The mRNA secondary structures of the UTR regions exhibited a high number of predicted stem-loop structures in the WDCP transcript. The 5' UTR region closest to the start codon contained about 22 predicted loops. Stem loops in the 5' UTR near the start codon could indicate lower levels of expression. There are 108 predicted loops in the 3' UTR region. There are no known miRNA targets in the 3' UTR. WDCP Isoform 1 contains the following post-translational modifications:  Glycation is the addition of a sugar molecule to an amino acid and is associated with pathologies including renal failure and diabetes. Glycation is predicted to occur at lysine residues: 5, 7, 83, 189, 244, 262, 294, 325, 389, 405, 407, 461, 552, and 617. Acetylation is the addition of an acetyl group at the starting methionine residue. This is usually associated with metabolic-relating pathways. WDCP has one confirmed acetylation site at the starting methionine residue. Phosphorylation is the addition of a phosphate group to amino acids. It is mainly associated with cellular signaling pathways and can instigate tumor development. Serine, Threonine, and Tyrosine phosphorylation sites were identified in 27 residues at a NetPhos threshold of 0.9. Phosphorylation was detected at:   Possible kinases that interact with WDCP include Casein kinase 1, Casein kinase 2, cAMP, cGMP, P38MAPK, DNAPK, Protein kinase A, and Protein kinase C.   SUMOylation is the addition of a small ubiquitin-like modifier to lysine residues in proteins. SUMOYlation sites in WDCP include lysine residues 47, 152, 298, 310, 709, with lysine residues 47 and 152 having the highest probability of SUMOylation. SUMOylation can affect protein-protein interactions and affect protein ubiquitination. Palmitoylation is the addition of a fatty acid chain to cysteine residues. There is one confirmed site of palmitoylation at cysteine residue 714. GalNAc O-Glycosylation is the addition of a sugar molecule to a serine or threonine residue, which possibly increases structural stability. Some of these residues overlap with phosphorylation sites, indicating that these residues can switch between a phosphorylation site.