Literature summary for 2.3.1.B41 extracted from

Gao, Y.; Tan, J.; Jin, J.; Ma, H.; Chen, X.; Leger, B.; Xu, J.; Spagnol, S.; Dahl, K.; Levine, A.; Liu, Y.; Lan, L.
SIRT6 facilitates directional telomere movement upon oxidative damage (2018), Sci. Rep., 8, 5407 .

Search for more literature for 2.3.1.B41

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of SIRT6 knockout MEF cells which exhibit an increased basal level of mobility compared to that in wild-type cells before damage. But the cells do not show the damage-induced increase in total movement after damage	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chromatin	-	Homo sapiens	785	-
nucleus	-	Homo sapiens	5634	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q8N6T7	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
MEF cell	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
More	cf. EC 2.3.1.286	Homo sapiens
SIRT6	-	Homo sapiens
sirtuin 6	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	SIRT6 knockout (KO) cells show neither damage-induced telomere movement nor chromatin decondensation at damaged telomeres, while both are observed in wild-type cells. A Deacetylation mutant of SIRT6 increases damage-induced telomeric movement in SIRT6 KO cells as well as wild-type SIRT6	Homo sapiens
metabolism	telomere stability, movement, and chromosomal condensation are regulated by SIRT6 in the presence of oxidative damage at telomeres	Homo sapiens
physiological function	SIRT6 facilitates directional telomere movement upon oxidative damage. Oxidative damage at telomeres triggers directional telomere movement. The presence of the human Sir2 homologue, sirtuin 6 (SIRT6) is required for oxidative damage-induced telomeric movement. SIRT6 recruits the chromatin-remodeling protein SNF2H to damaged telomeres, which appears to promote chromatin decondensation independent of its deacetylase activity. SIRT6 is critical for directional movement in DNA damage repair. SIRT6 increases the short-term telomere mobility in response to telomere-specific oxidative damage. SIRT6 cooperates with SNF2H in the regulation of telomere chromatin structure, overview	Homo sapiens

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Release 2023.1 (January 2023)