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.

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.

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.

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.

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.
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.