Part:BBa_K4165014

UBC (Ubiquitin C)

This basic part encodes ubiquitin C which is essential in the degradation of misfolded proteins through the ubiquitin-proteasome cascade.

Usage and Biology

Ubiquitin c involved in the proteasomal degradation pathway of proteins. Ubiquitination of a misfolded protein starts with ubiquitin molecule being transferred by E1 ligase to E2 then to E3 ligase with both steps being in an ATP-dependent manner. Finally, The E3 ubiquitin ligase then promotes the transfer of ubiquitin onto the substrate by binding to both the protein substrate and the E2-bound ubiquitin. This results in recognition of polyubiquitinated protein by the 26S proteasomes to initiate its degradation.

Covalently attached ubiquitin can be a monomer (monoubiquitin), a polymer (polyubiquitin chains), or a linear polymer (polyubiquitin chains with a Met as the initiator) (linear polyubiquitin chains). When polyubiquitin chains bind to a protein, the Lys residue of the ubiquitin determines the chain's function.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 5
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

References

1. Komander D. (2009). The emerging complexity of protein ubiquitination. Biochemical Society transactions, 37(Pt 5), 937–953. https://doi.org/10.1042/BST0370937.

2. David, Y., Ziv, T., Admon, A., & Navon, A. (2010). The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. The Journal of biological chemistry, 285(12), 8595–8604. https://doi.org/10.1074/jbc.M109.089003.

3. Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M. (2014). RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1843(1), 47-60.

4. Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006). Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. Journal of the American Society of Nephrology: JASN, 17(7), 1807–1819. https://doi.org/10.1681/ASN.2006010083