Literature summary for 2.3.2.31 extracted from

White, R.R.; Ponsford, A.H.; Weekes, M.P.; Rodrigues, R.B.; Ascher, D.B.; Mol, M.; Selkirk, M.E.; Gygi, S.P.; Sanderson, C.M.; Artavanis-Tsakonas, K.
Ubiquitin-dependent modification of skeletal muscle by the parasitic nematode, Trichinella spiralis (2016), PLoS Pathog., 12, e1005977 .

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Application

Application	Comment	Organism
medicine	upon infection, Trichinella spiralis secretes E2 Ub-conjugating protein UBE2L3, located in the secretory organ of the parasite during the muscle stages of infection. UBE2L3 but specifically binds to a panel of human RING E3 ligases, including the RBR E3 ARIH2 with which it interacts with a higher affinity than the mammalian ortholog UbcH7/UBE2L3. Expression of UBE2L3 in skeletal muscle cells causes a global downregulation in protein ubiquitination, most predominantly affecting motor, sarcomeric and extracellular matrix proteins, thus mediating their stabilization with regards to proteasomal degradation	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O95376	isoform ARIH2	-

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Release 2023.1 (January 2023)