Mouse Anti-DDX1 Recombinant Antibody (0997) (CBMAB-0997-YC)

DEAD (Asp-Glu-Ala-Asp) box polypeptide 1

DDX1 is a DEAD box protein of unknown function which shows high transcription levels in 2 retinoblastoma cell lines and in tissues of neuroectodermal origin. DEAD box proteins 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.

DBP-RB; UKVH5d

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 proinflammatory 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.

Defense response to virus Source: UniProtKB-KW
DNA duplex unwinding Source: UniProtKB
Double-strand break repair Source: UniProtKB
Innate immune response Source: UniProtKB-KW
Multicellular organism development Source: UniProtKB
Nucleic acid phosphodiester bond hydrolysis Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Protein localization to cytoplasmic stress granule Source: AgBase
Regulation of translational initiation Source: UniProtKB
Spliceosomal complex assembly Source: UniProtKB
tRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
Viral process Source: UniProtKB-KW

Cytoplasm; Cytosol; Nucleus; Mitochondrion; Cytoplasmic granule. Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (PubMed:24608264). Colocalizes in the cytosol with DDX21, DHX36 and TICAM1. Colocalizes in the mitochondria with TICAM1 and poly(I:C) RNA ligand. The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) stimulation (By similarity).
Cytoplasm. (Microbial infection) Relocalized to the cytoplasm with a perinuclear staining pattern in avian infectious bronchitis virus (IBV)-infected cells (PubMed:20573827). Required for proper localization of HIV-1 Rev (PubMed:15567440).

Phosphorylated by ATM kinase; phosphorylation is increased in response to ionizing radiation (IR).