Uggt1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: This is the defining core molecular function of UGGT1. It transfers a glucose residue from UDP-glucose onto deglucosylated N-linked glycans on non-native glycoproteins, regenerating the monoglucosylated tag of the calnexin/calreticulin cycle. Falcon deep research confirms the reaction and its Ca2+/DxD-motif requirement. Reason: Core molecular function, well supported phylogenetically (IBA), by direct rat biochemistry (PMID:10764828, PMID:1533626), and by the falcon synthesis. Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 is a reglucosylating glycosyltransferase that transfers a glucose residue from UDP-glucose onto deglucosylated N-linked glycans on glycoproteins that have not reached a native conformation. file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 converted Man9GlcNAc2 → Glc1Man9GlcNAc2 on MHC I, which is the canonical “tag” for lectin-chaperone binding in the ER. file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 catalytic activity requires Ca2+, coordinated by a DxD motif in the catalytic site
GO:0005783 endoplasmic reticulum	IBA GO_REF:0000033	ACCEPT	Summary: UGGT1 is a soluble ER-resident enzyme; immunogold labeling places it throughout the ER, including the nuclear envelope, and in pre-Golgi intermediates. The IBA from the PTN000132051 node (WITH/FROM includes fly, fission yeast, human and rat family members) is consistent with this conserved ER residence. Reason: ER residence is directly observed for the rat enzyme and is conserved across the UGGT family; the IBA node placement is sound and the rat protein's own appearance in WITH/FROM reflects its experimental grounding. Supporting Evidence: PMID:11535823 Labeling for GT, as well as for glucosidase II and calreticulin, was found in the endoplasmic reticulum (ER), including nuclear envelope and pre-Golgi intermediates located between ER and Golgi apparatus PMID:10764828 The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins.
GO:0051082 unfolded protein binding	IBA GO_REF:0000033	MARK AS OVER ANNOTATED	Summary: UGGT1 is a conformation sensor that selectively recognizes and binds non-native/partially folded glycoproteins (preferring exposed hydrophobic surfaces) as the recognition step preceding reglucosylation. That recognition is real and directly assayed (GO:0051082 IDA from PMID:10764828), but it is the substrate-selection step of the glucosyltransferase rather than a standalone chaperone-like binding function, and GO:0051082 is now formally obsolete with no replacement that fits a glycoprotein quality-control sensor - so the term over-annotates the gene. Reason: Recognition/binding of non-native glycoprotein clients is real, but it is the substrate-selection step intrinsic to UGGT1's glucosyltransferase activity rather than a standalone chaperone-like binding function. GO:0051082 has been formally obsoleted in the ontology (OLS returns the label "obsolete unfolded protein binding", with the stated reason that binding terms of this kind should be replaced by an activity term such as GO:0044183 or GO:0140309); neither replacement fits a glycoprotein quality-control sensor. This restores the project-level call in projects/UNFOLDED_PROTEIN_BINDING.md, which records rat Uggt1 (Q9JLA3) as OVER_ANNOTATED for this term with no suitable replacement ("not chaperones"). The IBA is additionally stale — the current PANTHER PAINT release no longer carries an IBD for GO:0051082 in PTHR11226. GOA no longer carries this IBA row. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: ROLE CONFLATION Sources checked: PANTHER:PTHR11226 · UDP-glucose glycoprotein glucosyltransferase family (PAINT) SOURCE STALE OR MISSING No IBD for GO:0051082 remains in the current PTHR11226 PAINT slice (snapshot 20260528); the remaining IBDs at PTN000132051 are GO:0003980, GO:0005783, and GO:0006487 only. GO:0051082 (unfolded protein binding) has been formally obsoleted in the ontology, which likely explains its removal from PAINT. The underlying binding is real and directly assayed (PMID:10764828 IDA), so the defect is the term - it conflates conformation-sensing substrate selection by a glucosyltransferase with chaperone-like unfolded-protein binding - not the propagation path. Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 is a conformation sensor: it preferentially acts on proteins that are non-native and can prefer clients with exposed hydrophobic regions, consistent with recognition of misfolded/partially folded surfaces rather than fully folded proteins.
GO:0097359 UDP-glucosylation	IEA GO_REF:0000108	ACCEPT	Summary: Inter-ontology inference from GO:0003980 (UDP-glucosylation is part_of UDP-glucose:glycoprotein glucosyltransferase activity). UGGT1 transfers glucose from UDP-glucose to N-glycans, which is a UDP-glucosylation. Reason: Follows logically from the well-established glucosyltransferase activity, including the rat enzyme's absolute UDP-Glc requirement. Supporting Evidence: PMID:1533626 The pure enzyme shows an almost absolute requirement for Ca2+ ions and for UDP-Glc as sugar donor.
