2.3.1.B41	D63H	naturally occuring mutation in SIRT6, the homozygous inactivating mutation of histone deacetylase SIRT6 results in severe congenital anomalies and perinatal lethality in four affected fetuses, it causes human perinatal lethality, missense mutation SIRT6 p.D63H in affected fetal amniocytes. SIRT6 D63H mutant mESCs fail to form EBs and retain pluripotent gene expression. The amino acid change at Asp63 to a histidine results in virtually complete loss of H3K9 deacetylase and demyristoylase functions. Asp63 is located in the NAD+-binding pocket, forming hydrogen bonds with neighboring amino acids and thus providing structure to the NAD+-binding loop	756879	
2.3.1.B41	D63H	naturally occuring mutation in SIRT6, the homozygous inactivating mutation of histone deacetylase SIRT6. Asp63 is located in the NAD+-binding pocket, forming hydrogen bonds with neighboring amino acids and thus providing structure to the NAD+-binding loop	756879	
2.3.1.B41	G60A	inactive	737946	
2.3.1.B41	G60A	the mutant is a lysine defatty acylase in vitro with substantially decreased deacetylase activity in vitro and no detectable deacetylase activity in cells	739139	
2.3.1.B41	G60A	the SIRT6 G60A mutant retains an efficient defatty-acylase activity, but has significantly decreased deacetylase activity	757667	
2.3.1.B41	H131Y	the mutant enzyme can still bind NAD+ but has a decreased ability to bind ADP-ribose	729972	
2.3.1.B41	H133Y	a catalytically inactive mutant of SIRT6, the acetylation level of PER2 is significantly increased in SIRT6-KO HEK293 cells compared to wild-type	755978	
2.3.1.B41	H133Y	catalytically inactive SIRT6 mutant, the SIRT6 H133Y mutant without histone deacetylase activity fails to inhibit phosphorylation and nuclear translocation of Smad2	757294	
2.3.1.B41	H133Y	inactive	739139, 739158	
2.3.1.B41	H133Y	inactive enzyme mutant	756407