RBM7 — RNA binding motif protein 7
RBM7 belongs to a gene co-expression module in 1 of 30 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.
RBM7's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Colonocytes | GPCR Peptide Signaling Secretion | ABHD11, AKIRIN1, AVPI1, BAG1, DNAJA1, DNAJA2, EDN1, FBXO33 +31 more | View in SCUBA |
About the gene
| Chromosome | 11: 114400030-114414203 |
|---|---|
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Predicted intracellular proteins |
| Molecular function | RNA-binding |
| Biological process | Meiosis |
Function
RNA-binding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs. Binds preferentially polyuridine sequences and associates with newly synthesized RNAs, including pre- mRNAs and short-lived exosome substrates such as promoter upstream transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products from small nuclear RNAs (snRNAs). Participates in several biological processes including DNA damage response (DDR) and stress response. During stress response, activation of the p38MAPK-MK2 pathway decreases RBM7-RNA-binding and subsequently the RNA exosome degradation activities, thereby modulating the turnover of non-coding transcriptome. Participates in DNA damage response (DDR), through its interaction with MEPCE and LARP7, the core subunits of 7SK snRNP complex, that release the positive transcription elongation factor b (P-TEFb) complex from the 7SK snRNP. In turn, activation of P-TEFb complex induces the transcription of P- TEFb-dependent DDR genes to promote cell viability.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.