HNRPD

From Wikipedia, the free encyclopedia


Heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa)
PDB rendering based on 1hd0.
Available structures: 1hd0, 1hd1, 1iqt, 1wtb, 1x0f
Identifiers
Symbol(s) HNRPD; AUF1; AUF1A; P37; hnRNPD0
External IDs OMIM: 601324 HomoloGene22410
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 3184 n/a
Ensembl ENSG00000138668 n/a
Uniprot Q14103 n/a
Refseq NM_001003810 (mRNA)
NP_001003810 (protein)
n/a (mRNA)
n/a (protein)
Location Chr 4: 83.49 - 83.51 Mb n/a
Pubmed search [1] n/a

Heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa), also known as HNRPD, is a human gene.[1]

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. 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 repeats of quasi-RRM domains that bind to RNAs. It localizes to both the nucleus and the cytoplasm. This protein is implicated in the regulation of mRNA stability. Alternative splicing of this gene results in four transcript variants.[1]

[edit] References

[edit] Further reading

  • Tay N, Chan SH, Ren EC (1992). "Identification and cloning of a novel heterogeneous nuclear ribonucleoprotein C-like protein that functions as a transcriptional activator of the hepatitis B virus enhancer II.". J. Virol. 66 (12): 6841–8. PMID 1433497. 
  • Lahiri DK, Thomas JO (1986). "A cDNA clone of the hnRNP C proteins and its homology with the single-stranded DNA binding protein UP2.". Nucleic Acids Res. 14 (10): 4077–94. PMID 3754960. 
  • Kajita Y, Nakayama J, Aizawa M, Ishikawa F (1995). "The UUAG-specific RNA binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2xRBD-Gly family.". J. Biol. Chem. 270 (38): 22167–75. PMID 7673195. 
  • Zhang W, Wagner BJ, Ehrenman K, et al. (1994). "Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1.". Mol. Cell. Biol. 13 (12): 7652–65. PMID 8246982. 
  • Wagner BJ, Long L, Rao PN, et al. (1997). "Localization and physical mapping of genes encoding the A+U-rich element RNA-binding protein AUF1 to human chromosomes 4 and X.". Genomics 34 (2): 219–22. doi:10.1006/geno.1996.0269. PMID 8661052. 
  • Kiledjian M, DeMaria CT, Brewer G, Novick K (1997). "Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the alpha-globin mRNA stability complex.". Mol. Cell. Biol. 17 (8): 4870–6. PMID 9234743. 
  • Wagner BJ, DeMaria CT, Sun Y, et al. (1998). "Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms.". Genomics 48 (2): 195–202. doi:10.1006/geno.1997.5142. PMID 9521873. 
  • Dempsey LA, Li MJ, DePace A, et al. (1998). "The human HNRPD locus maps to 4q21 and encodes a highly conserved protein.". Genomics 49 (3): 378–84. doi:10.1006/geno.1998.5237. PMID 9615222. 
  • Siomi MC, Fromont M, Rain JC, et al. (1998). "Functional conservation of the transportin nuclear import pathway in divergent organisms.". Mol. Cell. Biol. 18 (7): 4141–8. PMID 9632798. 
  • Tolnay M, Vereshchagina LA, Tsokos GC (1999). "Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-binding protein.". Biochem. J. 338 ( Pt 2): 417–25. PMID 10024518. 
  • Nagata T, Kurihara Y, Matsuda G, et al. (1999). "Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0.". J. Mol. Biol. 287 (2): 221–37. PMID 10080887. 
  • Laroia G, Cuesta R, Brewer G, Schneider RJ (1999). "Control of mRNA decay by heat shock-ubiquitin-proteasome pathway.". Science 284 (5413): 499–502. PMID 10205060. 
  • Blaxall BC, Dwyer-Nield LD, Bauer AK, et al. (2000). "Differential expression and localization of the mRNA binding proteins, AU-rich element mRNA binding protein (AUF1) and Hu antigen R (HuR), in neoplastic lung tissue.". Mol. Carcinog. 28 (2): 76–83. PMID 10900464. 
  • Arao Y, Kuriyama R, Kayama F, Kato S (2000). "A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D.". Arch. Biochem. Biophys. 380 (2): 228–36. doi:10.1006/abbi.2000.1938. PMID 10933876. 
  • Grosset C, Chen CY, Xu N, et al. (2000). "A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.". Cell 103 (1): 29–40. PMID 11051545. 
  • Katahira M, Miyanoiri Y, Enokizono Y, et al. (2001). "Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA.". J. Mol. Biol. 311 (5): 973–88. doi:10.1006/jmbi.2001.4862. PMID 11531333. 
  • Lapucci A, Donnini M, Papucci L, et al. (2002). "AUF1 Is a bcl-2 A + U-rich element-binding protein involved in bcl-2 mRNA destabilization during apoptosis.". J. Biol. Chem. 277 (18): 16139–46. doi:10.1074/jbc.M201377200. PMID 11856759. 
  • Tolnay M, Juang YT, Tsokos GC (2002). "Protein kinase A enhances, whereas glycogen synthase kinase-3 beta inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashion.". Biochem. J. 363 (Pt 1): 127–36. PMID 11903055. 
  • Pioli PA, Hamilton BJ, Connolly JE, et al. (2002). "Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1.". J. Biol. Chem. 277 (38): 35738–45. doi:10.1074/jbc.M204002200. PMID 12107167. 
  • Shchors K, Yehiely F, Kular RK, et al. (2003). "Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27.". J. Biol. Chem. 277 (49): 47061–72. doi:10.1074/jbc.M202272200. PMID 12356764.