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Literature summary for 3.4.25.1 extracted from

  • Elangovan, M.; Shin, D.Y.; Yoo, Y.J.
    The ubiquitin-interacting motifs of S5a as a unique upstream inhibitor of the 26S proteasome (2009), Biochem. Biophys. Res. Commun., 388, 723-726.
    View publication on PubMed
Search for more literature for 3.4.25.1

Protein Variants

Protein Variants Comment Organism
additional information Ubiquitinated proteins accumulate upon ectopic expression of S5aC. Ectopic S5a-UIM expression arrests cell cycle at G0 rather than at G2/M by epoxomicin. Downregulation of S5a by siRNA Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
epoxomicin inhibits the proteasome and causes cell cycle arrest at G2/M Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
A-549 cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate docking sites, e.g. S5a, contain ubiquitin-interacting motifs that selectively recruit ubiquinated proteins to the proteasome. Human S5a-ubiquitin-interacting motifs stabilize only a subset of proteasomal substrates. Proliferation of A549 lung cancer cells is inhibited by S5a-ubiquitin-interacting motifs. S5a-ubiquitin-interacting motifs result in an increase in the number of apoptotic G0 cells, presumably because of inhibition of a subset of proteasomal substrate proteins Homo sapiens ?
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 ?
unstable green fluorescence protein + H2O artificial substrate for the proteasome. The model proteasomal substrate is stabilized by the carboxyl-terminal half of S5a, S5aC Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
26S proteasome
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 Homo sapiens

General Information

General Information Comment Organism
physiological function the ubiquitin-proteasome system is involved in many cellular functions by mediating selective protein degradation. Protein substrates are first selected and marked by polyubiquitination, polyubiquitinated proteins are next recognized and degraded by the 26S proteasome, which consists of a 20S catalytic core particle and a 19S regulatory particle. Once polyubiquitin on a substrate protein is recruited to the 19S RP, the protein moiety is unfolded, translocated into the 20S CP, and finally degraded with release of polyubiquitin, which is processed into free ubiquitin and recycled Homo sapiens