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RNA polymerase II associated protein 3

RPAP3, RNA polymerase II-associated protein 3
This gene encodes an RNA polymerase II-associated protein. The encoded protein may function in transcriptional regulation and may also regulate apoptosis. Alternatively spliced transcript variants have been described. [provided by RefSeq, Mar 2009] (from NCBI)
Top mentioned proteins: POLYMERASE, Hsp90, NOP17, fibrillin-1, Pontin
Papers on RPAP3
Structure/Function Analysis of Protein-Protein Interactions Developed by the Yeast Pih1 Platform Protein and Its Partners in Box C/D snoRNP Assembly.
Manival et al., Vandœuvre-lès-Nancy, France. In J Mol Biol, Sep 2015
They contain one guide RNA and four core proteins and their in vivo assembly requires numerous factors including (HUMAN/Yeast) BCD1/Bcd1p, NUFIP1/Rsa1p, ZNHIT3/Hit1p, the R2TP complex composed of protein PIH1D1/Pih1p and RPAP3/Tah1p that bridges the R2TP complex to the HSP90/Hsp82 chaperone and two AAA+ ATPases.
(1)H, (15)N and (13)C resonance assignments of the two TPR domains from the human RPAP3 protein.
Quinternet et al., Vandœuvre-lès-Nancy, France. In Biomol Nmr Assign, Apr 2015
We report the nearly complete (1)H, (15)N and (13)C resonance assignments of the two tetratricopeptide-repeat domains of the human RPAP3 protein, a co-chaperone of the heat-shock protein family.
Substrate recognition and function of the R2TP complex in response to cellular stress.
Macurek et al., Praha, Czech Republic. In Front Genet, 2014
The R2TP complex is a HSP90 co-chaperone, which consists of four subunits: PIH1D1, RPAP3, RUVBL1, and RUVBL2.
Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
Prodromou et al., Brighton, United Kingdom. In Structure, 2014
Hsp90 involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the connection to Hsp90.
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.
Chaperone-interacting TPR proteins in Caenorhabditis elegans.
Richter et al., Garching bei München, Germany. In J Mol Biol, 2013
C34B2.5 and ZK370.8 may encode weakly conserved homologs of the human proteins RPAP3, TTC1 and TOM70.
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.
Genetic and Biochemical Identification of a Novel Single-Stranded DNA-Binding Complex in Haloferax volcanii.
Allers et al., Nottingham, United Kingdom. In Front Microbiol, 2011
Deletion of the rpa3-associated gene rpap3 led to similar levels of DNA damage sensitivity, as did deletion of the rpa3 operon, suggesting that RPA3 and RPAP3 function in the same pathway.
RPAP3 enhances cytotoxicity of doxorubicin by impairing NF-kappa B pathway.
Kamisaki et al., Suita, Japan. In Biochem Biophys Res Commun, 2011
These results indicate that RPAP3 may be a novel modulator of NF-kappaB pathway in apoptosis induced by anti-cancer chemotherapeutic agents.
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.
HSP90 and its R2TP/Prefoldin-like cochaperone are involved in the cytoplasmic assembly of RNA polymerase II.
Bertrand et al., Dundee, United Kingdom. In Mol Cell, 2010
Data indicate that RNA polymerase II is built in the cytoplasm and reveal quality-control mechanisms that link HSP90 and its cochaperone hSpagh (RPAP3) to the nuclear import of fully assembled enzymes.
New insights into the biogenesis of nuclear RNA polymerases?
Coulombe et al., Montréal, Canada. In Biochem Cell Biol, 2010
One of the RPAPs, RPAP3, is part of an 11-subunit complex we termed the RPAP3/R2TP/prefoldin-like complex.
High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes.
Coulombe et al., Montréal, Canada. In Methods, 2009
Is part of an RNA polymerase II-associated complex with possible chaperone activity.
RPAP3 interacts with Reptin to regulate UV-induced phosphorylation of H2AX and DNA damage.
Kamisaki et al., Suita, Japan. In J Cell Biochem, 2009
RPAP3 interacts with Reptin to modulate UV-induced DNA damage by regulating H2AX phosphorylation
Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains.
Kamisaki et al., Suita, Japan. In Febs Lett, 2008
Overexpression of RPAP3 in HEK 293 cells potentiated caspase-3 activation and apoptosis.
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