Literature summary for 2.3.2.27 extracted from

Foglizzo, M.; Middleton, A.; Day, C.
Structure and function of the RING domains of RNF20 and RNF40, dimeric E3 ligases that monoubiquitylate Histone H2B (2016), J. Mol. Biol., 428, 4073-4086 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the RING domain (residues 907-975) at a resolution of 1.8 A. The core RING domain resembles other RING domains, with two zinc ions coordinated in a cross-braced arrangement by one His and seven Cys side chains. Residues in the core RING domain, the N-terminal alpha-helix, and the C-terminal tail comprise the dimer interface	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q5VTR2	isoform RNF20	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	no substrate: [E2 ubiquitin-conjugating enzyme UbcH5b]-S-ubiquitinyl-L-cysteine	Homo sapiens	?	-	-
[E2 ubiquitin-conjugating enzyme Ube2B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine	-	Homo sapiens	[E2 ubiquitin-conjugating enzyme Ube2B]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine	-	?

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Homo sapiens
More	the RING domains of RNF20 and RNF40 can heterodimerize to active dimers	Homo sapiens

Synonyms

Synonyms	Comment	Organism
BRE1A	-	Homo sapiens
RNF20	-	Homo sapiens

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Release 2023.1 (January 2023)