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 ?
Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase.
Mitochondrial superoxide mediates doxorubicin-induced keratinocyte apoptosis through oxidative modification of ERK and Bd-2 ubiquitination.
Insig-dependent ubiquitination and degradation of 3-hydroxy-3-methylglutaryl coenzyme a reductase stimulated by delta-and gamma-tocotrienols.
Under normal cellular conditions, Nrf2 is sequestered in the cytoplasm by its negative regulator kelch-like ECH-associated protein 1 (Keapl) and maintained at low levels through ubiquitination and proteasomal degradation (Hut.
60) HER2/neu-mediated resistance to DNA-damaging agents requires the activation of Akt, which phosphorylates murine double minute 2 (MDM2) and therefore enhances MDM2-mediated ubiquitination and degradation of p53.
We observed the M protein to be highly conserved across genotypes M and B, and we found just 2 aa residues exclusive to genotype B that are not located in any region of the protein with a known function, such as budding (24,25), nuclear localization, or ubiquitination (26).
The degradation of proteins via proteasome pathway is mediated by the ubiquitination of proteins prior to degradation and subsequent cleavage by specific protease enzymes (Courtney et al.
CTA1 escapes degradation in spite of passing through the degradasome, presumably because of its low lysine content, an essential marker for ubiquitination (20).
The topics include the NF-[kappa]B family of transcription factors and its regulation, a structural guide to proteins of the NF-[kappa]B signaling module, ubiquitination and degradation of the inhibitors of NF-[kappa]B, selectivity of the NF-[kappa]B response, its oncogenic activation, the nuclear factor NF-[kappa]B pathway in inflammation, roles of the pathway in lymphocyte development and function, its role in the immune response of Drosophila, and using forward genetics to discover novel regulators of it.
It is not completely clear how proteins are identified for ubiquitination and destruction, but it seems that some have more 'unstable' amino-terminal ends than others and this may identify them to the ubiquitinating enzymes.

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