Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Identification and characterization of a human mitochondrial NAD kinase.
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Purified NADK2 (C5orf33) phosphorylates NAD+ with ATP or polyphosphate; its NADH kinase activity is about 10% of the NAD+ kinase activity.
"the NADHK activity of C5orf33 protein was only 10% of its NADK activity"
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NADK2 is mitochondrial, and its N-terminal 62 residues are a functional targeting sequence.
"confirming that C5orf33 protein is a mitochondrial NADK, and that its N-terminal 62 residues contain a functional mitochondrial-targeting sequence"
MNADK, a novel liver-enriched mitochondrion-localized NAD kinase.
Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes dienoyl-CoA reductase deficiency with hyperlysinemia.
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NADK2 loss of function lowers mitochondrial NADP(H) and impairs NADP-dependent DECR and the first step of lysine degradation.
"DECR and also the first step in lysine degradation are performed by NADP-dependent oxidoreductases explaining their in vivo deficiency"
Deficiency of the Mitochondrial NAD Kinase Causes Stress-Induced Hepatic Steatosis in Mice.
Mitochondrial NADP(+) is essential for proline biosynthesis during cell growth.
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NADK2 deletion makes cells proline auxotrophs, because P5C formation by P5CS needs mitochondrial NADPH.
"suggesting that the generation of P5C through P5CS is the bottleneck step that requires mitochondrial NADPH and NADK2 activity"
Mitochondrial NADP(H) generation is essential for proline biosynthesis.
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NADK2 deletion did not change folate pathway, TCA cycle activity or mitochondrial oxidative stress, but blocked proline synthesis.
"Deletion of NADK2 in human cell lines did not alter mitochondrial folate pathway activity"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Structure of human NADK2 reveals atypical assembly and regulation of NAD kinases from animal mitochondria.
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NADK2 is a constitutively active, noncooperative homodimer; the catalytic Asp161 sits in the GGDG motif.
"The GGDG sequence motif bearing the catalytic side chain (D161 in human NADK2) is found in the expected position"
Crystal structure of human NADK2 reveals a dimeric organization and active site occlusion by lysine acetylation.
NADK2 dimer phosphorylates NAD+ to NADP+
LONP1 degrades mitochondrial matrix proteins
LONP1 binds mitochondrial matrix proteins
UniProt entry Q4G0N4 (human NADK2)