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UnknownThe RNA-Binding Domain of hnRNP U Extends beyond the RGG/RG Motifs.
Not available
S-EPMC11449452 | biostudies-literature
ProteomicsSpecific sDMA Modifications on the RGG/RG Motif of METTL14 Regulate Its Function in AML
Protein arginine methylations are crucial post-translational modifications (PTMs) in eukaryotes, playing a significant regulatory role in diverse biological processes. Different forms of arginine methylations are known to co-exist within densely modified arginine-rich protein regions. However, pinpo...
ORGANISM(S): Homo Sapiens 
PXD054570 |
UnknownThe RNA-binding domain of hnRNP U extends beyond the RGG/RG motifs.
Not available
S-EPMC10541603 | biostudies-literature
UnknownThe RNA-binding Selectivity of the RGG/RG Motifs of hnRNP U is Abolished by Elements Within the C-terminal Intrinsically Disordered Region.
Not available
S-EPMC11441334 | biostudies-literature
GenomicsRG/RGG boxes are common binding motifs in RNA-G-quadruplex-interacting proteins
RG/RGG boxes are common binding motifs in RNA-G-quadruplex-interacting proteins
PRJNA417119 | ENA
UnknownSpecific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML.
Not available
S-EPMC11889898 | biostudies-literature
UnknownThe RGG/RG motif of AUF1 isoform p45 is a key modulator of the protein's RNA chaperone and RNA annealing activities.
Not available
S-EPMC6550787 | biostudies-literature
UnknownORF73 LANA homologs of RRV and MneRV2 contain an extended RGG/RG-rich nuclear and nucleolar localization signal that interacts directly with importin β1 for non-classical nuclear import.
Not available
S-EPMC5929975 | biostudies-literature
UnknownIdentification and Characterization of Glycine- and Arginine-Rich Motifs in Proteins by a Novel GAR Motif Finder Program.
Not available
S-EPMC9957100 | biostudies-literature
ProteomicsOligomerization of PRMT1 Regulated RNA-Binding Protein Cascade Promotes Pancreatic Ductal Adenocarcinoma
PRMT1 is the predominant type I protein arginine methyltransferase responsible for generating monomethylarginine and asymmetric dimethylarginine (MMA and ADMA) in various protein substrates. It regulates numerous biological processes, including RNA metabolism, mRNA splicing, DNA damage repair, and c...
ORGANISM(S): Homo Sapiens 
2025-03-12 | PXD061743 |
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