Literature summary for 2.3.1.286 extracted from

Guo, X.; Kesimer, M.; Tolun, G.; Zheng, X.; Xu, Q.; Lu, J.; Sheehan, J.K.; Griffith, J.D.; Li, X.
The NAD(+)-dependent protein deacetylase activity of SIRT1 is regulated by its oligomeric status (2012), Sci. Rep., 2, 640.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q923E4	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	phosphorylation of Thr522 is an important allosteric mechanism to activate SIRT1 in response to stress. While non-phosphorylation of this residue leads to formation of less-active oligomers, phosphorylation helps to maintain the monomeric status of SIRT1, resulting in increased activity	Mus musculus

Purification (Commentary)

Purification (Comment)	Organism
-	Mus musculus

Synonyms

Synonyms	Comment	Organism
SIRT1	-	Mus musculus

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Release 2023.1 (January 2023)