DDX42

ATP-dependent RNA helicase DDX42 is an enzyme that in humans is encoded by the DDX42 gene.[5][6]

DDX42
Identifiers
Aliases	DDX42, DDX42P, RHELP, RNAHP, SF3B8, SF3b125, DEAD-box helicase 42
External IDs	OMIM: 613369 MGI: 1919297 HomoloGene: 49137 GeneCards: DDX42
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q23.3 Start 63,773,603 bp[1] End 63,819,317 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 E1 Start 106,216,926 bp[2] End 106,249,139 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GO:0001948 protein binding • hydrolase activity • ATP binding • GO:0008026 helicase activity • nucleic acid binding • RNA binding Cellular component • cytoplasm • Cajal body • membrane • cell nucleus • nucleoplasm • cytosol • nuclear speck • nucleolus Biological process • protein localization • RNA secondary structure unwinding • mRNA splicing, via spliceosome • regulation of apoptotic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11325	72047
Ensembl	ENSG00000198231	ENSMUSG00000020705
UniProt	Q86XP3	Q810A7
RefSeq (mRNA)	NM_007372 NM_203499	NM_028074
RefSeq (protein)	NP_031398 NP_987095	NP_082350 NP_001348569 NP_001348571 NP_001348572 NP_001348573
Location (UCSC)	Chr 17: 63.77 – 63.82 Mb	Chr 11: 106.22 – 106.25 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and 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. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. Two transcript variants encoding the same protein have been identified for this gene.[6]

Interactions

DDX42 has been shown to interact with SF3B1.[7]

Model organisms

Model organisms have been used in the study of DDX42 function. A conditional knockout mouse line called Ddx42^{tm1b(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.[8] Male and female animals underwent a standardized phenotypic screen[9] to determine the effects of deletion.[10][11][12][13] Additional screens performed: - In-depth immunological phenotyping[14]

Ddx42 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[9][14]
Peripheral blood leukocytes 6 Weeks	Normal
Insulin	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal

References

1. GRCh38: Ensembl release 89: ENSG00000198231 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020705 - 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. Suk K, Kim S, Kim YH, Oh SH, Lee MK, Kim KW, Kim HD, Seo YS (Apr 2000). "Identification of a novel human member of the DEAD box protein family". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1501 (1): 63–9. doi:10.1016/S0925-4439(00)00010-7. PMID 10727850.
6. "Entrez Gene: DDX42 DEAD (Asp-Glu-Ala-Asp) box polypeptide 42".
7. Will CL, Urlaub H, Achsel T, Gentzel M, Wilm M, Lührmann R (Sep 2002). "Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein". The EMBO Journal. 21 (18): 4978–88. doi:10.1093/emboj/cdf480. PMC 126279. PMID 12234937.
8. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
9. "International Mouse Phenotyping Consortium".
10. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
11. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
12. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
13. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
14. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Uhlmann-Schiffler H, Jalal C, Stahl H (2006). "Ddx42p--a human DEAD box protein with RNA chaperone activities". Nucleic Acids Research. 34 (1): 10–22. doi:10.1093/nar/gkj403. PMC 1325199. PMID 16397294.
• Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (Nov 2004). "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Will CL, Urlaub H, Achsel T, Gentzel M, Wilm M, Lührmann R (Sep 2002). "Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein". The EMBO Journal. 21 (18): 4978–88. doi:10.1093/emboj/cdf480. PMC 126279. PMID 12234937.