Difference between revisions of "Part:BBa K4165014"
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<partinfo>BBa_K4165014 short</partinfo>
 
<partinfo>BBa_K4165014 short</partinfo>
  
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This basic part encodes for ubiquitin C which is essential in the degradation of misfolded proteins through the ubiquitin-proteasome cascade.
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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===
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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.
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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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===Source===
 
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UBC: Q15819 IN Uniprot - NP_066289.3 In NCBI
 
  
 
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===Refrences===
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===References===
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1-Komander D. (2009). The emerging complexity of protein ubiquitination. Biochemical Society transactions, 37(Pt 5), 937–953. https://doi.org/10.1042/BST0370937.
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1. Komander D. (2009). The emerging complexity of protein ubiquitination. Biochemical Society transactions, 37(Pt 5), 937–953. https://doi.org/10.1042/BST0370937.
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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.
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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.
  
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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.
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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


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