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Combined automated annotation (InterPro IPR009448 and Rhea 61304) to the defining catalytic activity of UGGT1, matching direct biochemistry on the rat enzyme. Reason: Core molecular function, independently established for the purified rat liver and recombinant rat enzymes. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides. UniProtKB:Q9JLA3 Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum.
GO:0005788 endoplasmic reticulum lumen	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular-location mapping to the ER lumen. UGGT1 is a soluble luminal protein with a signal peptide and a C-terminal HEEL ER-retention tetrapeptide. Reason: The luminal location is where reglucosylation occurs and is supported by sequence features and direct localization of the rat protein. Supporting Evidence: UniProtKB:Q9JLA3 SUBCELLULAR LOCATION: Endoplasmic reticulum lumen PMID:10764828 The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins.
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular-location mapping to the ER-Golgi intermediate compartment, based on immunogold localization of UGGT1 to pre-Golgi intermediates in rat liver and pancreas. Reason: Directly supported by quantitative immunoelectron microscopy, where pre-Golgi intermediates carried the highest UGGT1 labeling density. Supporting Evidence: PMID:11535823 labeling intensity for GT was highest in pre-Golgi intermediates, corresponding to twice that of rough ER
GO:0009101 glycoprotein biosynthetic process	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: InterPro-based mapping (IPR009448) to glycoprotein biosynthetic process. UGGT1 covalently adds a glucose to N-glycans of glycoproteins, so it does modify glycoprotein glycans, but the added glucose is transient (removed again by glucosidase II) and serves folding quality control rather than building the mature glycan. Reason: Technically accurate as a broad parent of the N-glycan modification UGGT1 performs, but it does not describe the quality-control purpose of the reaction; kept as non-core. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides.
GO:0016740 transferase activity	IEA GO_REF:0000043	ACCEPT	Summary: Manual review: transferase activity is consistent with known biology of Uggt1. Reason: Retained as supported or plausible for this gene and evidence context. GOA no longer carries this keyword-mapping row. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides.
GO:0016757 glycosyltransferase activity	IEA GO_REF:0000043	ACCEPT	Summary: Manual review: glycosyltransferase activity is consistent with known biology of Uggt1. Reason: Retained as supported or plausible for this gene and evidence context. GOA no longer carries this keyword-mapping row. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides.
GO:1901135 carbohydrate derivative metabolic process	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Manual review: carbohydrate derivative metabolic process may be context-dependent or peripheral for Uggt1. Reason: Kept as non-core to preserve potentially valid context-specific annotation without elevating it to core function. GOA no longer carries this ARBA row. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides.
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	ISO GO_REF:0000121	ACCEPT	Summary: ISO transfer from human UGGT1 (UniProtKB:Q9NYU2) of the defining glucosyltransferase activity. The rat enzyme has its own direct biochemical evidence for the same activity. Reason: Correct transfer of a conserved core activity from the human ortholog; redundant with, and consistent with, the rat EXP/IDA rows. Supporting Evidence: PMID:10764828 The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver.
