Protein Name:
ATP-dependent RNA helicase DDX1
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UniprotKB/SwissProt ID: Q92499 (Q92499)
Gene Name:
DDX1
Organism: Homo sapiens (Human)
Function: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). 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. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity) (Microbial infection) Required for HIV-1 Rev function as well as for HIV-1 and coronavirus IBV replication. Binds to the RRE sequence of HIV-1 mRNAs (Microbial infection) Required for Coronavirus IBV replication
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Nucleus. Cytoplasm. Cytoplasmic granule. Cytoplasm, cytosol. Mitochondrion. Cytoplasm
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of Q92499
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
110 |
SAFAIGSDGL C CQSREVKEWH |
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| 2 |
111 |
AFAIGSDGLC C QSREVKEWHG |
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| 3 |
139 |
MKGKHYYEVS C HDQGLCRVGW |
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| 4 |
145 |
YEVSCHDQGL C RVGWSTMQAS |
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| 5 |
231 |
HMKNQALFPA C VLKNAELKFN |
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| 6 |
406 |
SDGKRLQVIV C SATLHSFDVK |
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| 7 |
513 |
EHKMDQAIIF C RTKIDCDNLE |
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| 8 |
519 |
AIIFCRTKID C DNLEQYFIQQ |
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| 9 |
571 |
FKKGDVRFLI C TDVAARGIDI |
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