ubiquitin


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ubiquitin

[yü′bik·wə‚tin]
(biochemistry)
A small, 76-amino-acid, highly conserved protein present in the cytoplasm and nucleus of all eukaryotes (but not eubacteria and archaea). The covalent, ATP-dependent linkage of multiple ubiquitin molecules to proteins serves as a signal for their degradation by the 26S proteasome.
References in periodicals archive ?
Rice XA21 binding protein 3 is a ubiquitin ligase required for full Xa21-mediated disease resistance.
However, they contain a ubiquitin-interacting motif that weakly binds to ubiquitin. (61) Furthermore, the UBL domain of Ddi family proteins exhibits an unconventional feature compared with ubiquitin or other UBL proteins.
Fischer et al., "Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression," Journal of Neurochemistry, vol.
The finger domains can interact with ubiquitin to transfer its C-terminal to the cleft [79].
Geurink et al., "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis," Cell, vol.
Yang, "Auto-ubiquitination of Mdm2 enhances its substrate ubiquitin ligase activity," Journal of Biological Chemistry, vol.
Similarly, UBE3A, which is another important molecule in the ubiquitin system, was found to be associated with autistic symptoms in the Angelman syndrome (25,26).
The researchers said they also created ubiquitin variant (UbVs) that blocks the Crimean-Congo virus, the cause of a haemorrhagic fever that kills about 40 per cent of those infected, Medical Xpress reported.
We hypothesized pCAF is playing a novel role as ubiquitin E3 ligase for CIITA in addition to its traditional role as HAT.
Loss of Pin1 activity may increase the modification of ubiquitin in PSD proteins and lead to the loss of Shank protein, resulting in aberrant PSD structure.
Although both variants share a common C-terminal ubiquitin isopeptidase region, the structure of the Nterminal extension differs in terms of sequence, suggesting distinct roles in cellular processes [27-29].
NF-[kappa]B signaling is negatively regulated by USP11 or USP15-mediated removal of K48-linked ubiquitin chains from I[kappa]B[alpha] [92, 93].