DGKE is an ATP-dependent lipid kinase that converts diacylglycerol to phosphatidic acid. Its preference for substrates bearing an arachidonoyl chain at sn-2 connects diacylglycerol signaling with phosphatidylinositol recycling. DGKE acts at membrane interfaces and is found in membrane-associated and cytosolic pools. The sn-1 chain preference is more flexible, so stearoyl-arachidonoyl diacylglycerol is not its only efficiently used substrate.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004143 ATP-dependent diacylglycerol kinase activity | EXP PMID:21477596 Study of arachidonoyl specificity in two enzymes of the PI c... | ACCEPT | Summary: DGKE catalyzes ATP-dependent phosphorylation of DAG to PA. Reason: Human FLAG-tagged DGKE wild type and substrate-selectivity mutants expressed in COS-7 cells were assayed in detergent extracts with radiolabeled ATP and mock subtraction. Lipid-dependent PA production supports the assigned reaction. PIP5Kalpha assays in the same paper concern a separate enzyme; the natural 177-residue DGKE product was not tested. Supporting Evidence: |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | EXP PMID:23949095 Evaluations of the selectivities of the diacylglycerol kinas... | ACCEPT | Summary: DGKE catalyzes ATP-dependent phosphorylation of DAG to PA. Reason: The accessible abstract explicitly includes epsilon in a ten-isozyme activity/inhibitor comparison. The full article could not be recovered, so exact species, tags and assay implementation remain unverified here. Retain the curator's basic catalytic assignment because the target-positive abstract and independently read human DGKE phosphorylation experiment in PMID18004883 agree; do not infer a DGKE-specific physiological effect from R59022 inhibition. |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Ancestral DAG kinase activity is retained in human DGKE. Reason: The current PTHR11255 tree places P52429 in the epsilon subfamily below the annotated IBD root PTN007499105. The literal root IBD includes direct human P52429 evidence, which is legitimate descendant grounding rather than circular transfer. Human substrate assays independently support the inherited activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN007499105 SUPPORTS TRANSFER Literal IBD and complete current target lineage inspected in PTHR11255. No inferred loss or circularity; target experimental grounding is legitimate where present. Supporting Evidence: |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | IDA PMID:15544348 The alpha isoform of diacylglycerol kinase exhibits arachido... | ACCEPT | Summary: DGKE catalyzes ATP-dependent phosphorylation of DAG to PA. Reason: Despite its alpha-focused title, the complete abstract explicitly reports epsilon-catalyzed phosphorylation in Triton mixed micelles and epsilon arachidonoyl preference. Full Methods were inaccessible. The target-positive abstract and independently read human DGKE assay in PMID18004883 support retaining this established catalytic assignment without inventing the inaccessible construct details. |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | IDA PMID:18004883 Substrate chirality and specificity of diacylglycerol kinase... | ACCEPT | Summary: DGKE catalyzes ATP-dependent phosphorylation of DAG to PA. Reason: The recovered original expresses human C-terminal 6His DGKE in Sf21 cells and measures radiolabeled ATP incorporation into PA from exogenous DAG. No-enzyme and mock-preparation controls are included. Table 1 and Figure 5 support DAG phosphorylation and stereoselectivity; the detergent extract is not a purified native membrane system. Supporting Evidence: PMID:18004883 degree of stereospecificity in the phosphorylation of diacylglycerol. |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | IDA PMID:19744926 Diacylglycerol kinase epsilon is selective for both acyl cha... | ACCEPT | Summary: DGKE catalyzes ATP-dependent phosphorylation of DAG to PA. Reason: The original tests human full-length and engineered Ξ58 DGKE in COS-7 cells and human His6-DGKE in Sf21 cells. Radiolabeled DAG-to-PA assays use enriched detergent lysates and mock controls, not purified enzyme. These human experiments directly support the reaction; the separate mouse fibroblast lipidomics and natural 177-residue product are distinct. Supporting Evidence: |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | IDA PMID:22108654 Substrate specificity of diacylglycerol kinase-epsilon and t... | ACCEPT | Summary: DGKE catalyzes ATP-dependent phosphorylation of DAG to PA. Reason: Human C-terminal His6-DGKE expressed in Sf21 cells