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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis.
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Reports identification and 1.9 A X-ray structures of human NMNAT3 (hsPNAT-3) in apo, substrate- and product-bound forms; localizes the enzyme to cytoplasm and mitochondria; the active enzyme is a homotetramer.
"human PNAT (hsPNAT-3) that is located in the cytoplasm and mitochondria"
Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms.
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NMNAT3 is localized to the mitochondria (NMNAT1 nuclear, NMNAT2 Golgi) and exhibits high tolerance toward substrate modifications; the three isoforms have differential catalytic properties.
"whereas NMNAT2 and -3 were localized to the Golgi complex and the mitochondria, respectively"
Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis.
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Determines initial-rate kinetics of the three human NMNAT isozymes; mitochondrial NMNAT3 has a distinctive substrate binding order and uniquely uses ITP efficiently in place of ATP.
"the opposite order is observed with the mitochondrial isozyme NMNAT3. Only the latter utilizes ITP efficiently in place of ATP"
NAD synthase NMNAT acts as a chaperone to protect against neurodegeneration.
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Demonstrates that NMNAT (in Drosophila) has a chaperone function in biochemical assays and cultured cells and shares structural similarity with known chaperones; the human NMNAT3 chaperone/protein-folding GO annotations derive from this family-level activity rather than a direct human NMNAT3 assay.
"NMNAT displays chaperone function both in biochemical assays and"
Alternative splicing of Drosophila Nmnat functions as a switch to enhance neuroprotection under stress.
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Primarily a study of Drosophila Nmnat splice variants; mentions that two splice variants of human NMNAT3 have been experimentally identified. Cited on a human NMNAT3 NMNAT-activity annotation, which is correct on other grounds.
"two splice variants of human NMNAT3 (v1 and V3-FKSG76) have"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
NMNAT3 transfers an adenylyl group from ATP to NAMN to yield NAAD
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Reactome reaction in which NMNAT3 adenylylates nicotinate D-ribonucleotide (NaMN) with ATP to yield deamido-NAD+ (NaAD) and pyrophosphate in the mitochondrial matrix; the active enzyme is a tetramer.
"NMNAT3 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form"