DDX21

DEAD (Asp-Glu-Ala-Asp) box helicase 21
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2M3D​
Identifiers
Symbols	DDX21 ; GUA; GURDB; RH-II/GU; RH-II/GuA
External IDs	OMIM: 606357 MGI: 1860494 HomoloGene: 3473 GeneCards: DDX21 Gene
EC number	3.6.4.13
Gene ontology Molecular function • double-stranded RNA binding • ATP-dependent RNA helicase activity • protein binding • ATP binding • rRNA binding • snoRNA binding • poly(A) RNA binding • 7SK snRNA binding Cellular component • nucleus • nucleoplasm • nucleolus • membrane Biological process • osteoblast differentiation • rRNA processing • transcription from RNA polymerase II promoter • response to virus • RNA secondary structure unwinding • response to exogenous dsRNA Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9188	56200
Ensembl	ENSG00000165732	ENSMUSG00000020075
UniProt	Q9NR30	Q9JIK5
RefSeq (mRNA)	NM_001256910	NM_019553
RefSeq (protein)	NP_001243839	NP_062426
Location (UCSC)	Chr 10: 68.96 – 68.99 Mb	Chr 10: 62.58 – 62.6 Mb
PubMed search

Nucleolar RNA helicase 2 is an enzyme that in humans is encoded by the DDX21 gene.^[1][2]

Function

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 family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is an antigen recognized by autoimmune antibodies from a patient with watermelon stomach disease. This protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription.^[2]

Interactions

DDX21 has been shown to interact with C-jun.^[3]

References

1. Valdez BC, Henning D, Busch RK, Woods K, Flores-Rozas H, Hurwitz J, Perlaky L, Busch H (Jun 1996). "A nucleolar RNA helicase recognized by autoimmune antibodies from a patient with watermelon stomach disease". Nucleic Acids Res. 24 (7): 1220–4. doi:10.1093/nar/24.7.1220. PMC 145780. PMID 8614622.
2. "Entrez Gene: DDX21 DEAD (Asp-Glu-Ala-Asp) box polypeptide 21".
3. Westermarck J, Weiss C, Saffrich R, Kast J, Musti AM, Wessely M, Ansorge W, Séraphin B, Wilm M, Valdez BC, Bohmann D (Feb 2002). "The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription". EMBO J. 21 (3): 451–60. doi:10.1093/emboj/21.3.451. PMC 125820. PMID 11823437.

Further reading

• Valdez BC, Henning D, Perlaky L, Busch RK, Busch H (1997). "Cloning and characterization of Gu/RH-II binding protein". Biochem. Biophys. Res. Commun. 234 (2): 335–40. doi:10.1006/bbrc.1997.6642. PMID 9177271.
• Valdez BC, Wang W (2000). "Mouse RNA helicase II/Gu: cDNA and genomic sequences, chromosomal localization, and regulation of expression". Genomics 66 (2): 184–94. doi:10.1006/geno.2000.6209. PMID 10860663.
• Zhu K, Henning D, Valdez B, Busch H (2001). "Human RNA helicase II/Gu gene: genomic organization and promoter analysis". Biochem. Biophys. Res. Commun. 281 (4): 1006–11. doi:10.1006/bbrc.2001.4446. PMID 11237763.
• Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Westermarck J, Weiss C, Saffrich R, Kast J, Musti AM, Wessely M, Ansorge W, Séraphin B, Wilm M, Valdez BC, Bohmann D (2002). "The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription". EMBO J. 21 (3): 451–60. doi:10.1093/emboj/21.3.451. PMC 125820. PMID 11823437.
• Valdez BC, Yang H, Hong E, Sequitin AM (2002). "Genomic structure of newly identified paralogue of RNA helicase II/Gu: detection of pseudogenes and multiple alternatively spliced mRNAs". Gene 284 (1-2): 53–61. doi:10.1016/S0378-1119(01)00888-5. PMID 11891046.
• Henning D, So RB, Jin R, Lau LF, Valdez BC (2003). "Silencing of RNA helicase II/Gualpha inhibits mammalian ribosomal RNA production". J. Biol. Chem. 278 (52): 52307–14. doi:10.1074/jbc.M310846200. PMID 14559904.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Yang H, Henning D, Valdez BC (2005). "Functional interaction between RNA helicase II/Gu(alpha) and ribosomal protein L4". FEBS J. 272 (15): 3788–802. doi:10.1111/j.1742-4658.2005.04811.x. PMID 16045751.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (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.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.