneRIF
Henry et al., East Lansing, United States. In J Biol Chem, 2007
CK2 phosphorylation triggers an allosteric inhibition of the SNAP190 Myb DNA binding domain
The unorthodox SNAP50 zinc finger domain contributes to cooperative promoter recognition by human SNAPC.
Henry et al., East Lansing, United States. In J Biol Chem, 2006
DNA binding by SNAPC involves direct DNA contacts by the SNAP190 subunit in cooperation with SNAP50 and SNAP43.
Co-expression of multiple subunits enables recombinant SNAPC assembly and function for transcription by human RNA polymerases II and III.
Henry et al., East Lansing, United States. In Protein Expr Purif, 2006
SNAP(C) consists of five subunits: SNAP190, SNAP50, SNAP45, SNAP43, and SNAP19.
Cooperation between small nuclear RNA-activating protein complex (SNAPC) and TATA-box-binding protein antagonizes protein kinase CK2 inhibition of DNA binding by SNAPC.
GeneRIF
Henry et al., East Lansing, United States. In J Biol Chem, 2005
CK2 may have the capacity to differentially regulate U1 and U6 transcription even though SNAP(C) is universally utilized for human snRNA gene transcription [SNAPC protein, also called PTF or PSE-binding transcription factor]
STAT5 and Oct-1 form a stable complex that modulates cyclin D1 expression.
Dusanter-Fourt et al., Paris, France. In Mol Cell Biol, 2003
This interaction involves a small motif in the carboxy-terminal region of STAT5 which, remarkably, is similar to an Oct-1 POU-interacting motif present in two well-known partners of Oct-1, namely, OBF-1/Bob and SNAP190.
Inhibition of p53, p21 and Bax by pifithrin-alpha does not affect UV induced apoptotic response in CS-B cells.
Palitti et al., Viterbo, Italy. In Dna Repair (amst), 2003
PTFalpha effectively inhibited the induction of p53, p21 and Bax after UV treatment without affecting the apoptotic response in CS-B cells.
The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition.
Henry et al., East Lansing, United States. In J Biol Chem, 2003
To investigate the role of SNAP(c) for TBP function at U6 promoters, TBP recruitment assays were performed using full-length TBP and a mini-SNAP(c) containing SNAP43, SNAP50, and a truncated SNAP190.
Activator recruitment by the general transcription machinery: X-ray structural analysis of the Oct-1 POU domain/human U1 octamer/SNAP190 peptide ternary complex.
Geiger et al., East Lansing, United States. In Genes Dev, 2002
The U1 octamer only weakly recruits the Oct-1 POU domain, although recruitment is stimulated by a peptide containing the Oct-1-binding domain of SNAP190.
Redundant cooperative interactions for assembly of a human U6 transcription initiation complex.
Hernandez et al., New York City, United States. In Mol Cell Biol, 2002
The PSE is recognized by the snRNA-activating protein complex (SNAP(c)), which consists of five types of subunits, SNAP190, SNAP50, SNAP45, SNAP43, and SNAP19.
Crystallization of the Oct-1/SNAP190 peptide/DNA complex.
Geiger et al., East Lansing, United States. In Acta Crystallogr D Biol Crystallogr, 2002
Crystals of the Oct-1 POU/SNAP190 peptide/DNA tertiary complex have been obtained by hanging-drop vapor diffusion at 293K in 20% 2-propanol, 20% PEG 4000 and 0.1M sodium citrate pH 5.6.
Recruitment of the priming protein pTP and DNA binding occur by overlapping Oct-1 POU homeodomain surfaces.
van der Vliet et al., Utrecht, Netherlands. In Embo J, 2002
The human transcription factor Oct-1 can stimulate transcription from a variety of promoters by interacting with the coactivators OBF-1/OCA-B/BOB-1, SNAP190 and VP16.
A map of protein-protein contacts within the small nuclear RNA-activating protein complex SNAPc.
Hernandez et al., United States. In J Biol Chem, 2001
This factor, the snRNA-activating protein complex or SNAP(c), binds to the PSE of both types of promoters and contains five types of subunits, SNAP190, SNAP50, SNAP45, SNAP43, and SNAP19.
The Oct-1 POU domain activates snRNA gene transcription by contacting a region in the SNAPc largest subunit that bears sequence similarities to the Oct-1 coactivator OBF-1.
Hernandez et al., New York City, United States. In Genes Dev, 1998
Here, we show that SNAPc recruitment is mediated by an interaction between the Oct-1 POU domain and a small region of the largest subunit of SNAPc, SNAP190.
SNAP19 mediates the assembly of a functional core promoter complex (SNAPc) shared by RNA polymerases II and III.
Hernandez et al., New York City, United States. In Genes Dev, 1998
Here we reconstitute SNAPc from five recombinant subunits, SNAP43, SNAP45, SNAP50, SNAP190, and a newly identified subunit, SNAP19.
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