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NHP2 non-histone chromosome protein 2-like 1

15.5K, fertilization antigen-1
Originally named because of its sequence similarity to the Saccharomyces cerevisiae NHP2 (non-histone protein 2), this protein appears to be a highly conserved nuclear protein that is a component of the [U4/U6.U5] tri-snRNP. It binds to the 5' stem-loop of U4 snRNA. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, Nop58p, Nop56, fibrillin-1, NUFIP
Papers on 15.5K
NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins.
Bertrand et al., Montpellier, France. In Nucleic Acids Res, Nov 2015
They both contain the 15.5K and proteins with NOP domains (PRP31 for U4, NOP56/58 for snoRNPs).
Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control.
Bertrand et al., Montpellier, France. In J Cell Biol, 2014
In this paper, we describe systematic quantitative stable isotope labeling by amino acids in cell culture proteomic experiments and the crystal structure of the core protein Snu13p/15.5K
Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.
Branlant et al., Illkirch-Graffenstaden, France. In Nucleic Acids Res, 2014
The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs.
Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction.
Charpentier et al., Vandœuvre-lès-Nancy, France. In Nucleic Acids Res, 2013
Biogenesis of eukaryotic box C/D small nucleolar ribonucleoprotein particles (C/D snoRNPs) involves conserved trans-acting factors, which are proposed to facilitate the assembly of the core proteins Snu13p/15.5K,
Influence of reproductive tract obstruction on expression of epididymal proteins and their restoration after patency.
Xu et al., Guangzhou, China. In Asian J Androl, 2013
Further verified experiments on human epididymis 2 (HE2), fertilization antigen-1 (FA-1), clusterin and PH20 demonstrated that compared with the correspondent obstruction group, the translation levels of HE2 and the mRNA transcription levels of HE2 showed an upward trend in patency groups, especially in the groups of obstruction for 60 days where the expression levels of HE2 were significantly upregulated after patency (P<0.05).
Structural basis for the dual U4 and U4atac snRNA-binding specificity of spliceosomal protein hPrp31.
Wahl et al., Berlin, Germany. In Rna, 2011
Human proteins 15.5K and hPrp31 are components of the major spliceosomal U4 snRNP and of the minor spliceosomal U4atac snRNP.
A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.
Lamond et al., Dundee, United Kingdom. In Mol Cell, 2010
Unlike Nop58 and Nhp2, the closely related Nop56 and 15.5K proteins appear not to be SUMO targets.
Evidence that the AAA+ proteins TIP48 and TIP49 bridge interactions between 15.5K and the related NOP56 and NOP58 proteins during box C/D snoRNP biogenesis.
Watkins et al., Newcastle upon Tyne, United Kingdom. In Mol Cell Biol, 2009
snoRNP assembly factor NUFIP can regulate the interactions between TIP48 and TIP49 and the core box C/D proteins.
Probing mutation-induced structural perturbations by refinement against residual dipolar couplings: application to the U4 spliceosomal RNP complex.
Carlomagno et al., Heidelberg, Germany. In Chembiochem, 2009
We demonstrate application of the protocol to a mutant of the 15.5K protein, a core component of the U4 spliceosomal ribonucleoprotein (RNP) complex.
Enrichment of protein-RNA crosslinks from crude UV-irradiated mixtures for MS analysis by on-line chromatography using titanium dioxide columns.
Urlaub et al., Göttingen, Germany. In Biopolymers, 2009
In this feasibility study, we demonstrate the specific enrichment of peptide-RNA oligonucleotides derived from UV-irradiated native spliceosomal U1 snRNPs and spliceosomal [15.5K-61K-U4atac snRNA] complex reconstituted in vitro.
Isolation of human single chain variable fragment antibodies against specific sperm antigens for immunocontraceptive development.
Naz et al., Morgantown, United States. In Hum Reprod, 2008
AFA-1 and FAB-7 scFv antibodies both reacted with fertilization antigen-1 antigen, but against different epitopes.
The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery.
Charpentier et al., Montpellier, France. In J Cell Biol, 2008
Inhibition of Hsp90 in human cells prevents the accumulation of U3, U4, and telomerase RNAs and decreases the levels of newly synthesized hNop58, hNHP2, 15.5K, and SBP2.
Functional implications for a prototypical K-turn binding protein from structural and dynamical studies of 15.5K.
Flynn et al., Salt Lake City, United States. In Biochemistry, 2008
describe the solution NMR structure of free 15.5K, as well as studies of conformational flexibility from 15N NMR relaxation and H/D exchange experiments
Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
Wahl et al., Göttingen, Germany. In Science, 2007
hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes.
Biogenesis and intranuclear trafficking of human box C/D and H/ACA RNPs.
Weber et al., Toulouse, France. In Cold Spring Harb Symp Quant Biol, 2005
The box C/D snoRNAs associate with fibrillarin, Nop56, Nop58, and 15.5K/NHPX proteins to form functional snoRNP particles, whereas all box H/ACA snoRNAs form complexes with the dyskerin, Nop10, Nhp2, and Gar1 snoRNP proteins.
Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP.
Lührmann et al., Göttingen, Germany. In Mol Cell Biol, 2002
Data show that binding of the 15.5 kD RNA binding protein to the box C/D motif of snoRNAs is essential for the association of other snoRNP-associated proteins.
Molecular cloning and sequencing of cDNA encoding for human FA-1 antigen.
Zhu et al., Toledo, United States. In Mol Reprod Dev, 2002
the testis-specific expression of FA-1 antigen at the mRNA level
In vivo analysis of NHPX reveals a novel nucleolar localization pathway involving a transient accumulation in splicing speckles.
Lamond et al., Dundee, United Kingdom. In J Cell Biol, 2002
NHPX is specifically accumulated in both nucleoli and Cajal bodies (CBs) in vivo. The data show a specific temporal pathway involving the sequential and directed accumulation of NHPX in distinct subnuclear compartments
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