DDX21

Nucleolar RNA helicase 2 is an enzyme that in humans is encoded by the DDX21 gene.[5][6]

DDX21
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2M3D
Identifiers
Aliases	DDX21, GUA, GURDB, RH-II/GU, RH-II/GuA, DEAD-box helicase 21, DExD-box helicase 21
External IDs	OMIM: 606357 MGI: 1860494 HomoloGene: 3473 GeneCards: DDX21
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q22.1 Start 68,956,170 bp[1] End 68,985,068 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 B4|10 32.43 cM Start 62,580,251 bp[2] End 62,602,281 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • rRNA binding • GO:0008026 helicase activity • 7SK snRNA binding • GO:0001948 protein binding • nucleic acid binding • double-stranded RNA binding • hydrolase activity • ATP binding • snoRNA binding • RNA binding • miRNA binding • identical protein binding Cellular component • membrane • nucleoplasm • cell nucleus • nucleolus • cytoplasm • mitochondrion • cytosol Biological process • positive regulation of gene expression, epigenetic • response to exogenous dsRNA • response to virus • transcription from RNA polymerase II promoter • transcription, DNA-templated • osteoblast differentiation • RNA secondary structure unwinding • rRNA processing • immune system process • positive regulation of myeloid dendritic cell cytokine production • positive regulation of I-kappaB kinase/NF-kappaB signaling • innate immune system • defense response to virus Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9188	56200
Ensembl	ENSG00000165732	ENSMUSG00000020075
UniProt	Q9NR30	Q9JIK5
RefSeq (mRNA)	NM_001256910 NM_004728	NM_019553
RefSeq (protein)	NP_001243839 NP_004719	NP_062426
Location (UCSC)	Chr 10: 68.96 – 68.99 Mb	Chr 10: 62.58 – 62.6 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

DDX21 has been shown to interact with C-jun.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000165732 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020075 - 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. 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.
6. "Entrez Gene: DDX21 DEAD (Asp-Glu-Ala-Asp) box polypeptide 21".
7. 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.