phosphorylates defined DAG species in detergent-extract/mixed-micelle assays. The data support ATP-dependent DAG-to-PA conversion and sn-2 arachidonoyl preference, with broader sn-1 tolerance. The natural 177-residue product was not assayed. Supporting Evidence: |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic mappings agree on DGKE's ATP-dependent DAG kinase reaction. Reason: The literal InterPro mappings for IPR000756/IPR037607 and ARBA00028046 output this activity; the official human record supplies the corresponding EC and Rhea reaction assertions. These mappings agree with target-specific human DAG-to-PA assays. Domain membership is not used to assign activity to the short alternative product. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR000756 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. InterPro:IPR037607 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. ARBA:ARBA00028046 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Supporting Evidence: |
| GO:0004143 ATP-dependent diacylglycerol kinase activity | TAS Reactome:R-HSA-426240 | ACCEPT | Summary: DGKE is an explicit catalyst-set member for DAG phosphorylation. Reason: Reactome 426240βcatalyst426239βdefined set426070βDGKE426061 resolves directly to human P52429 residues 1β567. The modeled activity is ATP-dependent DAG phosphorylation to PA, matching human biochemical evidence; this is a catalyst role, not mere pathway proximity. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:23542698 Recessive mutations in DGKE cause atypical hemolytic-uremic ... | MODIFY | Summary: Human DGKE has a cytosolic pool. Reason: PMID23542698 Figure 4b and Methods detect endogenous DGKE in the cytoplasmic fraction of unstimulated human platelets, with Ξ²-tubulin and Na,K-ATPase fraction controls. Current HPA immunofluorescence independently identifies cytosol. Refine cytoplasm to cytosol using this combined support; the same term already exists in row 11, so this changes specificity without claiming extra coverage. Proposed replacements: cytosol Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Refine the cytoplasm mapping to the supported cytosolic pool. Reason: The UniProt SL-0086 mapping is consistent with the human platelet cytoplasmic fraction and the approved HPA cytosol call in A-431, U-251MG and U2OS. Cytosol is more informative than cytoplasm and already represented by row 11. This does not erase the separately supported membrane-associated pool. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB-SubCell:SL-0086 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Proposed replacements: cytosol Supporting Evidence: |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: HPA supports cytosolic localization in human cells. Reason: The exact ENSG00000153933 HPA record reports approved cytosol/nucleoplasm localization, with supported antibody-based ICC/IF in A-431, U-251MG and U2OS. The source thus supports the existing cytosol annotation. It does not resolve individual natural protein products or establish a cytosolic-only distribution. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-426240 | KEEP AS NON CORE | Summary: Reactome models full-length DGKE at the plasma membrane. Reason: The exact P52429 residues 1β567 member426061 has the plasma-membrane compartment in the DAG-kinase catalyst set. Retain this curated pathway-localization context. The independently read platelet fractionation distinguishes membranes from cytoplasm but not one membrane compartment, so the specific plasma-membrane model is not used as the sole defining location of the enzyme. Supporting Evidence: |
| GO:0006654 phosphatidic acid biosynthetic process | IDA PMID:15544348 The alpha isoform of diacylglycerol kinase exhibits arachido... | ACCEPT | Summary: DGKE directly synthesizes phosphatidic acid from DAG. Reason: Direct phosphorylation of DAG produces PA, so DGKE performs a chemical step of this biosynthetic process rather than merely being required for it. The accessible source abstract explicitly includes epsilon activity, while full Methods remain inaccessible; the independently recovered human experiment in PMID18004883 corroborates PA production. Retain the established curator assignment with this access limit. |
| GO:0006654 phosphatidic acid biosynthetic process | IDA PMID:19744926 Diacylglycerol kinase epsilon is selective for both acyl cha... | ACCEPT | Summary: DGKE directly synthesizes phosphatidic acid from DAG. Reason: Human recombinant DGKE directly phosphorylates DAG to the measured PA product. DGKE therefore performs the biosynthetic step, rather than merely being required for it. The cell-extract assays do not establish activity of the natural 177-residue product; PA product inhibition is a separate kinetic observation. Supporting Evidence: |
