RNA-binding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that functions as an RNA exosome cofactorthat directs a subset of non-coding short-lived RNAs for exosomaldegradation. NEXT is involved in surveillance andturnover of aberrant transcripts and non-coding RNAs. Binds preferentially polyuridinesequences and associates with newly synthesized RNAs, including pre-mRNAs and short-lived exosome substrates such as promoter upstreamtranscripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended productsfrom small nuclear RNAs (snRNAs). Participates in several biologicalprocesses including DNA damage response (DDR) and stress response. During stress response, activationof the p38MAPK-MK2 pathway decreases RBM7-RNA-binding and subsequentlythe RNA exosome degradation activities, thereby modulating the turnoverof non-coding transcriptome. Participates in DNAdamage response (DDR), through its interaction with MEPCE and LARP7, the core subunits of 7SK snRNP complex, that release the positivetranscription 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. [1-6]

MGAAAAEADRTLFVGNLETKVTEELLFELFHQAGPVIKVKIPKDKDGKPKQFAFVNFKHEVSVPYAMNLLNGIKLYGRPIKIQFRSGSSHAPQDVSLSYPQHHVGNSSPTSTSPSRYERTMDNMTSSAQIIQRSFSSPENFQRQAVMNSALRQMSYGGKFGSSPLDQSGFSPSVQSHSHSFNQSSSSQWRQGTPSSQRKVRMNSYPYLADRHYSREQRYTDHGSDHHYRGKRDDFFYEDRNHDDWSHDYDNRRDSSRDGKWRSSRH