COG7

Summary: COG7 associates with Golgi membranes.

Reason: The original full variant localizes tagged human COG7 near Golgi mannosidase II in HeLa cells. This supports peripheral Golgi association in the assembled COG complex, not membrane insertion.

Summary: COG7 associates with Golgi membranes.

Reason: The UniProt subcellular-location mapping agrees with direct human COG7 Golgi localization and COG-complex membership. COG7 is a peripheral complex component.

Summary: COG7 associates with Golgi membranes.

Reason: The knockout study places COG7 in the Golgi-associated octamer and directly examines its contribution to complex integrity. Original human COG7 localization supplies independent support.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 associates with Golgi membranes.

Reason: The exact Reactome event contains the Golgi-membrane COG complex, whose physical-entity chain includes COG7/P83436. Retain that location without assigning the event’s Rab, uncoating or SNARE-fusion chemistry to COG7.

Summary: COG7 supports retrograde intra-Golgi recycling.

Reason: The human knockout study directly establishes COG7-dependent lobe-B integrity and Golgi architecture. Its toxin assays use representative knockout subsets, so no uninspected panel is presented as a COG7-specific flux measurement. Original COG7 depletion and patient-cell studies independently show defective recycling of Golgi-resident proteins, while COG7’s performed assembly role supplies a molecular contribution to this machinery.

Summary: Retain the positive COG7–COG4 association.

Reason: Two exact COG7–COG4 co-immunoprecipitation records support this pair. The original reconstruction uses human cDNAs in rabbit reticulocyte lysate and explicitly limits binary directness pending purified-protein confirmation. The integrated COG7 scaffold refinement is anchored to its separately mapped COG5 interface, rather than assigning the whole assembly mechanism to every pair.

Summary: COG7 provides a structural interface for lobe-B assembly.

Reason: The original human reconstruction shows cooperative incorporation of COG6 by COG5 plus COG7 and optimal COG8 incorporation with the lobe-B partners. Independent human COG7 interface mutations impair COG5 association and reduce recovered lobe-B assembly. Together these establish performed structural assembly, supporting protein complex scaffold activity. The crystallographic fragments are from K. lactis, and the glycosylation-rescue experiment tests COG5 mutants; neither is presented as a full-length human COG7 assay. Human COG7 knockout also reduces the abundance of its lobe-B partners; this supports complex maintenance, separately from the measured interface and assembly assays.

Proposed replacements: protein complex scaffold activity

Summary: Retain source-specific COG7–rat Sly1 association.

Reason: The original Methods identify recombinant/transfected rat Sly1, consistent with Q62991. COG7 shows positive but weak co-isolation in the tested complex context. The strong selective, purified-binding and syntaxin-bridging results belong to COG4, not COG7. No exact pair was recovered in the queried interaction exports; that absence does not negate the original positive experiment or justify replacing the source partner.

Summary: Retain COG7–COG4 co-complex association.

Reason: Two exact anti-bait co-immunoprecipitation records in HeLa cells support the pair. The source investigates COG4-dependent Sly1/SNARE coordination, but its COG7 association does not independently establish COG7-specific bridging or purified affinity.

Summary: Retain the human COG7–mouse TRAF5 association.

Reason: Two exact anti-tag co-immunoprecipitation records map human COG7 and mouse P70191/TRAF5 in a human cell host. Preserve the mouse bait identity and positive complex association. The selected paper body provides Introduction and Discussion, while the literal interaction records authenticate this pair. No COG7 innate-immune signaling or catalytic role follows from the association.

Summary: Retain the positive COG7–TAX1BP1 interaction.

Reason: The HI-II-14 supplies three positive TAX1BP1–COG7 records labelled array, pooling and validated two hybrid. These records describe stages of a shared Y2H screening pipeline, not independent biological replications. TAX1BP1 is an experimentally supported ubiquitin-binding adaptor and selective-autophagy receptor. Those activities characterize the partner but do not identify a more specific applicable binding class here: binding an adaptor is not itself adaptor activity, and this pair does not establish ligand-triggered cargo-receptor activity. The positive generic interaction is retained without requiring a mapped interface or native colocalization.

Summary: Refine the MEOX2 interaction to RNA polymerase II-specific transcription-factor binding.

