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Heterogeneous nuclear ribonucleoprotein D-like

JKTBP, HNRPDL, JKTBP2, heterogeneous nuclear ribonucleoprotein D-like JKTBP, laAUF1
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two RRM domains that bind to RNAs. Three alternatively spliced transcript variants have been described for this gene. One of the variants is probably not translated because the transcript is a candidate for nonsense-mediated mRNA decay. The protein isoforms encoded by this gene are similar to its family member HNRPD. [provided by RefSeq, May 2011] (from NCBI)
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Top mentioned proteins: MIP, ACID, caspase-3, cGKII, HAD
Papers on JKTBP
The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.
Ventura et al., Barcelona, Spain. In Microb Cell Fact, 2014
RESULTS: Here we characterize the IBs formed by the human prion-like RNA-processing protein HNRPDL.
Phenotypic variability in a Hungarian patient with the 4q21 microdeletion syndrome.
Melegh et al., Pécs, Hungary. In Mol Cytogenet, 2014
A minimal critical region of 1.37 Mb accounting for the common features with 5 known genes (PRKG2, RASGEF1B, HNRNPD, HNRPDL, and ENOPH1) has been described so far.
A defect in the RNA-processing protein HNRPDL causes limb-girdle muscular dystrophy 1G (LGMD1G).
Zatz et al., Boston, United States. In Hum Mol Genet, 2014
Whole genome sequencing identified, in both families, mutations in the HNRPDL gene.
Genetic basis of limb-girdle muscular dystrophies: the 2014 update.
Review
Savarese et al., Napoli, Italy. In Acta Myol, 2014
The dominant forms (LGMD1) are: LGMD1A (myotilin), LGMD1B (lamin A/C), LGMD1C (caveolin 3), LGMD1D (DNAJB6), LGMD1E (desmin), LGMD1F (transportin 3), LGMD1G (HNRPDL), LGMD1H (chr.
Growth arrest specific 2 is up-regulated in chronic myeloid leukemia cells and required for their growth.
Zhao et al., Suzhou, China. In Plos One, 2013
Lastly, we generated microarray data to identify the differentially expressed genes upon GAS2DN and validated that the expression of HNRPDL, PTK7 and UCHL5 was suppressed by GAS2DN.
Expanding the spectrum of microdeletion 4q21 syndrome: a partial phenotype with incomplete deletion of the minimal critical region and a new association with cleft palate and Pierre Robin sequence.
Zackai et al., Philadelphia, United States. In Am J Med Genet A, 2013
A 1.37 MB minimal critical region has been described that accounts for this shared phenotype and includes five known genes: PRKG2, RASGEF1B, HNRNPD, HNRPDL, and ENOPH1.
Mutually exclusive splicing regulates the Nav 1.6 sodium channel function through a combinatorial mechanism that involves three distinct splicing regulatory elements and their ligands.
Baralle et al., Trieste, Italy. In Nucleic Acids Res, 2012
These elements bind a series of positive (RbFox-1, SRSF1, SRSF2) and negative (hnRNPA1, PTB, hnRNPA2/B1, hnRNPD-like JKTBP) splicing regulatory proteins.
Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
GeneRIF
Bahn et al., Cambridge, United Kingdom. In J Proteome Res, 2012
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins.
Blackshear et al., United States. In J Biol Chem, 2012
We found that TTP and its related family members could bind to certain isoforms of another AU-rich element-binding protein, HNRNPD/AUF1, as well as a related protein, laAUF1.
JKTBP1 is involved in stabilization and IRES-dependent translation of NRF mRNAs by binding to 5' and 3' untranslated regions.
GeneRIF
Reboll et al., Hannover, Germany. In J Mol Biol, 2011
The results indicate that JKTBP1 regulates the level of NRF protein expression by binding to both NRF 5' and 3' UTRs.
Microdeletion at chromosome 4q21 defines a new emerging syndrome with marked growth restriction, mental retardation and absent or severely delayed speech.
Sanlaville et al., Nancy, France. In J Med Genet, 2010
The boundaries and the sizes of the nine deletions are different, but an overlapping region of 1.37 Mb is defined; this region contains five RefSeq genes: PRKG2, RASGEF1B, HNRNPD, HNRPDL and ENOPH1.
Overexpression of JKTBP1 induces androgen-independent LNCaP cell proliferation through activation of epidermal growth factor-receptor (EGF-R).
GeneRIF
Wei et al., Chengdu, China. In Cell Biochem Funct, 2008
overexpression of JKTBP1 in LNCaP cells leads to abnormal cell proliferation
Structural basis for substrate recognition and dissociation by human transportin 1.
Sato et al., Yokohama, Japan. In Mol Cell, 2007
Here we describe four crystal structures of human Trn1 in a substrate-free form as well as in the complex with three NLSs (hnRNP D, JKTBP, and TAP, respectively).
Identification of differential expression of genes in hepatocellular carcinoma by suppression subtractive hybridization combined cDNA microarray.
Feng et al., Nanjing, China. In Oncol Rep, 2007
In addition to the overexpression of AFP, these genes (increased in the presence of HCC) are involved in many processes, such as transcription and protein biosynthesis (HNRPDL, PABPC1, POLR2K, SRP9, SNRPA, and six ribosomal protein genes including RPL8, RPL14, RPL41, RPS5, RPS17, RPS24), the metabolism of lipids and proteins (FADS1, ApoA-II, ApoM, FTL), cell proliferation (Syndecan-2, and Annexin A2), and signal transduction (LRRC28 and FMR1).
NRF IRES activity is mediated by RNA binding protein JKTBP1 and a 14-nt RNA element.
GeneRIF
Nourbakhsh et al., Hannover, Germany. In Rna, 2007
The data of this study show that JKTBP1 and the 14-nt element act independently to mediate NRF internal ribosome entry segment activity.
Crystallization and preliminary X-ray crystallographic studies of transportin 1 in complex with nucleocytoplasmic shuttling and nuclear localization fragments.
Sato et al., Yokohama, Japan. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2006
The transport receptor transportin1 (Trn1) transports various kinds of RNA-binding proteins such as JKTBP, hnRNP D and TAP.
Two motifs essential for nuclear import of the hnRNP A1 nucleocytoplasmic shuttling sequence M9 core.
Yamada et al., Yokohama, Japan. In Febs Lett, 2006
Key residues of the motifs are conserved in the shuttling signals of hnRNP D and JKTBP.
[The interaction of the intracellular domain of beta-amyloid precursor protein with JKTBP2].
GeneRIF
Chen et al., Xiamen, China. In Shi Yan Sheng Wu Xue Bao, 2005
Study shows that there is interaction of the intracellular domain of beta-amyloid precursor protein with JKTBP2, indicating that JKTBP2 may have an important function in AD formation.
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