Difference between revisions of "Part:BBa K4165015"

 
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Ubiquitin-conjugating E2 ligase has a role in the ubiquitination cascade for protein degradation.
 
Ubiquitin-conjugating E2 ligase has a role in the ubiquitination cascade for protein degradation.
  
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===Usage and Biology===
 
===Usage and Biology===
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Inactive RING/U-box type E3s, such lacking the active site cysteine residues to form thioester linkages with ubiquitin, or even the absence of E3 will not prevent UBE2W-catalyzed ubiquitination, albeit at a slow rate.
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===source===
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UBE2W: Q96B02 in Uniprot - NP_001001481.3 in NCBI
  
 
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<partinfo>BBa_K4165015 parameters</partinfo>
 
<partinfo>BBa_K4165015 parameters</partinfo>
 
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===Refrences===
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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

Revision as of 13:48, 6 October 2022


UBE2W

Ubiquitin-conjugating E2 ligase has a role in the ubiquitination cascade for protein degradation.

Usage and Biology

Inactive RING/U-box type E3s, such lacking the active site cysteine residues to form thioester linkages with ubiquitin, or even the absence of E3 will not prevent UBE2W-catalyzed ubiquitination, albeit at a slow rate.

source

UBE2W: Q96B02 in Uniprot - NP_001001481.3 in NCBI

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Refrences

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