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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Zinc finger, RAN-binding domain containing 2

ZNF265, ZRANB2, Zis1, zinc-finger, splicing, Zis2
Top mentioned proteins: CAN, RAN, V1a, ZNF, Renin
Papers on ZNF265
Identification of the zinc finger protein ZRANB2 as a novel maternal LPS-binding protein that protects embryos of zebrafish against Gram-negative bacterial infections.
Zhang et al., Taiwan. In J Biol Chem, Feb 2016
UNASSIGNED: Zinc finger ZRANB2 proteins are widespread in animals, but their functions and mechanisms remain poorly defined.
A splicing-regulatory polymorphism in DRD2 disrupts ZRANB2 binding, impairs cognitive functioning and increases risk for schizophrenia in six Han Chinese samples.
Glatt et al., Syracuse, United States. In Mol Psychiatry, Oct 2015
rs1076560(T) disrupted a binding site for the splicing factor ZRANB2, diminished binding affinity between DRD2 pre-mRNA and ZRANB2 and abolished the ability of ZRANB2 to modulate short:long isoform-expression ratios of DRD2 minigenes in cell culture.
Changes in cellular microRNA expression induced by porcine circovirus type 2-encoded proteins.
Lee et al., Seoul, South Korea. In Vet Res, 2014
Among the potential target genes of ORF-regulated miRNAs, two genes encoding proteins that are known to interact with PCV2-encoded proteins, zinc finger protein 265 (ZNF265) and regulator of G protein signaling 16 (RGS16), were selected for further analysis.
miR-186 inhibits muscle cell differentiation through myogenin regulation.
Phylactou et al., Nicosia, Cyprus. In J Biol Chem, 2014
Interestingly, the expression of miR-186 mirrored that of its host gene, ZRANB2, during development.
[Effect of curcumin on radiosensitization of CNE-2 cells and its mechanism].
Fan et al., In Zhongguo Zhong Yao Za Zhi, 2014
In the Cur group, the GUCY2GP, H2BFXP, LINC00623 IncRNA were significantly up-regulated and ZRANB2-AS2 LOC100506835, FLJ36000 IncRNA were significantly down-regulated.
ZRANB2 localizes to supraspliceosomes and influences the alternative splicing of multiple genes in the transcriptome.
Morris et al., Sydney, Australia. In Mol Biol Rep, 2013
The human splicing factor zinc finger, Ran-binding domain containing protein 2 (ZRANB2) is a splicing protein whose specific endogenous targets are unknown.
Selection of new appropriate reference genes for RT-qPCR analysis via transcriptome sequencing of cynomolgus monkeys (Macaca fascicularis).
Chang et al., South Korea. In Plos One, 2012
Using a modification of this large-scale transcriptome sequencing dataset, we selected and compared 12 novel candidate reference genes (ARFGAP2, ARL1, BMI1, CASC3, DDX3X, MRFAP1, ORMDL1, RSL24D1, SAR1A, USP22, ZC3H11A, and ZRANB2) and 4 traditionally used reference genes (ACTB, GAPDH, RPS19, and YWHAZ) in 13 different whole-body tissues by the 3 well-known programs geNorm, NormFinder, and BestKeeper.
Identification and functional analysis of Zranb2 as a novel Smad-binding protein that suppresses BMP signaling.
Katagiri et al., Saitama, Japan. In J Cell Biochem, 2012
In the present study, we analyzed Smad1-binding proteins in HEK293T cells using a proteomic technique and identified the protein, zinc-finger, RAN-binding domain-containing protein 2 (ZRANB2).
Intron Retention and TE Exonization Events in ZRANB2.
Chang et al., South Korea. In Comp Funct Genomics, 2011
The Zinc finger, RAN-binding domain-containing protein 2 (ZRANB2), contains arginine/serine-rich (RS) domains that mediate its function in the regulation of alternative splicing.
Characterization of a family of RanBP2-type zinc fingers that can recognize single-stranded RNA.
Mackay et al., Sydney, Australia. In J Mol Biol, 2011
Recently, we demonstrated that the RanBP2-type zinc finger (ZnF) domains from the human splicing factor ZnF Ran binding domain-containing protein 2 (ZRANB2) can bind to a sequence containing the consensus AGGUAA.
Expression of IL-1alpha, IL-6, TGF-beta, FasL and ZNF265 during sertoli cell infection by ureaplasma urealyticum.
Li et al., Shanghai, China. In Cell Mol Immunol, 2009
We investigated the expressions of IL-1alpha, IL-6, TGF-beta, FasL and ZNF265 at the first, second and third weeks post-infection.
The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences.
Mackay et al., Sydney, Australia. In Proc Natl Acad Sci U S A, 2009
ZRANB2 is a widely-expressed and highly-conserved RS-domain protein that can regulate alternative splicing but lacks canonical RNA-binding domains.
Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins.
Mankertz et al., Berlin, Germany. In Virology, 2009
Six cellular proteins were found to interact with Cap (MKRN1, gC1qR, Par-4, NAP1, NPM1 and Hsp40) and three with Rep (ZNF265, TDG and VG5Q).
Crystallization of a ZRANB2-RNA complex.
Mackay et al., Sydney, Australia. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009
Crystallization of a ZRANB2-RNA complex
ZRANB2: structural and functional insights into a novel splicing protein.
Morris et al., Sydney, Australia. In Int J Biochem Cell Biol, 2007
ZRANB2 was identified originally in a differential display experiment on 2-day and 10-day primary cultures of rat juxtaglomerular cells.
The structure of the zinc finger domain from human splicing factor ZNF265 fold.
Mackay et al., Sydney, Australia. In J Biol Chem, 2003
sites responsible for MRNA binding have been characterized.
Renin gene expression: the switch and the fingers.
van der Weyden et al., Sydney, Australia. In Clin Exp Pharmacol Physiol, 2001
We have cloned the human and mouse homologues of a protein (ZNF265) that is important in renin mRNA processing and stability.
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