Difference between revisions of "Part:BBa K4165014"
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<partinfo>BBa_K4165014 short</partinfo> | <partinfo>BBa_K4165014 short</partinfo> | ||
− | This basic part encodes | + | This basic part encodes ubiquitin C which is essential in the degradation of misfolded proteins through the ubiquitin-proteasome cascade. |
===Usage and Biology=== | ===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. | 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. | ||
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− | === | + | ===References=== |
− | 1 | + | 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 |
Revision as of 14:57, 10 October 2022
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 5
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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