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
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine.
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Purified recombinant human AGXT2L1 (ETNPPL) degrades phosphoethanolamine to ammonia, inorganic phosphate and acetaldehyde.
"AGXT2L1 catalyzed a similar reaction on phosphoethanolamine, converting it to ammonia, inorganic phosphate, and acetaldehyde."
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AGXT2L1 does not act as a transaminase despite homology to AGXT2.
"Unlike AGXT2, AGXT2L1 and AGXT2L2 did not act as transaminases"
Strict reaction and substrate specificity of AGXT2L1, the human O-phosphoethanolamine phospho-lyase.
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Human ETNPPL is at least 500-fold more active as a lyase than as an aminotransferase and strongly selective for O-phosphoethanolamine.
"is at least 500-fold more active as a lyase than as an aminotransferase"
Kinetic characterization of the human O-phosphoethanolamine phospho-lyase reveals unconventional features of this specialized pyridoxal phosphate-dependent lyase.
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The active site is optimized for dianionic groups, a main determinant of specificity for phosphoethanolamine.
"the active site of PEA phospho-lyase is optimized to bind dianionic groups and that this is a prime determinant of the enzyme specificity towards PEA"
Structural Basis for Phospholyase Activity of a Class III Transaminase Homologue.
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Bacterial class-III homologue A1RDF1 has phosphoethanolamine phospho-lyase activity and no transaminase activity; its structure served as the model for the human enzyme.
"Activity screening revealed that the enzyme possesses phospholyase (E.C. 4.2.3.2) activity towards O-phosphoethanolamine (PEtN)"
Structural characterization of human O-phosphoethanolamine phospho-lyase.
The role of ethanolamine phosphate phospholyase in regulation of astrocyte lipid homeostasis.
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Etnppl is an astrocyte-specific, fasting-induced gene in mouse brain.
"ethanolamine phosphate phospholyase (Etnppl) was identified as an astrocyte-specific fasting-induced gene"
Utilization of ethanolamine phosphate phospholyase as a unique astrocytic marker.
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ETNPPL protein is predominantly nuclear in adult mouse brain astrocytes, shown with knockout-validated monoclonal antibodies.
"In the mouse brain, we observed that ETNPPL was predominantly localized in the cell nuclei"
Transformation Foci in IDH1-mutated Gliomas Show STAT3 Phosphorylation and Downregulate the Metabolic Enzyme ETNPPL, a Negative Regulator of Glioma Growth.
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ETNPPL is detected in the cytoplasm or nucleus of astrocytes in human cortex and in glioma cells.
"ETNPPL is detected in the cytoplasm (yellow arrow) or the nucleus (red arrow)."
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Overexpression of ETNPPL reduces glioma stem cell growth.
"Overexpression of ETNPPL reduces the growth of glioma stem cells"
The emerging role of ethanolamine phosphate phospholyase in regulating hepatic phosphatidylethanolamine and plasma lipoprotein metabolism in mice.
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Etnppl-null mouse hepatocytes convert more ethanolamine to phosphoethanolamine and PE.
"Primary hepatocytes isolated from Etnppl-/- mice showed increased conversion of [3H]ethanolamine to [3H]p-ETN and [3H]PE compared to Etnppl+/+ mice."
Female ethanolamine phosphate phospholyase knockout mice resisted high-fat diet-induced obesity with attenuated hepatic cholesterol deposition.
Alterations in phosphatidylethanolamine metabolism impacts hepatocellular lipid storage, energy homeostasis, and proliferation.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
PXLP-K278-ETNPPL tetramer hydrolyses PETA
UniProt record Q8TBG4 (ETNPPL_HUMAN)