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RNA polymerase II associated protein 1

RNA polymerase II-associated protein
The function of this gene is unknown. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, RPAP3, p105, Pontin, fibrillin-1
Papers on RNA polymerase II-associated protein
Human RNA polymerase II-associated protein 2 (RPAP2) interacts directly with the RNA polymerase II subunit Rpb6 and participates in pre-mRNA 3'-end formation.
Ohkuma et al., Toyama, Japan. In Drug Discov Ther, 2014
Human RNA polymerase II-associated protein 2 (RPAP2) was originally identified as a Pol II-associated protein and was subsequently shown to function as a novel Ser5-specific CTD phosphatase.
Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineries.
Pradet-Balade et al., Montpellier, France. In J Biol Chem, 2014
The R2TP is a recently identified Hsp90 co-chaperone, composed of four proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2.
Nuclear import of RNA polymerase II is coupled with nucleocytoplasmic shuttling of the RNA polymerase II-associated protein 2.
Coulombe et al., Montréal, Canada. In Nucleic Acids Res, 2013
The RNA polymerase II (RNAP II)-associated protein (RPAP) 2 has been discovered through its association with various subunits of RNAP II in affinity purification coupled with mass spectrometry experiments.
RPAP3 splicing variant isoform 1 interacts with PIH1D1 to compose R2TP complex for cell survival.
Kamisaki et al., Suita, Japan. In Biochem Biophys Res Commun, 2013
We previously characterized RNA polymerase II-associated protein 3 (RPAP3) as a cell death enhancer.
A two-stage association study identifies methyl-CpG-binding domain protein 2 gene polymorphisms as candidates for breast cancer susceptibility.
Damaraju et al., Edmonton, Canada. In Eur J Hum Genet, 2012
The remaining three SNPs were in proximity to RAD21 homolog (S. pombe), O-6-methylguanine-DNA methyltransferase and RNA polymerase II-associated protein 1.
RPAP3 enhances cytotoxicity of doxorubicin by impairing NF-kappa B pathway.
Kamisaki et al., Suita, Japan. In Biochem Biophys Res Commun, 2011
In this study, we revealed that RPAP3 (RNA polymerase II-associated protein 3) possesses an activity to bind with NEMO and to inhibit the ubiquitination of NEMO and that RPAP3 enhances doxorubicin-induced cell death in breast cancer cell line T-47D through the marked impairment of NF-κB pathway.
PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced apoptosis.
Kamisaki et al., Suita, Japan. In Biochem Biophys Res Commun, 2011
We have previously reported that the two components of R2TP complex, RNA polymerase II-associated protein 3 (RPAP3), and Reptin, regulate apoptosis.
RPAP3 interacts with Reptin to regulate UV-induced phosphorylation of H2AX and DNA damage.
Kamisaki et al., Suita, Japan. In J Cell Biochem, 2009
By affinity purification and mass spectrometry, RNA polymerase II-associated protein 3 (RPAP3) was identified as a Monad binding protein and may function with Monad as a novel modulator of apoptosis pathways.
Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains.
Kamisaki et al., Suita, Japan. In Febs Lett, 2008
By affinity purification and mass spectrometry, we identified RNA polymerase II-associated protein 3 (RPAP3) as a binding protein of Monad.
RNA polymerase II bypasses 8-oxoguanine in the presence of transcription elongation factor TFIIS.
GeneRIF
Tanaka et al., Suita, Japan. In Dna Repair (amst), 2007
SII is important for preventing cellular death due to oxidative DNA damage, assisting RNAPII to bypass 8-oxoG
RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunits.
GeneRIF
Coulombe et al., Montréal, Canada. In Mol Cell Biol, 2004
Data report the purification of RNA polymerase II-associated protein 1 (RPAP1), a 153-kDa polypeptide of unknown function.
Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism.
Jaehning et al., Denver, United States. In Mol Genet Genomics, 2002
Paf1 is an RNA polymerase II-associated protein in yeast, which defines a complex that is distinct from the Srb/Mediator holoenzyme.
RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding.
Burton et al., East Lansing, United States. In J Biol Chem, 1996
A set of deletion mutants of human RNA polymerase II-associated protein (RAP) 30, the small subunit of transcription factor IIF (TFIIF; RAP30/74), was constructed to map functional domains.
Localization of subunits of transcription factors IIE and IIF immediately upstream of the transcriptional initiation site of the adenovirus major late promoter.
Coulombe et al., Sherbrooke, Canada. In J Biol Chem, 1996
Using 5-[N-(p-azidobenzoyl)-3-aminoallyl] photocross-linking, we previously determined the locations of the two large subunits of transcription factor (TF) IIA (A35 and A21), TATA box-binding protein (TBP), RNA polymerase II-associated protein (RAP) 30, and TFIIB along the Ad2 ML promoter.
Topological localization of the human transcription factors IIA, IIB, TATA box-binding protein, and RNA polymerase II-associated protein 30 on a class II promoter.
Greenblatt et al., Toronto, Canada. In J Biol Chem, 1994
The human general transcription factors IIA and IIB bind directly to the TATA box-binding protein (TBP), and modulate transcription initiation by RNA polymerase II.
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