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Ubiquitination process

UBP6 S. c revisia low levels of free ubiquitin processes polyubiquitin chains at proteasome [94]... [Pg.192]

Sequence motifs [33330 ANK (ANKyrin-like) repeats AAA (ATPases associated with a variety of cellular activities) domain or CAD (conserved ATPase domain) with Walker A and B motifs KEKE (motif rich in alternating lysine (K) and glutamate (E) residues) cys box of UBPs (ubiquitin-processing enzymes) nun- LRR (leucine-rich repeat)-like motif [ZD MPN (found in Mprland Padl in the N terminus) motif ISSSSSSS PCI (for proteasome, COP9andinitiation factor 3) motif H UCH (ubiquitin C-terminal hydrolases) block. [Pg.210]

The human genome contains more than 90 different DUBs. Besides cleaving ubiquitin from distinct substrates, DUBs are also responsible for the recycling of free ubiquitin from ubiquitin chains and processing of ubiquitin- or ubiquitin like precursor proteins. Certain DUBs are also associated with the proteasome in order to detach ubiquitin chains before proteolysis. [Pg.422]

Proteosomal degration is the process by which improperly folded proteins or proteins with altered post-translational modifications are removed from a cell before they have a detrimental effect on cellular function. This is performed in small organelles known as proteosomes. Proteins are targeted for destruction in the proteosome by having a number of small ubiquitin molecules added. [Pg.1031]

Small Ubiquitin-like modifier (SUMO) is a conserved protein that is ubiquitously expressed in eukaryotes and is essential for viability. It serves as a reversible posttranslational modifier by forming an isopeptide bond with lysine residues in many target proteins, in a catalytic process termed SUMOylation. SUMOylation of proteins results in altered inter- or intramolecular interactions of the modified target (Fig. 1). [Pg.1163]

Hyperphosphorylation of ERAK-1 by itself and ERAK-4 causes ERAK-1 to dissociate from the membrane-bound complex. Tumour necrosis factor (TNF) receptor-associated factor-6 ( TRAF-6), a cytoplasmic protein, is activated by ERAK-1 and with TAB-2, another cytoplasmic protein, activates transforming growth factor-P (TFG-P)-activating kinase (TAK-1). During this process both TRAF-6 and TAK-1 become ubiquitinated. TAK-1 then promotes activation of the IkB kinases, or the IKK family, EKKa and EKK 3 (found in a complex with NFicB-essential modulator [NEMO]), which phosphorylate the IkB family, notably IkB-u. IkB-u is an inhibitor of NFkB as it sequesters NFkB in an... [Pg.1208]


See other pages where Ubiquitination process is mentioned: [Pg.157]    [Pg.134]    [Pg.198]    [Pg.410]    [Pg.283]    [Pg.90]    [Pg.126]    [Pg.157]    [Pg.134]    [Pg.198]    [Pg.410]    [Pg.283]    [Pg.90]    [Pg.126]    [Pg.568]    [Pg.886]    [Pg.1017]    [Pg.1163]    [Pg.1206]    [Pg.1206]    [Pg.1263]    [Pg.1263]    [Pg.1264]    [Pg.1265]    [Pg.1317]    [Pg.427]    [Pg.242]    [Pg.149]    [Pg.227]    [Pg.340]    [Pg.250]    [Pg.122]    [Pg.466]    [Pg.360]    [Pg.360]    [Pg.362]    [Pg.145]    [Pg.154]    [Pg.732]    [Pg.750]    [Pg.767]    [Pg.156]    [Pg.461]    [Pg.309]    [Pg.1]    [Pg.3]    [Pg.6]    [Pg.10]    [Pg.11]    [Pg.12]    [Pg.14]    [Pg.18]   
See also in sourсe #XX -- [ Pg.283 , Pg.284 ]




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Ubiquitin, ubiquitination

Ubiquitination

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