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Literature summary for 2.3.2.27 extracted from

  • Raheja, R.; Liu, Y.; Hukkelhoven, E.; Yeh, N.; Koff, A.
    The ability of TRIM3 to induce growth arrest depends on RING-dependent E3 ligase activity (2014), Biochem. J., 458, 537-545.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-ubiquitinyl-[UbcH5a]-L-cysteine + [p21]-L-lysine substrate p21 is a protein necessary for the proliferation of a subset of platelet-derived growth factor-transformed proneural glioma cells Mus musculus [UbcH5a]-L-cysteine + N6-ubiquitinyl-[p21]-L-lysine UbcH5a is a preferred E2 enzyme for TRIM3-dependent p21 ubiquitination. Ubiquitination is practically eliminated in a p21 K15R/K74R/K91R/K136R quadruple mutant ?

Synonyms

Synonyms Comment Organism
TRIM3
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Mus musculus

General Information

General Information Comment Organism
physiological function the RING domain is necessary for TRIM3-induced growth arrest of cells Mus musculus