DHX32

Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32 is an enzyme that in humans is encoded by the DHX32 gene.[5]

DHX32
Identifiers
AliasesDHX32, DDX32, DHLP1, DEAH-box helicase 32 (putative)
External IDsOMIM: 607960 MGI: 2141813 HomoloGene: 56798 GeneCards: DHX32
Gene location (Human)
Chr.Chromosome 10 (human)[1]
Band10q26.2Start125,836,337 bp[1]
End125,896,436 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

55760

101437

Ensembl

ENSG00000089876

ENSMUSG00000030986

UniProt

Q7L7V1

Q8BZS9

RefSeq (mRNA)

NM_018180

NM_001286030
NM_001286031
NM_001286032
NM_133941
NM_001357685

RefSeq (protein)

NP_060650

NP_001272959
NP_001272960
NP_001272961
NP_598702
NP_001344614

Location (UCSC)Chr 10: 125.84 – 125.9 MbChr 7: 133.72 – 133.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), 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 DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a member of this family. The function of this member has not been determined. Alternative splicing of this gene generates two transcript variants, but the full length nature of one of the variants has not been defined.[5]

References
  1. GRCh38: Ensembl release 89: ENSG00000089876 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000030986 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: DHX32 DEAH (Asp-Glu-Ala-His) box polypeptide 32".

Further reading
  • Alli Z, Chen Y, Abdul Wajid S, et al. (2007). "A role for DHX32 in regulating T-cell apoptosis". Anticancer Res. 27 (1A): 373–7. PMID 17352256.
  • Chen Y, Alli Z, Ackerley C, et al. (2007). "Altered distribution of heat shock protein 60 (Hsp60) with dysregulated expression of DHX32". Exp. Mol. Pathol. 82 (3): 256–61. doi:10.1016/j.yexmp.2006.11.002. PMID 17174952.
  • Alli Z, Ackerley C, Chen Y, et al. (2007). "Nuclear and mitochondrial localization of the putative RNA helicase DHX32". Exp. Mol. Pathol. 81 (3): 245–8. doi:10.1016/j.yexmp.2006.07.005. PMID 16959245.
  • Alli Z, Nam EH, Beimnet K, Abdelhaleem M (2006). "The activation-induced expression of DHX32 in Jurkat T cells is specific and involves calcium and nuclear factor of activated T cells". Cell. Immunol. 237 (2): 141–6. doi:10.1016/j.cellimm.2005.12.003. PMID 16414036.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Abdelhaleem M (2002). "The novel helicase homologue DDX32 is down-regulated in acute lymphoblastic leukemia". Leuk. Res. 26 (10): 945–54. doi:10.1016/S0145-2126(02)00040-1. PMID 12163057.
  • Liu J, Yuan Y, Huan J, Shen Z (2001). "Inhibition of breast and brain cancer cell growth by BCCIPalpha, an evolutionarily conserved nuclear protein that interacts with BRCA2". Oncogene. 20 (3): 336–45. doi:10.1038/sj.onc.1204098. PMID 11313963.


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