GO:0009306 protein secretion	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: ISO transfer from mouse Uggt1 (MGI:2443162), whose source row (QuickGO, Q6P5E4) is IMP from PMID:20498017. In ugt1-/- mouse cells, secretion of the endogenous UGGT1 substrate prosaposin dropped sharply and prosaposin accumulated in aggresome-like inclusions. Reason: The acts_upstream_of_or_within qualifier fits - UGGT1 does not perform secretion but its folding quality-control role is required for some glycoproteins to mature and be secreted. A real but indirect, substrate-dependent consequence, so non-core. Supporting Evidence: PMID:20498017 A dramatic decrease in the secretion of prosaposin was observed in ugt1(-/-) cells
GO:0032991 protein-containing complex	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: ISO transfer from human UGGT1 (UniProtKB:Q9NYU2) to protein-containing complex. Rat UGGT1 occurs in a tight complex with the selenoprotein SELENOF (Sep15), first isolated from rat prostate, and in a large ER chaperone multiprotein complex. Reason: Accurate - the UGGT1-SELENOF complex is directly documented for the rat protein - but the generic complex term carries little information; kept as non-core. Supporting Evidence: UniProtKB:Q9JLA3 Monomer as well as in a tight complex with SELENOF (PubMed:11278576). PMID:11278576 The native Sep15 isolated from rat prostate and mouse liver occurred in a complex with a 150-kDa protein. The latter protein was identified as UDP-glucose:glycoprotein glucosyltransferase (UGTR)
GO:0005515 protein binding	IPI PMID:11278576 Association between the 15-kDa selenoprotein and UDP-glucose...	REMOVE	Summary: This IPI corresponds to the specific UGGT1-SELENOF (SEP15) interaction reported in PMID:11278576. The bare 'protein binding' term is uninformative; the functionally relevant partnership is a stable, high-affinity complex with the redox-active selenoprotein cochaperone SELENOF, documented in the falcon synthesis. The interaction itself is real and biologically meaningful, but GO:0005515 does not capture it. Reason: GO:0005515 is uninformative. The partner is rat SELENOF (UniProtKB:Q923V8); the paper shows co-purification of the two proteins but no activity of UGGT1 toward SELENOF, so no more specific MF term is supported (SELENOF is a proposed redox cochaperone, not a substrate or established chaperone). The complex membership is already captured by the protein-containing complex row. Removal reflects the uninformative term, not doubt about the interaction, which is well established. Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 forms a stable complex with the selenoprotein SEP15/SELENOF, which is proposed to act as a redox-active cochaperone in ER folding surveillance. PMID:11278576 The native Sep15 isolated from rat prostate and mouse liver occurred in a complex with a 150-kDa protein. The latter protein was identified as UDP-glucose:glycoprotein glucosyltransferase (UGTR)
GO:0005788 endoplasmic reticulum lumen	IDA PMID:11535823 Immunolocalization of UDP-glucose:glycoprotein glucosyltrans...	ACCEPT	Summary: UGGT1 is a soluble ER luminal enzyme bearing a C-terminal ER-retention motif; the ER lumen is where it carries out reglucosylation as part of the CNX/CRT quality-control cycle. This is the core site of action, supported by direct immunolocalization (PMID:11535823) and the falcon synthesis. Reason: Core subcellular localization, directly observed (IDA) and consistent with the falcon synthesis describing UGGT1 as an ER-resident luminal enzyme. Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 is described across multiple mammalian studies as ER-localized/ER-resident and operating in the ER lumen as part of ER protein quality control and early secretory pathway surveillance.
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment	IDA PMID:11535823 Immunolocalization of UDP-glucose:glycoprotein glucosyltrans...	ACCEPT	Summary: Quantitative immunogold electron microscopy of rat liver and pancreas localized UGGT1 to pre-Golgi intermediates between the ER and Golgi, at about twice the labeling density of rough ER, with no specific Golgi labeling. Reason: Direct localization evidence; places UGGT1 quality-control activity in the ER-Golgi intermediate compartment as well as the ER. Supporting Evidence: PMID:11535823 labeling intensity for GT was highest in pre-Golgi intermediates, corresponding to twice that of rough ER
GO:0051082 unfolded protein binding	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: Same call as the IBA/IDA unfolded protein binding rows. Recognition and binding of non-native glycoprotein clients is real and conserved - the ISO transfer from human UGGT1 is sound and the donor carries its own IDA - but the obsolete term casts a glucosyltransferase's substrate selection as chaperone-like unfolded-protein binding, so it over-annotates the gene. Reason: Same call as the IBA and IDA rows for this obsolete term. The ISO transfer is consistent with the conserved folding-sensor mechanism, but the term itself is obsolete and characterises UGGT1 as a chaperone-like binder rather than a glycoprotein quality-control sensor, per projects/UNFOLDED_PROTEIN_BINDING.md. GOA no longer carries this ISO row. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: ROLE CONFLATION Sources checked: UniProtKB:Q9NYU2 · human UGGT1 SUPPORTS SOURCE BUT NOT TARGET The rat ISO names human UGGT1 as its donor (WITH/FROM UniProtKB Q9NYU2 in the rat GOA record), and the donor annotation is experimentally grounded rather than weak - the human record carries GO:0051082 by IDA (PMID:10694380) alongside the IBA. The defect is therefore in the term, not in the propagation path or the source evidence. GO:0051082 is obsolete, and it conflates conformation-sensing substrate selection by a glucosyltransferase with chaperone-like unfolded-protein binding. The same call is recorded for the human gene in projects/UNFOLDED_PROTEIN_BINDING.md. Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 preferentially acts on non-native/partially folded glycoproteins and prefers proteins with exposed hydrophobic regions over folded proteins.