| GO:0006654 phosphatidic acid biosynthetic process | IDA PMID:22108654 Substrate specificity of diacylglycerol kinase-epsilon and t... | ACCEPT | Summary: DGKE directly synthesizes phosphatidic acid from DAG. Reason: Human recombinant DGKE directly phosphorylates DAG to the measured PA product. DGKE therefore performs the biosynthetic step, rather than merely being required for it. The cell-extract assays do not establish activity of the natural 177-residue product; PA product inhibition is a separate kinetic observation. Supporting Evidence: |
| GO:0006661 phosphatidylinositol biosynthetic process | IEA GO_REF:0000107 | ACCEPT | Summary: DGKE supplies PA to phosphatidylinositol resynthesis. Reason: The exact mouse donor Q9R1C6 carries IMP evidence from PMID19744926 and matches Ensembl protein ENSMUSP00000000285. Original knockout-MEF lipidomics show altered PI acyl-chain composition; the method does not assign sn positions. Together with direct human DGKE DAG-to-PA activity, this supports conserved upstream participation by producing PA for PI recycling. It does not assert PI synthase chemistry or direct measurement of human PI-synthesis flux. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q9R1C6 Β· Dgke SUPPORTS TRANSFER Official mouse564-aa Dgke record cross-references ENSMUSP00000000285. Exact experimental donor record and original source scope were traced; human interpretation retains the species/context distinction. Supporting Evidence: |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: DGKE regulates intracellular signaling through DAG metabolism. Reason: IPR037607 maps the family to generic signal transduction. Human full-length DGKE and loss-of-function/siRNA experiments alter M3-receptor-evoked TRPC6 currents, supporting intracellular lipid signaling. Refine to intracellular signal transduction, already present in row 28, without claiming an additional pathway or making the current readout a direct DAG measurement. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR037607 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Proposed replacements: intracellular signal transduction Supporting Evidence: |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: DGKE participates in the lipid branch of PLC-linked receptor signaling. Reason: IPR000756 supplies the literal PLC-activating GPCR-pathway mapping. The human M3/TRPC6 experiment supports modulation of receptor-driven DAG signaling, and mouse Dgke deletion alters phosphoinositide signaling and synaptic responses. Retain this pathway context as non-core; DGKE phosphorylates DAG rather than activating PLC itself, and no receptor-general activity is inferred. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: InterPro:IPR000756 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | ACCEPT | Summary: DGKE membrane association is established; retain the curated screen annotation. Reason: The source abstract describes YTS membrane proteomics, but its DGKE-specific peptide/table entry was not recovered. Retain the curatorβs broad membrane assignment because endogenous human platelet fractionation independently establishes DGKE membrane association (PMID23542698), consistent with the other target annotations. This is deference to the curated HDA observation with corroborating target evidence, not a claim that this particular NK-cell table was independently verified or that it identifies a specific membrane compartment. |
| GO:0016020 membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Membrane association is supported by ancestry and target experiments. Reason: The exact membrane IBD is placed at PTN007499105, on the current human DGKE lineage, and includes target experimental evidence among its descendants. Endogenous human platelet membrane fractionation corroborates the inherited association. A unique membrane subcompartment is not established across these sources, so retain the useful general membrane term. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN007499105 SUPPORTS TRANSFER Literal IBD and complete current target lineage inspected in PTHR11255. No inferred loss or circularity; target experimental grounding is legitimate where present. Supporting Evidence: |
