DPAGT1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: Conserved, directly corroborated GlcNAc-1-phosphate transferase activity. Reason: The literal PAINT IBD at PTN000060284 places GO:0003975 at the eukaryotic ancestor; the human Q9H3H5 leaf descends from that node. Human experimental annotations among the descendants are legitimate grounding, not circularity. Independent purified full-length human substrate/product assays establish the same Dol-P-acceptor reaction. No evidence of target-specific loss challenges the placement. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: PMID:29459785 catalyzes the first and committed step of N-linked glycosylation on the cytosolic face of endoplasmic reticulum (ER) membrane PMID:30388443 It catalyzes the transfer of an N-acetyl-D-glucosamine-1-phosphoryl unit (GlcNAc-1-P) from UDP-N-acetyl glucosamine (UDP-GlcNAc) onto dolichyl phosphate (Dol-P)
GO:0016020 membrane	IBA GO_REF:0000033	MODIFY	Summary: Membrane localization is valid but can be specified to the ER membrane. Reason: The PAINT membrane assertion is inherited through the verified target path from PTN000060284. Human ten-pass architecture, curated ER localization and reaction context justify the more informative ER-membrane term. This refines the target localization without rejecting the ancestral membrane judgment or claiming every donor assay resolved the ER. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:29459785 catalyzes the first and committed step of N-linked glycosylation on the cytosolic face of endoplasmic reticulum (ER) membrane file:human/DPAGT1/DPAGT1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Electronic annotation matches the established Dol-P phosphotransferase reaction. Reason: Current official EC 2.7.8.15/Rhea:13289 chemistry uses UDP-GlcNAc and dolichyl phosphate to form GlcNAc-PP-dolichol and UMP; the genuine current mapping and human biochemical assays agree. This does not imply the differently named lysosomal-enzyme phosphotransferase activity. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt transferring GlcNAc-1-P from
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000044	ACCEPT	Summary: The curated subcellular-location mapping correctly specifies ER membrane. Reason: The UniProt location mapping is corroborated by the multispanning human protein and the ER-membrane catalytic context. The cytoplasmic orientation of the active site does not make the entire polytopic protein a soluble cytosolic enzyme. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum PMID:29459785 hGPT crystallized as a homodimer with one tunicamycin molecule bound to the active site of each protomer near the cytosolic side of the ER membrane
GO:0006488 dolichol-linked oligosaccharide biosynthetic process	IEA GO_REF:0000002	ACCEPT	Summary: The InterPro family mapping correctly assigns the performed LLO-synthesis step. Reason: IPR033895 currently maps to GO:0006488 and GO:0003975, and the target carries this family. DPAGT1 itself catalyzes formation of the first lipid-linked GlcNAc intermediate, so participation is supported by a performed chemical step rather than merely a requirement for the eventual glycoprotein product. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: PMID:30388443 The product GlcNAc-PP-Dol is anchored to the ER membrane by its dolichyl moiety
GO:0016020 membrane	IEA GO_REF:0000120	MODIFY	Summary: The historical electronic membrane assertion remains biologically correct but broad. Reason: The membrane claim is supported; ER membrane is the specific target location. Its absence as this GO_REF:0000120 identity in the current snapshot is a source-lifecycle change, not evidence that membrane localization is false. The current membrane mapping is retained separately with its genuine source identity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt Multi-pass membrane protein
