Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry GNMT_HUMAN (Q14749)
Effect of naturally occurring mutations in human glycine N-methyltransferase on activity and conformation.
Glycine N -methyltransferase deficiency: a new patient with a novel mutation.
Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.
Towards a proteome-scale map of the human protein-protein interaction network.
Destabilization of human glycine N-methyltransferase by H176N mutation.
Toward an understanding of the protein interaction network of the human liver.
A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers.
GNMT tetramer transfers methyl group from AdoMet to Gly to form AdoHyc and SARC
Affinage mechanistic annotation for GNMT (human)
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GNMT is a homotetrameric SAM-dependent methyltransferase that transfers a methyl group from SAM to glycine to produce sarcosine and SAH, serving as a regulatory node for the cellular SAM:SAH ratio under feedback inhibition by 5-methyltetrahydrofolate pentaglutamate.
"GNMT catalyzes methyl group transfer from S-adenosylmethionine (SAM) to glycine, producing S-adenosylhomocysteine (SAH) and sarcosine (N-methylglycine). The enzyme is inhibited by 5-methyltetrahydrofolate pentaglutamate, functioning as a regulatory enzyme controlling the SAM:SAH ratio."
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Through control of one-carbon flux, GNMT increases hepatic folate retention, supports folate-dependent homocysteine remethylation via methionine synthase, and supports folate-dependent purine/pyrimidine synthesis.
"Through this control of one-carbon flux, GNMT increases hepatic folate retention and folate-dependent homocysteine remethylation via methionine synthase"