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Proteins/UNIPROT:Q8IU60
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping. Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts..
Function from UniProtKB (Q8IU60), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
44 statements
44 statements · 5 reference databases · Subject: DCP2 · Sources: gene ontology, Hetionet, Reactome, UniProt, WikiPathways
1 reaction
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA+waterCHEBI:63714+a 5'-end phospho-ribonucleoside in mRNA+2hydron
Catalysed by NUDT3 or NUDT17 or DCP2 or DCP1B or NUDT16 or DCP1A
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:67484CC BY 4.0Reference data
5 names
Resolves to: DCP2