GO:0016780 phosphotransferase activity, for other substituted phosphate groups	IEA GO_REF:0000002	MODIFY	Summary: The broad phosphotransferase class can be refined to the measured reaction. Reason: IPR000715 covers polyisoprenol-phosphate phosphotransferases, including bacterial reactions as well as eukaryotic GPT. For human DPAGT1, the defined Dol-P/UDP-GlcNAc reaction and the target-specific IPR033895 family support GO:0003975, an is_a descendant of GO:0016780. No bacterial substrate chemistry is assigned to the human protein. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity Supporting Evidence: PMID:30388443 It catalyzes the transfer of an N-acetyl-D-glucosamine-1-phosphoryl unit (GlcNAc-1-P) from UDP-N-acetyl glucosamine (UDP-GlcNAc) onto dolichyl phosphate (Dol-P)
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	KEEP AS NON CORE	Summary: Retain the positive HTT interaction under its tested binary-screen scope. Reason: Three literal IntAct records for PMID:32814053 link human HTT and DPAGT1 by array, pooling and validated yeast two-hybrid assays. They annotate an HTT 1–546 sufficient-binding region and repeat-region modifications; these participant features are separate from the parent sequence identifiers. The original screen uses non-autoactivating baits and growth/reporters. This is positive binding evidence, not a false interaction merely because the term is generic. Native ER contact, a physiological regulatory role and recognition of a narrower partner functional class are not established by these assays; retain the existing interaction as non-core. Supporting Evidence: PMID:32814053 It facilitates the identification of interacting proteins that significantly influence mutant TDP-43 and HTT toxicity in transgenic flies file:human/DPAGT1/DPAGT1-uniprot.txt Q9H3H5; P42858: HTT; NbExp=3
GO:0006488 dolichol-linked oligosaccharide biosynthetic process	TAS Reactome:R-HSA-446193	ACCEPT	Summary: Reactome correctly places DPAGT1 in LLO biosynthesis. Reason: The curated LLO pathway contains the DPAGT1-catalyzed first reaction; GO-CAM 65c57c3400000687 independently models Q9H3H5 enabling GO:0003975 as part of GO:0006488. DPAGT1 performs the first chemical transfer, while downstream enzymes extend the glycan and oligosaccharyltransferase transfers it to protein. Supporting Evidence: PMID:30388443 The product GlcNAc-PP-Dol is anchored to the ER membrane by its dolichyl moiety and then monosaccharide units are added sequentially to build the N-glycan that is then transferred
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	TAS Reactome:R-HSA-446191	ACCEPT	Summary: The normal Reactome event encodes the correct catalytic reaction. Reason: R-HSA-446191 identifies DPAGT1 as catalyst for UDP-GlcNAc plus Dol-P conversion to GlcNAc-PP-Dol and UMP. Its reaction context and independent direct human assays support the molecular function. The precise phosphotransfer reaction is used here without adopting an imprecise glycosidic-linkage shorthand from the summary. Supporting Evidence: PMID:29459785 This reaction involves the transfer of N-acetylglucosamine-1-phosphate (GlcNAc-1-P) from UDP-N-acetylglucosamine (UDP-GlcNAc) to the carrier lipid dolichyl-phosphate (Dol-P).
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	TAS Reactome:R-HSA-4549334	ACCEPT	Summary: The disease-event source identifies the same normal DPAGT1 activity. Reason: R-HSA-4549334 is a defective-mutant event explicitly linked to normal reaction R-HSA-446191. It supports the identity of the disrupted normal enzyme activity, not a claim that every disease variant is catalytically null. In particular, PMID:30388443 reports increased purified rates for some variants together with exon-trap splicing abnormalities; these are distinct mechanisms. Supporting Evidence: PMID:29459785 This reaction involves the transfer of N-acetylglucosamine-1-phosphate (GlcNAc-1-P) from UDP-N-acetylglucosamine (UDP-GlcNAc) to the carrier lipid dolichyl-phosphate (Dol-P).
