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
Combined Automated Annotation using Multiple IEA Methods
Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-beta forming a phosphohistidine enzyme intermediate during catalysis.
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G6Pase-beta is a nine-transmembrane ER protein that forms a covalent phosphoryl enzyme intermediate during G6P hydrolysis; the phosphate acceptor is His167, lying in the ER lumen with active-site residues Arg79 and His114.
"we demonstrated that the phosphate acceptor in Glc-6-Pase-beta is His(167) and that it lies inside the ER lumen with the active site residues, Arg(79) and His(114)."
Defining the membrane proteome of NK cells.
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Large-scale membrane-proteome MS survey of an NK-like cell line that identified G6PC3 among 1843 high-confidence proteins; the source of the generic HDA "membrane" annotation.
"spectrometric analysis identified 1843 proteins with high confidence scores."
Functional analysis of mutations in a severe congenital neutropenia syndrome caused by glucose-6-phosphatase-β deficiency.
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G6PC3 (G6Pase-beta) is an ER-membrane enzyme that hydrolyses G6P to glucose and phosphate; functional analysis of SCN4 missense mutations shows 14 of 16 completely abolish enzymatic activity, establishing the core function and disease mechanism.
"Fourteen missense mutations completely abolish G6Pase-β enzymatic activity while the p.S139I and p.R189Q mutations retain 49% and 45%, respectively of wild type G6Pase-β activity."
G6PC3 hydrolyzes G6P to form Glc and Pi (ubiquitous)
Defective G6PC3 does not hydrolyze glucose 6-phosphate