GO:0051082 unfolded protein binding	IDA PMID:10764828 Cloning and characterization of mammalian UDP-glucose glycop...	MARK AS OVER ANNOTATED	Summary: Direct-assay evidence that UGGT1 binds non-native protein substrates. The binding itself is not in doubt and the falcon synthesis corroborates the conformation-sensing recognition activity; but that recognition is the substrate-selection step of the glucosyltransferase mechanism, and the obsolete GO:0051082 frames it as chaperone-like unfolded-protein binding, so the term over-annotates the gene even on this, the strongest of the three rows. Reason: The direct experimental evidence (IDA) for binding of non-native protein clients is not in doubt, and this row is the strongest of the three. It is kept rather than removed for that reason. The term is nonetheless obsolete, and it frames a glycoprotein quality-control sensor as a chaperone-like binder, so it is marked over-annotated in line with projects/UNFOLDED_PROTEIN_BINDING.md. The underlying recognition step is retained in core_functions as part of the glucosyltransferase activity (GO:0003980) that it serves. GOA no longer carries this row (the term is obsolete). Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md UGGT1 is a conformation sensor: it preferentially acts on proteins that are non-native and can prefer clients with exposed hydrophobic regions
GO:0005515 protein binding	IPI PMID:10764828 Cloning and characterization of mammalian UDP-glucose glycop...	REMOVE	Summary: IPI row citing the rat UGGT1 cloning paper with rat SELENOF (UniProtKB:Q923V8) as the partner. The cached abstract (full text unavailable) covers cloning, substrate preference and catalytic residues and does not mention SELENOF, so the specific interaction evidence the curator used could not be inspected here. The UGGT1-SELENOF complex itself is independently documented (PMID:11278576). Reason: GO:0005515 is uninformative, and no more specific MF can be derived from a UGGT1-SELENOF co-association (see the PMID:11278576 row). Complex membership is captured by the protein-containing complex row. Removal reflects the uninformative term, not doubt about the interaction. Supporting Evidence: PMID:11278576 The native Sep15 isolated from rat prostate and mouse liver occurred in a complex with a 150-kDa protein. The latter protein was identified as UDP-glucose:glycoprotein glucosyltransferase (UGTR)
GO:0005783 endoplasmic reticulum	ISO GO_REF:0000121	ACCEPT	Summary: ISO transfer of ER localization from human UGGT1 (UniProtKB:Q9NYU2). Consistent with direct immunolocalization of the rat protein to the ER. Reason: Conserved ER residence, directly observed for rat UGGT1. Supporting Evidence: PMID:11535823 Labeling for GT, as well as for glucosidase II and calreticulin, was found in the endoplasmic reticulum (ER), including nuclear envelope and pre-Golgi intermediates located between ER and Golgi apparatus
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	IDA PMID:10764828 Cloning and characterization of mammalian UDP-glucose glycop...	ACCEPT	Summary: Arnold et al. cloned rat liver UGGT, expressed it in insect cells and showed the recombinant enzyme glucosylates unfolded Man9GlcNAc2-bearing glycoprotein acceptors (Km 44 microM for UDP-glucose), mapping catalytic residues D1334, D1336, Q1429 and N1433. Reason: Direct assay of the recombinant rat enzyme for the core activity. Supporting Evidence: PMID:10764828 The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver. PMID:10764828 Recombinant rat UGGT has a K (m) of 44 microM for UDP-glucose.
GO:0051084 'de novo' post-translational protein folding	TAS PMID:10764828 Cloning and characterization of mammalian UDP-glucose glycop...	MODIFY	Summary: TAS to 'de novo' post-translational protein folding citing the rat UGGT cloning paper. UGGT1 contributes to folding of newly synthesized glycoproteins by reglucosylating non-native ones so they re-enter calnexin/calreticulin binding; it does not itself fold polypeptides, and the cycle operates specifically in the ER lumen. Reason: The involvement is real, but the specific contribution is to the ER glycoprotein folding/quality-control cycle. As for the protein folding TAS row, GO:0034975 (protein folding in endoplasmic reticulum) states it at the right scope and is the process term carried in core_functions. Proposed replacements: protein folding in endoplasmic reticulum Supporting Evidence: UniProtKB:Q9JLA3 Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum.
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	TAS PMID:10764828 Cloning and characterization of mammalian UDP-glucose glycop...	ACCEPT	Summary: TAS for the defining glucosyltransferase activity, citing the rat UGGT cloning and characterization paper, which directly assayed the activity. Reason: Correct; redundant with the IDA row from the same paper. Supporting Evidence: PMID:10764828 The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver.