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	EXP PMID:30388443 Structures of DPAGT1 Explain Glycosylation Disease Mechanism...	ACCEPT	Summary: Purified human DPAGT1 directly catalyzes GlcNAc-1-phosphate transfer to Dol-P. Reason: PMID:30388443 assays full-length human DPAGT1 produced in Sf9 cells, with direct product/TLC and mass-spectrometric evidence and kinetic analyses. Sf9 is the expression host, not the protein species. The resolved 7–400 structural model is not a naturally shortened product, and variant splicing or rate measurements are not generalized to all isoforms. Supporting Evidence: PMID:30388443 It catalyzes the transfer of an N-acetyl-D-glucosamine-1-phosphoryl unit (GlcNAc-1-P) from UDP-N-acetyl glucosamine (UDP-GlcNAc) onto dolichyl phosphate (Dol-P)
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	EXP PMID:9451016 Cloning and functional expression of the human GlcNAc-1-P tr...	ACCEPT	Summary: Human cDNA complementation and membrane biochemistry support GPT activity. Reason: The accessible original abstract reports a human lung-fibroblast clone complementing conditional yeast GPT deficiency and isolated-membrane synthesis of GlcNAc- and GlcNAc2-PP-Dol, stimulated by Dol-P and inhibited by tunicamycin. The deposited CAB04787.1/Z82022.1 clone is 400 aa and matches current product2 boundaries with a documented L25 versus canonical R33 conflict. Full article access was unsuccessful; no unseen assay detail or direct DPAGT1 catalysis of the second GlcNAc addition is inferred. Supporting Evidence: PMID:9451016 GlcNAc2-PP-Dolichol biosynthesis could be shown with isolated S.cerevisiae PMID:9451016 the enzyme for the committed step of the dolichol cycle
GO:0005789 endoplasmic reticulum membrane	ISS GO_REF:0000024	ACCEPT	Summary: Ortholog-derived ER localization agrees with independent human evidence. Reason: The normal fetched context identifies hamster P23338 for this historical ISS assertion. Official source annotation and the conserved membrane enzyme support transfer; human structural/biochemical and curated reaction evidence independently corroborate ER-membrane localization. The historical source dictionary lacks donor fields and is preserved as such, with the recovered donor context recorded separately. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum PMID:8940049
GO:0042802 identical protein binding	ISS GO_REF:0000024	MODIFY	Summary: Self-association can be specified as homodimerization. Reason: The original ISS self-binding claim is positively corroborated by human dimer structures and solution/biophysical evidence in the two 2018 studies. GO:0042803 specifically describes binding an identical protein to form a homodimer and is an is_a child of GO:0042802. The reports disagree on a Cys106 intersubunit disulfide, with PMID:30388443 favoring a predominantly noncovalent dimer; the refinement asserts dimerization, not an obligatory covalent interface or a separate catalytic function. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: protein homodimerization activity Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt SUBUNIT: Homodimer. PMID:29459785 hGPT crystallized as a homodimer with one tunicamycin molecule bound to the active site of each protomer near the cytosolic side of the ER membrane PMID:30388443
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	IDA PMID:29459785 GlcNAc-1-P-transferase-tunicamycin complex structure reveals...	ACCEPT	Summary: Direct human enzyme assays support the defining phosphotransferase activity. Reason: PMID:29459785 expresses full-length 408-aa human GPT in Sf9 cells and measures radiolabeled GlcNAc-1-phosphate transfer to dolichyl phosphate with product TLC. The structural and inhibition experiments complement this direct reaction evidence; neither the insect host nor a historical residue variant is treated as a natural human isoform. Supporting Evidence: PMID:29459785 catalyzes the first and committed step of N-linked glycosylation on the cytosolic face of endoplasmic reticulum (ER) membrane
GO:0006488 dolichol-linked oligosaccharide biosynthetic process	IDA PMID:29459785 GlcNAc-1-P-transferase-tunicamycin complex structure reveals...	ACCEPT	Summary: The directly measured reaction is the first step of LLO biosynthesis. Reason: The human GPT/Dol-P assays in PMID:29459785 demonstrate formation of the lipid-linked precursor. This is direct participation in GO:0006488 through catalysis, without assigning the later oligosaccharyltransferase reaction or downstream glycoprotein-specific effects as additional activities. Supporting Evidence: PMID:29459785 This reaction involves the transfer of N-acetylglucosamine-1-phosphate (GlcNAc-1-P) from UDP-N-acetylglucosamine (UDP-GlcNAc) to the carrier lipid dolichyl-phosphate (Dol-P).
