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A small protein found in all eukaryotic cells that attaches to other proteins, thereby regulating their activity or location or marking them for degradation.

American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.


(Biochemistry) biochem a small polypeptide, found in most eukaryotic cells, that combines with other proteins to make them susceptible to degradation
[C20: from ubiquitous + -in]
uˌbiquitiˈnation n
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014
References in periodicals archive ?
On the other hand, PROTACs are chimeric compounds with sites for binding targeted protein and for binding ubiquitin ligase and leads to degradation by proteolytic enzyme (proteasome) in cells.
Towards the end of the defense process, transcription factors (WRKY and MYB) and regulatory enzyme such as E3 ubiquitin ligases will regulate the expression of defense-associated genes (18-31).
In ERAD, ER proteins are ubiquitinated by ER-resident E3 ubiquitin ligases, extracted from the ER into the cytosol by [AAA.sup.+] ATPase p97/valosin containing protein (VCP), and degraded by the proteasome.
In someone with a relevant mutation that destroys this BAPl function, the ubiquitin compounds fail to be removed.
Taylor, "Function of the ubiquitin proteolytic pathway in the eye," Experimental Eye Research, vol.
To date, studies investigating ubiquitin ligase and bone remodeling have demonstrated that several E3 ubiquitin ligases take part in regulation of bone metabolism.
TNFAIP3, also known as A20, is an ubiquitin-editing enzyme, which has dual roles in ubiquitin ligase and deubiquitinase activity.
Ubiquitination is a biological process, in which the targeting proteins were modified with ubiquitin for degradation [1].
We examined the association between autism and serum transactive response DNA-binding protein-43 (TDP-43) and ubiquitin c-terminal hydrolase-L1 (UCH-L1) levels, both of which are members of the ubiquitin-proteosome system.
Biochemists and biologists from around the world offer 35 articles in various areas of biochemistry, such as protein misfolding diseases, amyloid proteins at the molecular level, the mechanisms and functions of spatial protein quality control, regulated protein degradation and the ubiquitin system and autophagy, ubiquitin ligases, mechanisms of deubiquitinase specificity and regulation, proteasomal and autophagic degradation systems, mechanisms of autophagy initiation, the systems biology of metabolism, metabolite measurement, isocitrate dehydrogenase and cancer therapeutics, tools for patchy switching in biology, the biochemistry of reductive dehalogenation, electric fields and enzyme catalysis, the eukaryotic DNA replication fork, and the telomerase mechanism of telomere synthesis.
Writing in the journal PLoS Pathogens, the team led by Professor Sachdev Sidhu of the University of Toronto described how they engineered the human ubiquitin protein into a new form that paralyses a key MERS enzyme, stopping the virus from replicating.