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DDX21 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9NR30 |
|---|---|
| Clone Names | 100712085 |
| Gene ID | 9188 |
|---|---|
| Other Names | Nucleolar RNA helicase 2, DEAD box protein 21, Gu-alpha, Nucleolar RNA helicase Gu, Nucleolar RNA helicase II, RH II/Gu, DDX21 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | DDX21 |
|---|---|
| Function | RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060, PubMed:28790157). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre- ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II- transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as a cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single- stranded RNA (foldase) (PubMed:9461305). Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). May bind to specific miRNA hairpins (PubMed:28431233). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (By similarity). |
| Cellular Location | Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JIK5}. Mitochondrion {ECO:0000250|UniProtKB:Q9JIK5}. Note=Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292) Interaction with WDR46 is required for localization to the nucleolus (PubMed:23848194). Colocalizes in the cytosol with DDX1, DHX36 and TICAM1. The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (By similarity) {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194} |
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Background
DEAD box proteins, characterized by the conserved motifAsp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They areimplicated in a number of cellular processes involving alterationof RNA secondary structure such as translation initiation, nuclearand mitochondrial splicing, and ribosome and spliceosome assembly.Based on their distribution patterns, some members of this familyare believed to be involved in embryogenesis, spermatogenesis, andcellular growth and division. This gene encodes a DEAD box protein,which is an antigen recognized by autoimmune antibodies from apatient with watermelon stomach disease. This protein unwindsdouble-stranded RNA, folds single-stranded RNA, and may playimportant roles in ribosomal RNA biogenesis, RNA editing, RNAtransport, and general transcription.
References
Holmstrom, T.H., et al. J. Biol. Chem. 283(11):7046-7053(2008)Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Olsen, J.V., et al. Cell 127(3):635-648(2006)Nousiainen, M., et al. Proc. Natl. Acad. Sci. U.S.A. 103(14):5391-5396(2006)
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