| Primary Identifier | IPR057051 | Type | Domain |
| Short Name | PARP14_RPM_1 |
| description | This domain is found at the N-terminal of proteins homologous to human mono-ADP-ribosyltransferase PARP14. It is also present in E3 ubiquitin-protein ligase DTX3L and RRM containing proteins. It shares significant sequence similarity with NID domain found in IFP35 and Nmi. These domains are predicted to adopt similar structures with topology typical for RNA-binding domains.PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved in multiple signaling pathways linked to cancer, inflammation, and infection. PARP14 is an ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate residues on target proteins [, , ]. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation [].DTX3L is a E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon- mediated antiviral responses []. In response to DNA damage, DTX3L mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1) []. In association with PARP9, this protein plays a role in antiviral responses by mediating 'Lys-48'-linked ubiquitination of encephalomyocarditis virus (EMCV) and human rhinovirus (HRV) C3 proteases and promotes their proteasomal-mediated degradation []. |
