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Literature summary for 3.4.19.12 extracted from

  • Setsuie, R.; Suzuki, M.; Tsuchiya, Y.; Wada, K.
    Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses (2010), Neurochem. Int., 56, 911-918.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and hydrolase-deficient mutant UCH-L3 in mouse embryonic finbroblasts Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information embryonic fibroblasts from Uchl3-/- mice show an accumulation of polyubiquitinated proteins, the polyubiquitinated protein accumulation in Uchl3-/- embryonic fibroblasts is attenuated by the exogenous expression of wild-type, but not hydrolase activity deficient UCH-L3, overview Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
embryonic fibroblast MEFs Mus musculus
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skeletal muscle
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information UCH-L3 is capable of cleaving Ub from the Ub chains in vitro, and UCH-L3 directly hydrolyses polyubiquitinated proteins. Wild-type, but not its hydrolase activity or ubiquitin binding activity deficient, UCH-L3 shows the ability to cleave ubiquitin from polyubiquitinated lysozyme in vitro, which is no substrate of UCH-L1 Mus musculus ?
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Synonyms

Synonyms Comment Organism
Uchl3
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Mus musculus

General Information

General Information Comment Organism
physiological function UCH-L3 functions as a de-ubiquitinating enzyme in vivo. The polyubiquitinated protein accumulation in Uchl3-/- embryonic fibroblasts is attenuated by the exogenous expression of wild-type, but not hydrolase activity deficient UCH-L3 Mus musculus