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Validated All-in-One™ qPCR Primer for HNRNPD(NM_031370.3) Search again
Product ID:
HQP155145
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AUF1, AUF1A, HNRPD, P37, hnRNPD0
Gene Description:
heterogeneous nuclear ribonucleoprotein D
Target Gene Accession:
NM_031370.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid 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.
Gene References into function
- NMR structure of RNA binding domain and its interactions with RNA and DNA
- bcl-2 A and U rich element-binding protein involved in bcl-2 mRNA destabilization during apoptosis.
- regulates apoptosis by altering mRNA turnover and CDIR inhibits apoptosis by acting as a competitive inhibitor of AUF1, preventing AUF1 from binding to its targets
- selective AUF1 phosphorylation may regulate ARE-directed mRNA turnover by remodeling local RNA structures
- signal transduction pathways may regulate ARE-directed mRNA turnover by reversible phosphorylation of polysome-associated p40AUF1
- a mechanism whereby reduced cytoplasmic levels of AUF1 in MNT1 melanoma cells may lead to IL-10 overexpression, with deleterious consequences for tumor surveillance and rejection
- composition and fate (stability, translation) of HuR- and/or AUF1-containing ribonucleoprotein complexes depend on the target mRNA of interest, RNA-binding protein abundance, stress condition, and subcellular compartment
- calcineurin regulates AUF1 posttranslationally in vitro and PTH gene expression in vivo but still allows its physiological regulation by calcium and phosphate
- analysis of the structure of the C-terminal-binding domain (BD2) of HNRPD complexed with single-stranded d(TTAGGG) determined by NMR
- AUF1 binds to multiple destabilizing elements within the 3'-UTR that participate in the rapid turnover of the phosphoenolpyruvate carboxykinase mRNA.
- coordinated regulation of mRNA stability by HuR and AUF1 proteins contributes to the observed increase in ATF3 expression following amino acid limitation
- The multiple instability elements present within the 3'-UTR may function synergistically to mediate both the rapid degradation and the cAMP-induced stabilization of PEPCK mRNA. The latter process may result from a PKA-dependent phosphorylation of AUF1
- HuR shows increased binding to some V-ATPase mRNAs during ATP depletion; siRNA-mediated knockdown of HuR results in diminished V-ATPase expression.
- c-Yes 3'-UTR contains at least three newly identified adenine/uridine-rich elements (AREs) which are bound specifically by ARE-binding proteins HuR and AUF1.
- Differential expression of AU-rich mRNAs in response to LPL-mediated lipolysis might have an impact on physiological processes regulating lipid metabolism or pathophysiological processes promoting endothelial dysfunction and atherogenesis.
- AUF1 could function in a novel pathway mediating the oncogenic effects of NPM-ALK
- These results indicate that AUF1 binds to the AU-rich element in vivo and promotes IL-6 mRNA degradation.
- AUF1 cell cycle variations define genomic DNA methylation by regulation of DNMT1 mRNA stability
- Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation.
- Two mRNA binding proteins, HuR and AUF1, are colocalized and are capable of functional interaction in both the nucleus and cytoplasm.
- both HuR and AUF1 bind to discrete regions of DENR/DRP mRNA and that AUF1 silencing increases DENR/DRP protein levels.
- This study determined that hnRNP L interacts specifically with the hnRNP D/AUF1 in the yeast two-hybrid system.
- Because AUF1 proteins are major components of messenger RNA stability complexes, our findings suggest that these complexes form a novel macromolecular target structure for autoantibodies in rheumatic autoimmune diseases
- Chaperone Hsp27 is a novel subunit that is itself an AU-rich elements (ARE)-binding protein essential for rapid ARE-mRNA degradation.
- UV cross-linking and immunoprecipitation experiments revealed 2 ARE-binding proteins, AUF1 and HuR, associated with IL-8 mRNA in saliva.
- hnRNP D plays an important role in the translation of hepatitis C virus mRNA through interactions with the internal ribosomal entry site
- isoform-specific regulation of anti-inflammatory IL10 expression in monocytes
- Regulation of the hTERT promoter activity by MSH2, the hnRNPs K and D, and GRHL2 in human oral squamous cell carcinoma cells.