| GO:0016020 membrane | IDA PMID:19744926 Diacylglycerol kinase epsilon is selective for both acyl cha... | ACCEPT | Summary: DGKE is associated with membranes used in its lipid reaction. Reason: The source treats DGKE as a membrane-associated interfacial enzyme and tests detergent-extracted human full-length and engineered Ξ58 proteins. Those preparations alone do not locate native DGKE. Curated-source interpretation and the independent endogenous human platelet membrane fractionation support the broad membrane annotation without naming an untested organelle or transferring deletion-construct behavior to the natural short product. |
| GO:0016020 membrane | IDA PMID:23542698 Recessive mutations in DGKE cause atypical hemolytic-uremic ... | ACCEPT | Summary: Endogenous human DGKE is detected in a membrane fraction. Reason: Figure 4b and Methods directly identify DGKE in membrane and cytoplasmic fractions of unstimulated human platelets, with Na,K-ATPase and Ξ²-tubulin controls. Membrane is the appropriate scope of this experiment; it does not separately distinguish plasma membrane from intracellular membranes. Supporting Evidence: |
| GO:0016020 membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The electronic membrane mapping agrees with direct localization. Reason: UniProt SL-0162 maps to membrane and is independently supported by human platelet fractionation. This describes association with a lipid bilayer, not a fully established transmembrane topology or a specific organelle. Retain the term at the experimentally warranted scope. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0162 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Supporting Evidence: |
| GO:0016301 kinase activity | IDA PMID:18004883 Substrate chirality and specificity of diacylglycerol kinase... | MODIFY | Summary: The source directly supports DAG kinase activity. Reason: The recovered original uses human C-terminal 6His DGKE, exogenous DAG and radiolabeled ATP, and measures PA formation with no-enzyme/mock controls. Replace generic kinase activity with ATP-dependent diacylglycerol kinase activity. The same source already provides this specific term in row 4; no additional biological coverage or protein-kinase activity is claimed. Proposed replacements: ATP-dependent diacylglycerol kinase activity Supporting Evidence: |
| GO:0016301 kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: Refine the broad catalytic-domain mapping to DAG kinase activity. Reason: IPR001206 occurs in several lipid kinase families and maps only to generic kinase activity. Exact human DGKE identity and direct target assays establish the more specific ATP-dependent DAG kinase reaction. This refinement uses target evidence, not an assumption that every domain-containing protein has the same substrate; the specific term is already represented. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR001206 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Proposed replacements: ATP-dependent diacylglycerol kinase activity Supporting Evidence: |
| GO:0030168 platelet activation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Platelet activation is a contextual electronic pathway assignment. Reason: ARBA00027406 includes a primate+DGK accessory/catalytic-domain condition and outputs platelet activation. Human platelets express DGKE, and Reactome places the exact protein in the DAG-removal reaction within platelet signaling. Retain this physiological context as non-core. The cited human disease study proposes a thrombosis mechanism and uses prior nonselective-inhibitor observations; it does not establish a DGKE-specific platelet-activation mechanism. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00027406 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Supporting Evidence: |
| GO:0030168 platelet activation | TAS Reactome:R-HSA-76002 | KEEP AS NON CORE | Summary: Reactome places DGKE-mediated DAG metabolism in platelet signaling. Reason: The exact source path is 76002β114508β426240βcatalyst426239βset426070βP52429 member426061. Thus DGKE performs a modeled lipid-metabolic step in the pathway, rather than merely appearing in an expression list. Keep the platelet context non-core, with no claim that DGKE directly triggers aggregation or that a selective DGKE platelet-perturbation experiment was performed. Supporting Evidence: |
| GO:0035556 intracellular signal transduction | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Ancestral intracellular lipid-signaling participation is defensible. Reason: The literal PTN007499105 IBD for intracellular signal transduction is on the target lineage. Its descendant evidence includes DGKZ, DGKK, DGKH and a Dictyostelium source; the donor count does not determine validity. Human DGKE perturbation in receptor-driven TRPC6 assays independently supports intracellular signaling context. Retain this contextual output without transferring any donor-specific RAF/RAS or immune pathway to DGKE. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN007499105 SUPPORTS TRANSFER Literal IBD and complete current target lineage inspected in PTHR11255. No inferred loss or circularity; target experimental grounding is legitimate where present. Supporting Evidence: |
