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Literature summary for 2.3.2.36 extracted from

  • Cadwell, K.; Coscoy, L.
    Biochemistry Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase (2005), Science, 309, 127-130 .
    View publication on PubMed
Search for more literature for 2.3.2.36

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine Human gammaherpesvirus 8
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 [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
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Organism

Organism UniProt Comment Textmining
Human gammaherpesvirus 8 P90495
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
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 Human gammaherpesvirus 8 [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine this form of ubiquitination requires a cysteine residue in the intracytoplasmic tail of histocompatibility complex class I (MHC I) molecules. An MHC I molecule containing a single cysteine residue in an artificial glycine and alanine intracytoplasmic domain was endocytosed and degraded in the presence of MIR1. Thus, ubiquitination can occur on proteins lacking accessible lysines or an accessible N terminus Human gammaherpesvirus 8 [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
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Synonyms

Synonyms Comment Organism
E3 ubiquitin ligase MIR1
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 Human gammaherpesvirus 8