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Our findings establish the role of DIS3L2 and oligouridylation as the cytoplasmic quality control for highly structured ncRNAs
Studies indicate important roles of the exoribonucleases DIS3L2 and XRN1 (show XRN1 Proteins) in cellular function, viability and disease.
these results indicate that catalytically inactive DIS3L2, characteristic of Perlman syndrome, can lead to deregulation of its target RNAs to disturb transcriptome homeostasis.
DIS3L2 interacts with Ago2 (show EIF2C2 Proteins) and governs target RNA-directed miRNA degradation.
DIS3L2 is the missing component of the LIN28 (show LIN28A Proteins)-TUT4 (show ZCCHC11 Proteins)/7-DIS3L2 pathway required for the repression of let-7 in pluripotent cells.
in cellular models DIS3L2 knockdown is associated with abnormalities of cell growth and division
Germline mutations in DIS3L2 cause the Perlman syndrome of overgrowth and Wilms tumor susceptibility.
structure of mouse Dis3l2 in complex with an oligoU RNA to mimic the uridylated tail of pre-let-7
identification of Dis3l2 as the 3'-5' exonuclease (show EXOSC10 Proteins) responsible for the decay of uridylated pre-let-7 in mouse embryonic stem cells
The protein encoded by this gene is similar in sequence to 3'/5' exonucleolytic subunits of the RNA exosome. The exosome is a large multimeric ribonucleotide complex responsible for degrading various RNA substrates. Several transcript variants, some protein-coding and some not, have been found for this gene.
DIS3 mitotic control homolog-like 2
, DIS3-like exonuclease 2
, DIS3 mitotic control-like 2
, DIS3 mitotic control homolog (S. cerevisiae)-like 2
, DIS3-like exonuclease 2-like
, family with sequence similarity 6, member A