| GO:0046339 diacylglycerol metabolic process | IDA PMID:15544348 The alpha isoform of diacylglycerol kinase exhibits arachido... | ACCEPT | Summary: DGKE directly metabolizes diacylglycerol. Reason: DGKE directly consumes DAG as the phosphate acceptor in PA production, making DAG metabolism a faithful description of the reaction. The complete abstract explicitly assays epsilon despite the alpha-focused title; full Methods remain inaccessible. Independent human assays in PMID18004883 corroborate the substrate-specific chemistry, so retain the curator assignment with that limit. |
| GO:0046339 diacylglycerol metabolic process | IDA PMID:19744926 Diacylglycerol kinase epsilon is selective for both acyl cha... | ACCEPT | Summary: DGKE directly metabolizes diacylglycerol. Reason: Human recombinant DGKE directly consumes DAG as the phosphate acceptor in PA production, making DAG metabolism a faithful description of the reaction. The controlled substrate assays support this process without implying every DAG-metabolic route or activity of the natural 177-residue product. Supporting Evidence: |
| GO:0046339 diacylglycerol metabolic process | IDA PMID:22108654 Substrate specificity of diacylglycerol kinase-epsilon and t... | ACCEPT | Summary: DGKE directly metabolizes diacylglycerol. Reason: Human recombinant DGKE directly consumes DAG as the phosphate acceptor in PA production, making DAG metabolism a faithful description of the reaction. The controlled substrate assays support this process without implying every DAG-metabolic route or activity of the natural 177-residue product. Supporting Evidence: |
| GO:0046474 glycerophospholipid biosynthetic process | IEA GO_REF:0000117 | MODIFY | Summary: PA biosynthesis is the demonstrated glycerophospholipid-synthesis step. Reason: The current ARBA00028351 record outputs the broad glycerophospholipid biosynthetic term; its exact present-day DGKE-matching condition was not resolved. Independent target assays nevertheless establish synthesis of PA directly from DAG. Refine to phosphatidic acid biosynthetic process, already represented by rows 13β15, without claiming synthesis of every glycerophospholipid or inventing a historical rule condition. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: ARBA:ARBA00028351 UNRESOLVED Current output0046474 verified, exact current target-matching condition unresolved; target chemistry independently resolves specificity. Proposed replacements: phosphatidic acid biosynthetic process Supporting Evidence: |
| GO:0046486 glycerolipid metabolic process | IBA GO_REF:0000033 | MODIFY | Summary: Refine inherited glycerolipid metabolism to the direct DAG reaction. Reason: The glycerolipid-metabolism IBD at PTN007499105 is validly inherited by the human epsilon lineage, with legitimate target descendant evidence. Direct human assays identify DAG as substrate and PA as product, supporting diacylglycerol metabolic process as a more informative description. That term already exists in rows 29β31; this is specificity refinement, not rejection of the ancestral function. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN007499105 SUPPORTS TRANSFER Literal IBD and complete current target lineage inspected in PTHR11255. No inferred loss or circularity; target experimental grounding is legitimate where present. Proposed replacements: diacylglycerol metabolic process Supporting Evidence: |
| GO:0046486 glycerolipid metabolic process | IEA GO_REF:0000041 | MODIFY | Summary: Refine the UniPathway glycerolipid label to DAG metabolism. Reason: The official P52429 pathway statement supplies UniPathway UPA00230 glycerolipid metabolism. Human target assays establish the direct DAG-to-PA reaction, supporting the more precise diacylglycerol metabolic process already represented in the review. No additional glycerolipid reaction is inferred from the broad pathway label. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniPathway:UPA00230 SUPPORTS TRANSFER Literal mapping/official source inspected; interpretation is constrained by target identity and the source-specific biological evidence described above. Proposed replacements: diacylglycerol metabolic process Supporting Evidence: |
