-
addition of
ubiquitin to a
substrate protein is
called ubiquitylation (or
ubiquitination or ubiquitinylation).
Ubiquitylation affects proteins in many ways:...
-
pathway which targets misfolded proteins of the
endoplasmic reticulum for
ubiquitination and
subsequent degradation by a protein-degrading complex,
called the...
-
enhancing the
trimethylation of
histone 3 at
lysine 27 (H3K27me3) and the
ubiquitination of
histone 2A at
lysine 119 (H2AK119) at its
target genes. Removing...
-
possible and
alter a protein's activity, interactions, or localization.
Ubiquitination by E3
ligases regulates diverse areas such as cell trafficking, DNA...
- degradation.
Recruitment of the E3
ligase to the
target protein results in
ubiquitination and
subsequent degradation of the
target protein via the proteasome...
-
substrates and
initiate the
degradation process. The
overall system of
ubiquitination and
proteasomal degradation is
known as the ubiquitin–proteasome system...
- complex) is a multi-protein E3
ubiquitin ligase complex that
catalyzes the
ubiquitination of
proteins destined for 26S
proteasomal degradation.
Along with the...
- acetylation, methylation, phosphorylation,
ubiquitination, and sumoylation. Acetylation, phosphorylation, and
ubiquitination are the most
common and most studied...
-
Through a
mechanism which has not been
completely elucidated, this
ubiquitination results in
reduced levels of
fibroblast growth factor 8 (FGF8) and fibroblast...
-
removal from the
protein leads to less
ubiquitination or if
their addition to
another protein leads to more
ubiquitination. In contrast, ubiquitin-independent...