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Literature summary 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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.36 [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

EC Number Organism UniProt Comment Textmining
2.3.2.36 Human gammaherpesvirus 8 P90495
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.36 [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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 ?
2.3.2.36 [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

EC Number Synonyms Comment Organism
2.3.2.36 E3 ubiquitin ligase MIR1
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 Human gammaherpesvirus 8