RNA Helicase A

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DHX9
Protein DHX9 PDB 1uil.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DHX9, DDX9, LKP, NDH2, NDHII, RHA, RNA Helicase A, DEAH-box helicase 9, DExH-box helicase 9
External IDs MGI: 108177 HomoloGene: 1039 GeneCards: DHX9
RNA expression pattern
PBB GE DHX9 212105 s at fs.png

PBB GE DHX9 202420 s at fs.png

PBB GE DHX9 212107 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001357
NM_030588

NM_007842

RefSeq (protein)

NP_001348

NP_031868

Location (UCSC) Chr 1: 182.84 – 182.89 Mb Chr 1: 153.46 – 153.49 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

ATP-dependent RNA helicase A (RHA; also known as DHX9, LKP, and NDHI) is an enzyme that in humans is encoded by the DHX9 gene.[3][4][5]

Function[edit]

DEAD/DEAH box helicases are proteins, and are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein with RNA helicase activity. It may participate in melting of DNA:RNA hybrids, such as those that occur during transcription, and may play a role in X-linked gene expression. It contains 2 copies of a double-stranded RNA-binding domain, a DEXH core domain and an RGG box. The RNA-binding domains and RGG box influence and regulate RNA helicase activity.[5]The DHX9 gene is located on the long arm q of chromosome 1.

Interactions[edit]

DHX9 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Lee CG, Hurwitz J (Aug 1993). "Human RNA helicase A is homologous to the maleless protein of Drosophila". The Journal of Biological Chemistry. 268 (22): 16822–30. PMID 8344961. 
  4. ^ Zhang S, Grosse F (Apr 1997). "Domain structure of human nuclear DNA helicase II (RNA helicase A)". The Journal of Biological Chemistry. 272 (17): 11487–94. PMID 9111062. doi:10.1074/jbc.272.17.11487. 
  5. ^ a b "Entrez Gene: DHX9 DEAH (Asp-Glu-Ala-His) box polypeptide 9". 
  6. ^ Yang JP, Tang H, Reddy TR, Wong-Staal F (Aug 2001). "Mapping the functional domains of HAP95, a protein that binds RNA helicase A and activates the constitutive transport element of type D retroviruses". The Journal of Biological Chemistry. 276 (33): 30694–700. PMID 11402034. doi:10.1074/jbc.M102809200. 
  7. ^ Westberg C, Yang JP, Tang H, Reddy TR, Wong-Staal F (Jul 2000). "A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element". The Journal of Biological Chemistry. 275 (28): 21396–401. PMID 10748171. doi:10.1074/jbc.M909887199. 
  8. ^ Schlegel BP, Starita LM, Parvin JD (Feb 2003). "Overexpression of a protein fragment of RNA helicase A causes inhibition of endogenous BRCA1 function and defects in ploidy and cytokinesis in mammary epithelial cells". Oncogene. 22 (7): 983–91. PMID 12592385. doi:10.1038/sj.onc.1206195. 
  9. ^ Anderson SF, Schlegel BP, Nakajima T, Wolpin ES, Parvin JD (Jul 1998). "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A". Nature Genetics. 19 (3): 254–6. PMID 9662397. doi:10.1038/930. 
  10. ^ Wilson BJ, Giguère V (November 2007). "Identification of novel pathway partners of p68 and p72 RNA helicases through Oncomine meta-analysis". BMC Genomics. 8: 419. PMC 3225811Freely accessible. PMID 18005418. doi:10.1186/1471-2164-8-419. 
  11. ^ Reddy TR, Tang H, Xu W, Wong-Staal F (Jul 2000). "Sam68, RNA helicase A and Tap cooperate in the post-transcriptional regulation of human immunodeficiency virus and type D retroviral mRNA". Oncogene. 19 (32): 3570–5. PMID 10951562. doi:10.1038/sj.onc.1203676. 
  12. ^ Fujita H, Fujii R, Aratani S, Amano T, Fukamizu A, Nakajima T (Apr 2003). "Antithetic effects of MBD2a on gene regulation". Molecular and Cellular Biology. 23 (8): 2645–57. PMC 152551Freely accessible. PMID 12665568. doi:10.1128/mcb.23.8.2645-2657.2003. 
  13. ^ Tang H, Wong-Staal F (Oct 2000). "Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus". The Journal of Biological Chemistry. 275 (42): 32694–700. PMID 10924507. doi:10.1074/jbc.M003933200. 
  14. ^ Smith WA, Schurter BT, Wong-Staal F, David M (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". The Journal of Biological Chemistry. 279 (22): 22795–8. PMID 15084609. doi:10.1074/jbc.C300512200. 
  15. ^ Tetsuka T, Uranishi H, Sanda T, Asamitsu K, Yang JP, Wong-Staal F, Okamoto T (Sep 2004). "RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator". European Journal of Biochemistry / FEBS. 271 (18): 3741–51. PMID 15355351. doi:10.1111/j.1432-1033.2004.04314.x. 
  16. ^ Pellizzoni L, Charroux B, Rappsilber J, Mann M, Dreyfuss G (Jan 2001). "A functional interaction between the survival motor neuron complex and RNA polymerase II". The Journal of Cell Biology. 152 (1): 75–85. PMC 2193649Freely accessible. PMID 11149922. doi:10.1083/jcb.152.1.75. 

Further reading[edit]