| GO:0046834 lipid phosphorylation | IDA PMID:15544348 The alpha isoform of diacylglycerol kinase exhibits arachido... | ACCEPT | Summary: DGKE phosphorylates a lipid substrate. Reason: Transfer of the ATP phosphate to DAG directly performs lipid phosphorylation. This process term describes the reaction class, while the paired DAG-metabolism and PA-biosynthesis annotations specify its substrate and product; it does not imply protein phosphorylation. The source abstract explicitly includes epsilon; full Methods remain unavailable, but the independently read human assay in PMID18004883 corroborates this established chemistry. |
| GO:0046834 lipid phosphorylation | IDA PMID:18004883 Substrate chirality and specificity of diacylglycerol kinase... | ACCEPT | Summary: DGKE phosphorylates a lipid substrate. Reason: Transfer of the ATP phosphate to DAG directly performs lipid phosphorylation. This process term describes the reaction class, while the paired DAG-metabolism and PA-biosynthesis annotations specify its substrate and product; it does not imply protein phosphorylation. The recovered original directly measures radiolabeled phosphate incorporation into PA with substrate and mock controls. Supporting Evidence: |
| GO:0046834 lipid phosphorylation | IDA PMID:19744926 Diacylglycerol kinase epsilon is selective for both acyl cha... | ACCEPT | Summary: DGKE phosphorylates a lipid substrate. Reason: Transfer of phosphate from ATP to DAG directly performs lipid phosphorylation in the source human-construct assays. This term captures the demonstrated reaction class, while DAG-metabolism and PA-biosynthesis annotations specify substrate and product. It does not imply protein phosphorylation or a separate catalytic unit. The saved typed ontology does not make lipid phosphorylation an ancestor of PA biosynthesis. Supporting Evidence: |
| GO:0046834 lipid phosphorylation | IDA PMID:22108654 Substrate specificity of diacylglycerol kinase-epsilon and t... | ACCEPT | Summary: DGKE phosphorylates a lipid substrate. Reason: Transfer of phosphate from ATP to DAG directly performs lipid phosphorylation in the source human-construct assays. This term captures the demonstrated reaction class, while DAG-metabolism and PA-biosynthesis annotations specify substrate and product. It does not imply protein phosphorylation or a separate catalytic unit. The saved typed ontology does not make lipid phosphorylation an ancestor of PA biosynthesis. Supporting Evidence: |
| GO:0050804 modulation of chemical synaptic transmission | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse synaptic modulation supports a conserved neuronal context. Reason: The exact Q9R1C6/ENSMUSP00000000285 donor carries SynGO IDA/IMP evidence from PMID11287665. The recovered original shows reduced high-frequency-stimulation-induced EPSP potentiation in Dgke-knockout perforant pathβdentate granule-cell synapses, with basic membrane properties preserved. Retain this orthology-based neuronal consequence as non-core; it is not a direct human synaptic assay and does not establish a new catalytic function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q9R1C6 Β· Dgke SUPPORTS TRANSFER Official mouse564-aa Dgke record cross-references ENSMUSP00000000285. Exact experimental donor record and original source scope were traced; human interpretation retains the species/context distinction. Supporting Evidence: |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The synaptic annotation reflects functional activity in a glutamatergic circuit. Reason: The source donor uses the same mouse knockout/electrophysiology study as the synaptic-modulation annotation, with SynGO glutamatergic-synapse context. The original supports function in perforant pathβdentate granule-cell signaling; it does not image DGKE protein in a presynaptic or postsynaptic compartment. Preserve the original is_active_in relation and contextual annotation without converting it to a demonstrated human physical localization. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q9R1C6 Β· Dgke SUPPORTS TRANSFER Official mouse564-aa Dgke record cross-references ENSMUSP00000000285. Exact experimental donor record and original source scope were traced; human interpretation retains the species/context distinction. Supporting Evidence: |
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Q: Which native membrane pools carry the physiologically relevant DGKE activity during phosphatidylinositol recycling? Platelet fractionation establishes membrane association without resolving an organelle or membrane face.
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