CUL7 mutations The majority of<unk>  patients have been identified with CUL7 mutations. The Cullin 7 gene contains instructions for making the protein Cullin-7. Cullin-7 acts as scaffold protein in the E3 ubiquitin ligase complex. The role of this complex is to tag damaged and excess proteins in the cell with ubiquitin. Intracellular and extracellular signals within the cell highly regulate when and which proteins are tagged with ubiquitin. Once attached to the protein, ubiquitin serves as a signaling molecule to the proteasomes, which then bind to the ubiquinated proteins and degrades them. This ubiquitin-proteasome system acts as the cell's quality control system by breaking down unwanted proteins. Additionally, the system regulates the level of proteins involved in critical cell activities such as the timing of cell division and growth. Mutations in the CUL7 gene blocks the ability of the cullin-7 protein to bring together the components of this E3 ubiquitin ligase complex. This leads to impaired ubiquination and hence the aggregation of damaged, misfolded, and excess proteins. Disruption of the protein degradation process plays a role in the pathogensis of prenatal growth retardation in humans, a key feature of<unk> . The skeletal abnormalities that are present in individuals with this disorder suggests that this gene may play a role in the endochondral ossification process. Preliminary data suggests that CUL7 is in fact involved in chondrocyte growth and proliferation. OBS1 and CCDC8 mutations Not much is known about the mutations in the genes OBS1and CCD8 and their function in growth and development so far. However, the implications of<unk>  suggest that both these genes encode for proteins that play a role in the CUL7 ubiquination pathway.
3-M syndrome
3C syndrome
WHIM syndrome
RIDDLE syndrome
CAMFAK syndrome
HUPRA syndrome
STAR syndrome
TEMPI syndrome