DDX42 — DEAD-box helicase 42
DDX42 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
DDX42's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | Centrosome Organization DNA/chromatin regulation | AKAP9, ARMCX6, CCNT2, CEP350, CUL5, DDHD1, DENND6A, DMTF1 +23 more | |
| Macrophages | Chromatin Transcriptional Regulation Housekeeping | AGO1, ARID1A, CARD8, CEPT1, CLOCK, CPSF7, CTNND1, DCAF10 +19 more | View in SCUBA |
About the gene
| Synonyms | RHELP, RNAHP, SF3b125, SF3B8 |
|---|---|
| Chromosome | 17: 63773603-63819317 |
| Predicted location | Intracellular |
| Essential gene | Yes |
| Protein class | Enzymes, Essential proteins, Plasma proteins, Predicted intracellular proteins |
| Molecular function | Helicase, Hydrolase, RNA-binding |
Function
ATP-dependent RNA helicase that binds to partially double- stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single- strand binding proteins. Also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP- bound form of the protein triggers annealing of complementary RNA strands. Required for assembly of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs: DDX42 associates transiently with the SF3B subcomplex of the 17S U2 SnRNP complex and is released after fulfilling its role in the assembly of 17S U2 SnRNP. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis- stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.