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.

ubiquitin

[yo̅o̅bik′witin]
a small polypeptide that is involved in histone modification and is a marker for intracellular protein transport and breakdown. It is found in all cells of higher organisms.

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.

ubiquitin (yōōˈ·biˑ·kwi·tin),

n a 76-amino acid polypeptide from modification of histones; present in yeast and in most eukaryotic cells.

ubiquitin

heat shock (cell stress) protein present in mammalian cytosol; attaches to other cytosolic proteins and marks them for degradation either by specific proteases or by lysosomal enzymes.
References in periodicals archive ?
It is involved in the process of ubiquitination of proteins destined for degradation via the proteosomal pathway to remove oxidized or misfolded proteins (13).
57) ITCH, in contrast, causes ubiquitination of RIP2 that induces reduced RIP2 activation and thus ITCH deficiency is associated with mucosal inflammation possibly due to inappropriate RIP2-mediated pro-inflammatory function.
Instead of gene editing or protein therapy, we have a new mechanism that may be ripe for proteasomal inhibitors or other targets of the ubiquitination pathway," he added.
Mellman, "Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination," Nature, vol.
The quantity, stability, and activity of p53 are regulated by various posttranslational modifications, including phosphorylation, ubiquitination, and acetylation.
For the maintenance of homeostasis, protein ubiquitination and relevant pathways were activated to remove the excessive reactive oxygen species and metabolite waste.
2013) A first-in-class, first-in-human, phase I trial of p28, a non-HDM2-mediated peptide inhibitor of p53 ubiquitination in patients with advanced solid tumours.
University of Lausanne associate professor, Margot Thome-Miazza, said, 'We have previously identified a novel way of regulating the catalytic activity of MALT1 via a protein modification called ubiquitination.
The ubiquitination system differs in one key way from the methylation and phosphorylation timing operations we mentioned above.
Immunofluorescence reveals ubiquitination of retained distal cytoplasmic droplets on ejaculated porcine spermatozoa.

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