Literature summary for 2.3.2.27 extracted from

Yamauchi, K.; Wada, K.; Tanji, K.; Tanaka, M.; Kamitani, T.
Ubiquitination of E3 ubiquitin ligase TRIM5alpha and its potential role (2008), FEBS J., 275, 1540-1555.

Search for more literature for 2.3.2.27

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293T cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C15A	mutation in the conserved RING-finger domain, loss of autoubiquitination ability	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9C035	isoform TRIM5	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
ubiquitination	isoform TRIM5 is monoubiquitinated both by itself and by E3 ubiquitin ligase Ro52, and ubiquitination does not lead to proteasomal degradation. Monoubiquitination may be a signal for TRIM5 to translocate from cytoplasmic bodies to the cytoplasm	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[TRIM5-ubiquitin-carrier protein UbcH5B]-S-ubiquitinyl-L-cysteine + [TRIM5]-L-lysine	TRIM5 functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. TRIM5 is monoubiquitinated, and ubiquitination does not lead to proteasomal degradation. Monoubiquitination may be a signal for TRIM5 to translocate from cytoplasmic bodies to the cytoplasm	Homo sapiens	[TRIM5-ubiquitin-carrier protein UbcH5B]-L-cysteine + [TRIM5]-N6-ubiquitinyl-L-lysine	-	?

Synonyms

Synonyms	Comment	Organism
TRIM5	-	Homo sapiens
TRIM5alpha	-	Homo sapiens
tripartite motif-containing protein 5	-	Homo sapiens

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Release 2023.1 (January 2023)