Exoribonuclease 3 (human ERI1 exoribonuclease family member 3) (ERI3)

Exoribonuclease 3 (human ERI1 exoribonuclease family member 3, ERI3) is a deeply conserved enzyme belonging to the DEDDh exonuclease family, with specific 3′–5′ exoribonuclease activity[1][2]. It participates in the 3′ end processing of 5.8S ribosomal RNA and the turnover of replication-dependent histone mRNAs, ensuring proper RNA maturation and degradation. The enzyme is also involved in the regulation and turnover of small regulatory RNAs such as microRNAs (miRNAs) and small interfering RNAs (siRNAs), contributing to the fine-tuning of RNAi-mediated gene silencing and epigenetic gene regulation. Structurally, it contains both a DEDDh catalytic core and a conserved SAP domain, which help anchor the enzyme to RNA and confer substrate specificity. Although it modulates essential pathways in RNA metabolism and posttranscriptional regulation, there are currently no known drugs targeting this enzyme, and no established biomarker or safety concerns exist regarding therapeutic modulation[1][2].

Other names

3'hExoThex1HEXOERI3 (as above)PINT1PRNPIPPRNPIP1Exoribonuclease 3Prion interactor 1Prion protein-interacting proteinFLJ22943

Not applicable; no drugs targeting ERI3/Exoribonuclease 3 are identified