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	IDA PMID:12518055 UDP-Glc:glycoprotein glucosyltransferase recognizes structur...	ACCEPT	Summary: Caramelo et al. used chemically glycosylated chymotrypsin inhibitor-2 variants as acceptors and showed that UGGT glucosylates molten globule-like folding intermediates with exposed hydrophobic patches, defining its folding-sensor substrate selectivity. Reason: Direct assay of glucosyltransferase activity on defined acceptors; supports the core activity and its conformation-sensing selectivity. Supporting Evidence: PMID:12518055 GT serves as a folding sensor because it only glucosylates misfolded or partly folded glycoproteins.
GO:0006457 protein folding	TAS PMID:12518055 UDP-Glc:glycoprotein glucosyltransferase recognizes structur...	MODIFY	Summary: UGGT1 contributes to protein folding indirectly, by reglucosylating non-native glycoproteins so they re-engage the calnexin/calreticulin lectin chaperones for additional folding rounds and avoid premature ER exit. The generic 'protein folding' term captures this only at a high level; the precise role is the glycan-dependent quality-control/folding cycle described in the falcon synthesis. Replaced by the compartment-specific GO:0034975 (protein folding in endoplasmic reticulum), which states the same involvement at the right scope. Reason: UGGT1 does not directly fold proteins; it drives the lectin-chaperone folding cycle in the ER lumen. The generic 'protein folding' term is broad relative to that mechanism and is not compartment-specific; GO:0034975 (protein folding in endoplasmic reticulum) states the same involvement at the right scope and is the term this review carries in core_functions. Proposed replacements: protein folding in endoplasmic reticulum Supporting Evidence: file:rat/Uggt1/Uggt1-deep-research-falcon.md When a glycoprotein carries a monoglucosylated N-glycan it can bind CNX/CRT; after deglucosylation, a protein that is still non-native can be reglucosylated by UGGT1, enabling additional rounds of CNX/CRT-assisted folding and preventing premature ER exit.
GO:0003980 UDP-glucose:glycoprotein glucosyltransferase activity	EXP PMID:1533626 Purification to apparent homogeneity and partial characteriz...	ACCEPT	Summary: Trombetta and Parodi purified UGGT to apparent homogeneity from rat liver and showed it synthesizes Glc1Man7-9GlcNAc2-protein from Man7-9GlcNAc2-protein, with an almost absolute requirement for Ca2+ and UDP-Glc, and with denatured glycoproteins glucosylated much more efficiently than native ones. Reason: Direct biochemical characterization of the purified rat enzyme; foundational evidence for the core activity and its preference for non-native acceptors. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides. PMID:1533626 Denatured glycoproteins are glucosylated much more efficiently than native ones by the apparently homogeneous glucosyltransferase.
GO:0005788 endoplasmic reticulum lumen	ISO GO_REF:0000121	ACCEPT	Summary: ISO transfer of ER lumen localization from human UGGT1 (UniProtKB:Q9NYU2); same term as the rat IDA and IEA rows. Reason: Soluble luminal residence is conserved and directly supported for the rat protein (signal peptide plus HEEL retention signal; immunolocalization). Supporting Evidence: UniProtKB:Q9JLA3 SUBCELLULAR LOCATION: Endoplasmic reticulum lumen PMID:10764828 The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins.
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment	ISO GO_REF:0000121	ACCEPT	Summary: ISO transfer of ER-Golgi intermediate compartment localization from human UGGT1 (UniProtKB:Q9NYU2); same term as the rat IDA row. Reason: Consistent with direct immunogold localization of rat UGGT1 to pre-Golgi intermediates. Supporting Evidence: PMID:11535823 labeling intensity for GT was highest in pre-Golgi intermediates, corresponding to twice that of rough ER
GO:0006487 protein N-linked glycosylation	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: New IBA from PANTHER node PTN000132051 (WITH/FROM PomBase:SPBPJ4664.06 and WB:WBGene00018604). UGGT adds a glucose to protein-linked N-glycans, which falls within N-glycan processing (part_of protein N-linked glycosylation in GO). Reason: The family-level placement is sound - every UGGT acts on asparagine-linked glycans - and the rat enzyme directly glucosylates protein-linked high-mannose oligosaccharides. The reaction is a transient, quality-control modification rather than biosynthesis of the mature glycan, so the term is kept as non-core. Supporting Evidence: PMID:1533626 The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides.

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

📚 Additional Documentation

Notes

Bioreason Rl Predictions

Bioreason Rl Review

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