This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. It is an RRM domain found second in PARP14.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 [].
This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found sixth in PARP14.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 [].
This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found fifth in PARP14.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 [].
This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. It is a KH domain found first in human PARP14.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 [].
This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found second in human PARP14.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 [].
This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found fourth in PARP14.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 [].
This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. It is a KH domain found third in PARP14.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 [].
This entry represents the WWE domain of protein mono-ADP-ribosyltransferase PARP14 from mouse and similar proteins from vertebrates. PARP14 is an ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate residues on target proteins []. It is related to inhibition of STAT1 phosphorylation, however it has been suggested that this may be the result of sumoylation of STAT1 'Lys-703' [].WWE domains are characterised by the presence of a Trp-Trp-Glu region, which is important for the structure stabilisation of PARP14. WWE domains can bind to ADP-Ribose derivatives, including iso-ADP-ribose, a molecule specifically found in PAR and promote interactions with ubiquitinated proteins. The PARP14 WWE domain, however, is unable to bind to any ADP-ribose derivatives and whether it interacts with iso-ADP ribose or ubiquitinated targets is unknown.
This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins including mono-ADP-ribosyltransferase PARP9. It is a KH domain found eighth in PARP14.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 [].PARP9 in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses []. It suppresses PARP14-mediated STAT6 ADP-ribosylation []. During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 []. PARP9 is a multidomain protein, predicted to contain only a single KH domain.
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 [].
