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Literature summary for 2.3.2.24 extracted from

  • Hoeller, D.; Hecker, C.M.; Wagner, S.; Rogov, V.; Doetsch, V.; Dikic, I.
    E3-independent monoubiquitination of ubiquitin-binding proteins (2007), Mol. Cell, 26, 891-898.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the presence of ubiquitin-binding domains (UBDs) allows the ubiquitination of host proteins independently of E3 ligases. UBDs of different types, including ubiquitin-interacting motif UIM, ubiquitin-associated domain UBM, and ubiquitin-binding zinc finger domain UBZ, can directly cooperate with ubiquitin-charged E2 enzymes to promote monoubiquitination. Ubiquitin-loaded E2 and substrates interact in cells and E2 enzymes are essential for their monoubiquitination in vivo. This modification is mechanistically and functionally distinct from E3-mediated and growth factor-dependent monoubiquitination. The ability to transfer ubiquitin to a substrate is a common feature of all tested E2 enzymes. However, E2 enzymes show substrate specificity Homo sapiens ?
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[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6 Homo sapiens [ubiquitin-carrier protein UbcH2]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6 Homo sapiens [ubiquitin-carrier protein UbcH2]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH5A]-S-ubiquitinyl-L-cysteine + [Stam2]-L-lysine substrate protein Stam2 contains a N-terminal ubiquitin-interacting motif and VHS domain, it is most strongly ubiquitinated by E2 isoform UbcH5A Homo sapiens [ubiquitin-carrier protein UbcH5A]-L-cysteine + [Stam6]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6 Homo sapiens [ubiquitin-carrier protein UbcH5]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6 Homo sapiens [ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol tau]-L-lysine substrate protein Pol tau contains two C-terminal ubiquitin-associated domains. It is ubiquitinated by all E2 isoforms tested Homo sapiens [ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol tau]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6 Homo sapiens [ubiquitin-carrier protein UbcH6]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
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[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6 Homo sapiens [ubiquitin-carrier protein UbcH6]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
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