GO:0003976 UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity	IDA PMID:6289658 Demonstration of the heterozygous state for I-cell disease a...	REMOVE	Summary: The full original assays a different phosphotransfer reaction. Reason: The recovered PMID:6289658 Methods on pp.718–720 assay human leukocyte/fibroblast extracts using alpha-methylmannoside and endogenous glycoprotein acceptors; Results/Fig.1 and Discussion pp.720–725 concern lysosomal phosphomannosyl targeting. GO:0003976 explicitly transfers GlcNAc-phosphate to lysosomal-enzyme D-mannose (EC2.7.8.17), whereas DPAGT1 transfers it to Dol-P (GO:0003975; EC2.7.8.15). The demonstrated reaction does not establish DPAGT1 activity and the attribution is miscited. This conclusion rests on actual assay chemistry, not the title or an abstract-only absence; the 1982 study is not claimed to have molecularly identified modern GNPT subunits. Supporting Evidence: PMID:6289658 a deficiency of the enzyme UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase PMID:29459785
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-4549334	ACCEPT	Summary: The disease-event source retains the correct ER-membrane context. Reason: The defective-event catalyst is explicitly modeled in the ER membrane and linked to the normal DPAGT1 event. This is consistent with the target enzyme location and does not assert identical stability, abundance or localization for every pathogenic variant. Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-446191	ACCEPT	Summary: The normal catalytic event places DPAGT1 in ER membrane. Reason: The exact Reactome catalyst identifies DPAGT1 in ER membrane; Dol-P and the lipid product occupy the cytoplasmic leaflet while soluble UDP-GlcNAc and UMP have cytosolic compartments. The reaction-level mixed compartments are not transferred wholesale to the protein. Supporting Evidence: PMID:30388443 The product GlcNAc-PP-Dol is anchored to the ER membrane by its dolichyl moiety
GO:0006487 protein N-linked glycosylation	IMP PMID:19549906 Overexpression of DPAGT1 leads to aberrant N-glycosylation o...	MODIFY	Summary: Retain the glycosylation role with the specific performed LLO-assembly step. Reason: The original human HOK/A253 and tumor studies measure E-cadherin glycan sensitivity and a DPAGT1-siRNA-associated decrease in N-glycosylation, with altered junctional organization. These are positive pathway effects. Independent direct enzyme evidence identifies the work DPAGT1 performs as initiation of LLO assembly (GO:0006488, a descendant of GO:0006487). This target-level refinement does not claim that the 2009 study itself measured purified lipid transfer or that DPAGT1 glycosylates E-cadherin directly. Proposed replacements: dolichol-linked oligosaccharide biosynthetic process Supporting Evidence: PMID:19549906 initiates the synthesis of the lipid-linked oligosaccharide (LLO) precursor for protein N-glycosylation in the endoplasmic reticulum PMID:19549906 elevated expression of DPAGT1, the gene that initiates protein N-glycosylation PMID:29459785
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	IMP PMID:12872255 Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosam...	ACCEPT	Summary: Patient-cell and mutant data support the established GPT reaction. Reason: The accessible PMID:12872255 abstract explicitly reports reduced GPT activity in patient fibroblast microsomal fractions and very low activity of the paternal Y170C cDNA product in CHO cells, while oligosaccharyltransferase activity is normal. This supports the curated molecular function and separates the two enzymes. Full Methods were not recovered; no additional construct or kinetic detail is inferred. Supporting Evidence: PMID:12872255 N-acetyl-glucosamine-1 phosphate transferase (GPT) activity encoded by DPAGT1 PMID:12872255 the GPT activity is reduced to approximately 10% of normal levels
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity	IDA PMID:8179616 Major defect of carbohydrate-deficient-glycoprotein syndrome...	ACCEPT	Summary: Retain the curated assay of the Dol-P-dependent GPT activity. Reason: The accessible PMID:8179616 abstract measures dolichyl-phosphate content and the specified GlcNAc-1-P transferase activity in patient and normal fibroblasts, finding similar levels in those cases. This is positive biochemical measurement of the reaction, not evidence that later established DPAGT1 deficiency cannot cause CDG. Full assay Methods were not recovered; the well-established target function is retained without inventing molecular construct details. Supporting Evidence: PMID:8179616 activity in CDG syndrome fibroblasts were similar to those in normal
