[9] Having a well-conserved primary structure to its family members, HuR has two adjacent RNA recognition motifs (RRMs) proximal to the N-terminus, followed by a flexible hinge region next to a final RRM at the C-terminus.

[5] The RRM domains of HuR each contain two alpha helices with several antiparallel beta sheets in their secondary structure, a 20 amino-acid long N-terminus before RRM1 and RRM2, and a 12 amino acid linker connecting them.

[14] This RNA-binding protein has been found to be involved in a number of valuable cellular processes in mammals, including embryonic development, stress responses, and the immune system.

[21] For instance, protein arginine methyltransferase enzymes (PRMTs) methylate HuR to promote mRNA stabilization of certain target transcripts, such as SIRT1 in HeLa cells.

The abundance of HuR suggests a tumorigenic promotion of angiogenesis, cellular proliferation, and anti-apoptotic properties in cancer cells, purportedly due to the impact of mRNA stabilization and its ubiquitous presence in human tissue.