Transferases;
Acyltransferases;
Aminoacyltransferases
BRITE hierarchy

[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (thioester bond-froming; RING-type)

[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine

[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine;
[acceptor protein]-L-cysteine

This relatively rare subpopulation of RING-type E3 ubiquitin transferases (cf. EC 2.3.2.27), found in mammals and herpes viruses, can transfer ubiquitin to a cysteine residue in target proteins. Additional ubiquitin molecules are polymerized on top of the initial ubiquitin molecule by formation of an isopeptide linkage with lysine48 in the pre-attached ubiquitin [2].

EC 2.3.2.36 created 2020

1  [PMID:15994556]

Cadwell K, Coscoy L.

Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase.

Science 309:127-30 (2005)
DOI:10.1126/science.1110340

2  [PMID:28604676]

Wang YJ, Bian Y, Luo J, Lu M, Xiong Y, Guo SY, Yin HY, Lin X, Li Q, Chang CCY, Chang TY, Li BL, Song BL.

Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2 through competitive oxidation.

Nat Cell Biol 19:808-819 (2017)
DOI:10.1038/ncb3551

3  [PMID:31953408]

Zhou ZS, Li MX, Liu J, Jiao H, Xia JM, Shi XJ, Zhao H, Chu L, Liu J, Qi W, Luo J, Song BL.

Competitive oxidation and ubiquitylation on the evolutionarily conserved cysteine confer tissue-specific stabilization of Insig-2.

Nat Commun 11:379 (2020)
DOI:10.1038/s41467-019-14231-w