isoform NMNAT2 localizes to the cis-Golgi and endoplasmic reticulum-Golgi intermediate compartment. It is palmitoylated at two adjacent cysteine residues of its isoform-specific domain and thereby anchored at the cytoplasmic surface
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm
generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells
generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells
generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells
generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
mutation R232Q in one allele plus a single duplication of a cytosine at position 403 in exon 5 resulting in a frameshift and premature stop after 44 amino acids lead to a loss of NMNAT2 function, identified in fetus with akinesia deformation sequence, severely reduced skeletal muscle mass and hydrops fetalis
loss of function mutations in two stillborn siblings lead to fetal akinesia deformation sequence, severely reduced skeletal muscle mass and hydrops fetalis. Both protein variants are incapable of supporting axon survival in mouse primary neuron cultures when overexpressed. Variants display altered protein stability and/or defects in NAD+ synthesis and chaperone functions
Severe biallelic loss-of-function mutations in nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) in two fetuses with fetal akinesia deformation sequence
Homology modeling of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 Insights into isoenzyme-specific differences using molecular docking simulatons