ubiquitin

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u·biq·ui·tin

(ū-bik'kwi-tin), [MIM*191320]
A small (76 amino acyl residues) protein found in all cells of higher organisms and one with a structure that has changed minimally during evolutionary history; involved in at least two processes; histone modification and intracellular protein breakdown.
Farlex Partner Medical Dictionary © Farlex 2012

ubiquitin

(yo͞o-bĭk′wĭ-tĭn)
n.
A small protein found in all eukaryotic cells that attaches to other proteins, thereby regulating their activity or location or marking them for degradation.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

u·bi·qui·tin

(yū-bik'kwi-tin)
A small protein found in all cells of higher organisms; its structure has changed minimally during evolutionary history; involved in histone modification and intracellular protein breakdown.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

ubiquitin

A small 76-residue protein found in all animal cells and known to have altered minimally throughout evolutionary history. Ubiquitin is linked by covalent bonds to proteins destined for destruction by PROTEASOMES.
Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005

ubiquitin

a small PROTEIN, present in all eukaryotic cells (ubiquitous protein), containing a highly conserved sequence of 76 AMINO ACIDS, that is identical in a wide range of organisms including humans, fish and insects. Ubiquitin is involved in a number of cellular functions, such as protein degradation and modifications to CHROMATIN structure.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
References in periodicals archive ?
Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Yarden, "Negative regulation of receptor tyrosine kinases: unexpected links to c-Cbl and receptor ubiquitylation," Cell Research, vol.
Nrf2 has been proved to be maintained at a low level through Keap1-mediated ubiquitylation and 26S proteasome-mediated degradation.
Osley, "Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B," Genes & Development, vol.
Lehner, "Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation," The EMBO Journal, vol.
Up to now, over 60 histone modifications including acetylation, methylation, phosphorylation, and ubiquitylation have been identified, either by specific antibodies or spectrophotometric techniques [11].
In recent years, it has been demonstrated that the dynamic association of histones and their variants to the genome plays a very important role in chromatin structure, while their post-translational modifications--acetylation, phosphorylation, methylation, ubiquitylation and ADP-ribosylation--participate in chromatin function and gene regulation (Berger, 2001).
Citation: "Fbxl10/Kdm2b Recruits Polycomb Repressive Complex 1 to CpG Islands and Regulates H2A Ubiquitylation"; Xudong Wu et al.; Molecular Cell, 2013; DOI: 10.1016/j.molcel.2013.01.016
Ubiquitylation is a regulated posttranslational modification of proteins in which an ubiquitin molecule is attached to a lysine amino acid in the target protein [15, 16].
Degradation of p63[alpha] is also promoted by the E3 ubiquitin ligase ITCH via ubiquitylation at the N-terminal border of the SAM domain of the p63[alpha] isoforms [14].
Cdc25A phosphatase: combinatorial phosphorylation, ubiquitylation and proteolysis.