Anti-RBM7 antibody

Target data

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 (PubMed : 25189701, PubMed : 25525152, PubMed : 25578728, PubMed : 25852104, PubMed : 27871484). NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs (PubMed : 25189701, PubMed : 25852104, PubMed : 27871484). 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) (PubMed : 25189701, PubMed : 25525152, PubMed : 25578728, PubMed : 25852104). Participates in several biological processes including DNA damage response (DDR) and stress response (PubMed : 25525152, PubMed : 30824372). 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 (PubMed : 25525152). 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 (PubMed : 30824372).