page_title: WD Repeat and Coiled Coil Containing Protein
section_title: Post-translational Modifications
hierarchical_section_title: WD Repeat and Coiled Coil Containing Protein / Regulation of Expression / Post-translational Modifications
caption_attribution_description: English: WDCP Conceptual Translation; Includes signaling sequences, post-translational modifications, and exon junctions
context_page_description: WD Repeat and Coiled-coiled containing protein is a protein which in humans is encoded by the WDCP gene. The function of the protein is not completely understood, but WDCP has been identified in a fusion protein with anaplastic lymphoma kinase found in colorectal cancer. WDCP has also been identified in the MRN complex, which processes double-stranded breaks in DNA.
context_section_description: 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: 
  Serine residues 43, 97, 147, 181, 267, 274, 278, 416, 417, 441, 504, 505, 528, 529, 535, 550, 590, 630, 676, 678, 686, 688, and 690.
  Threonine residues 73 and 385.
  Tyrosine residues 422 and 555.
  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. These sites were detected at:
  Serine residues 137, 243, 267, 271, 274, 295, 485, 528, 529, 688, and 695.  Sites 267, 274, 528, 529, and 688 overlap with a phosphorylation site.
  Threonine residues 412, 440, 447, 484, 534.
  N-glycosylation is the addition of a sugar molecule to an asparagine residue.  Asparagine residue 483 is the only detected N-glycosylation site in WDCP.
  There were no sites of amidation, C-linked mannosylation, GPI modification sites, non-classical protein secretion, transmembrane helices or regions, prediction of R and K cleavage sites, lipoprotein sites, sulfonated tyrosines, or Twin Arginine signal peptides.
caption: Figure 3. WDCP Conceptual Translation. Annotations include repeat sites, known post-translational modification sites, and protein-protein interaction sites
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