GO:0016020 membrane	ISS GO_REF:0000024	MODIFY	Summary: Specify the conserved membrane localization to ER membrane. Reason: The current source context identifies Chinese-hamster P24140, whose PMID:8940049 abstract describes selective-permeabilization, epitope and cleavage-site topology experiments for an ER enzyme. Human evidence independently supports the same compartment. The broad historical membrane assertion is therefore refined without claiming the original source dictionary already carried those donor details. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt Multi-pass membrane protein
GO:0016020 membrane	IDA PMID:8179616 Major defect of carbohydrate-deficient-glycoprotein syndrome...	MODIFY	Summary: Specify the correct membrane association using independent ER evidence. Reason: Retain the experimental curator's membrane assignment from PMID:8179616; its accessible abstract confirms cellular enzyme activity but does not expose the fractionation Methods. The ER-membrane replacement is supported independently by official localization, curated reactions and human structural/biochemical evidence. It is a target-level refinement, not a claim that the recovered 1994 text directly resolved ER topology. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt Multi-pass membrane protein PMID:29459785
GO:0043231 intracellular membrane-bounded organelle	IDA PMID:12872255 Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosam...	MODIFY	Summary: The intracellular-organelle term can be specified to ER membrane. Reason: PMID:12872255 explicitly reports patient-fibroblast microsomal enzyme assays, supporting an intracellular membrane fraction. Independent target evidence identifies ER membrane, whose is_a/part_of closure reaches intracellular membrane-bounded organelle. The more specific location retains the positive source claim without pretending that microsomes alone identify an exclusive organelle pool. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/DPAGT1/DPAGT1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum PMID:29459785
GO:0005789 endoplasmic reticulum membrane	ISS GO_REF:0000024	ACCEPT	Summary: Retain the separately seeded P24140-to-human ER-membrane assertion. Reason: This is a genuine additional ISS donor-specific source row from normal fetching, distinct from the historical donor-unspecified row. Chinese-hamster P24140 has ER-topology experimental support summarized in PMID:8940049; the accessible abstract and independent human evidence support conservation. No direct assay of all human natural products is inferred. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: PMID:8940049 PMID:29459785
GO:0005794 Golgi apparatus	IEA GO_REF:0000107	UNDECIDED	Summary: The current Golgi transfer has an unresolved donor-evidence scope. Reason: The genuine GO_REF:0000107 row names mouse P42867 and ENSMUSP00000056282. Current QuickGO traces P42867 GO:0005794 to an MGI IPI annotation with Q8BH26 and PMID:36074821. The available full main text describes LYSET–GNPTAB Golgi co-immunoprecipitation/localization; target-specific DPAGT1 evidence in the detailed supplementary material could not be inspected. The supplement endpoint reports unavailable open-access files and the PMC route challenges access. This does not prove a wrong-gene annotation or exclude a Golgi pool because DPAGT1 is mainly ER-localized. Retain the source but leave this particular transfer unresolved pending its actual target evidence. Propagation Review Root cause: UNRESOLVED Supporting Evidence: PMID:36074821
GO:0016020 membrane	IEA GO_REF:0000002	MODIFY	Summary: The genuine current InterPro membrane mapping can be specified to ER membrane. Reason: IPR000715 currently includes a membrane mapping and the target carries the entry. The broad family spans more than one phosphotransferase lineage, but human DPAGT1's own topology, location and reaction evidence identify ER membrane. This independently justified target refinement preserves the current mapping identity and does not replace the historical GO_REF:0000120 row in place. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:29459785

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

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Source Evidence

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