Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.22.68 extracted from

  • Nishida, T.; Yamada, Y.
    The nucleolar SUMO-specific protease SMT3IP1/SENP3 attenuates Mdm2-mediated p53 ubiquitination and degradation (2011), Biochem. Biophys. Res. Commun., 406, 285-291.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of FLAG-SMT3IP1 in COS-7 cells, coexpression with His6-ubiquitin. Overexpression of SMT3IP1 in cells results in the accumulation of Mdm2 in the nucleolus and increased stability of the p53 protein Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Mus musculus 5634
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Synonyms

Synonyms Comment Organism
SMT3IP1
-
Mus musculus
SMT3IP1/SENP3
-
Mus musculus
SUMO-specific protease
-
Mus musculus

General Information

General Information Comment Organism
physiological function nucleolar SUMO-specific protease, SMT3IP1/SENP3, controls the p53–Mdm2 pathway. SMT3IP1 interacts with p53 and Mdm2, and desumoylates both proteins. SMT3IP1 bound to the acidic domain of Mdm2, which also mediates the p53 interaction, and competes with p53 for binding. Increasing expression of SMT3IP1 suppresses Mdm2-mediated p53 ubiquitination and subsequent proteasomal degradation. Desumoylation activity of SMT3IP1 is not necessary for p53 stabilization Mus musculus