Reason: The three positive Q6FHY5 records identify array, pooling and validated-two-hybrid stages of one screen, not three independent replications. The exact 303-residue product differs from reviewed P50222 by one glutamine outside its unchanged homeobox. P50222 has experimentally supported RNA polymerase II-specific transcription-activator and sequence-specific DNA-binding functions. This supports the more specific partner class, with an explicit reference-product inference; the screen does not itself assay Q6FHY5 transcriptional activity. Neither compartment differences nor paper count negate the recorded binding, and no COG7 transcriptional role or native nuclear interaction is inferred.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the positive COG7–TAX1BP1 interaction.

Reason: The alternative-isoform screen supplies three positive TAX1BP1–COG7 records labelled array, pooling and validated two hybrid. These records describe stages of a shared Y2H screening pipeline, not independent biological replications. TAX1BP1 is an experimentally supported ubiquitin-binding adaptor and selective-autophagy receptor. Those activities characterize the partner but do not identify a more specific applicable binding class here: binding an adaptor is not itself adaptor activity, and this pair does not establish ligand-triggered cargo-receptor activity. The positive generic interaction is retained without requiring a mapped interface or native colocalization.

Summary: Refine the exact KIFC3/Q9BVG8-5 interaction to kinesin binding.

Reason: Three positive Y2H records map the exact 687-residue Q9BVG8-5 product, with matching sequence checksums and an intact kinesin motor domain at residues 306–629. Array, pooling and validated-two-hybrid labels describe screening stages, not independent biological replications; the related screen publications are not treated as independent confirmation. The established KIFC3 kinesin class and retained motor domain support kinesin binding. The record notes lack of experimental confirmation of the natural isoform, and no motor-activity assay of this exact product or native COG7–motor mechanism is claimed. The term assigns neither ATP hydrolysis nor cargo movement to COG7.

Proposed replacements: kinesin binding

Summary: Retain the positive COG7–TAX1BP1 interaction.

Reason: The positive variant-screen array-Y2H record includes a COG7 residue-749 feature classified as having no interaction effect; it is not a featureless wild-type assay. The related CCSB screen publications are not counted as independent biological replications. TAX1BP1 is an experimentally supported ubiquitin-binding adaptor and selective-autophagy receptor. Those activities characterize the partner but do not identify a more specific applicable binding class here: binding an adaptor is not itself adaptor activity, and this pair does not establish ligand-triggered cargo-receptor activity. The positive generic interaction is retained without requiring a mapped interface or native colocalization.

Summary: Retain the positive COG7–TAX1BP1 interaction.

Reason: The HuRI supplies three positive TAX1BP1–COG7 records labelled array, pooling and validated two hybrid. These records describe stages of a shared Y2H screening pipeline, not independent biological replications. TAX1BP1 is an experimentally supported ubiquitin-binding adaptor and selective-autophagy receptor. Those activities characterize the partner but do not identify a more specific applicable binding class here: binding an adaptor is not itself adaptor activity, and this pair does not establish ligand-triggered cargo-receptor activity. The positive generic interaction is retained without requiring a mapped interface or native colocalization.

Summary: Refine the exact KIFC3/Q9BVG8-5 interaction to kinesin binding.

Reason: Three positive Y2H records map the exact 687-residue Q9BVG8-5 product, with matching sequence checksums and an intact kinesin motor domain at residues 306–629. Array, pooling and validated-two-hybrid labels describe screening stages, not independent biological replications; the related screen publications are not treated as independent confirmation. The established KIFC3 kinesin class and retained motor domain support kinesin binding. The record notes lack of experimental confirmation of the natural isoform, and no motor-activity assay of this exact product or native COG7–motor mechanism is claimed. The term assigns neither ATP hydrolysis nor cargo movement to COG7.

Proposed replacements: kinesin binding

Summary: Retain the BioPlex COG7–COG4 association.

Reason: Two exact AP-MS records, from HEK293T and HCT116 contexts, support the source-specific pair. These are complex-association measurements; they are not independently mapped binary interfaces. The performed COG7 scaffold activity is represented by the original assembly-source refinement, while this distinct positive assertion remains non-core.

Summary: Retain the BioPlex COG7–COG5 association.

Reason: Two exact AP-MS records, from HEK293T and HCT116 contexts, support the source-specific pair. These are complex-association measurements; they are not independently mapped binary interfaces. The performed COG7 scaffold activity is represented by the original assembly-source refinement, while this distinct positive assertion remains non-core.

Summary: COG7 is localized to the Golgi apparatus.

Reason: The current Human Protein Atlas XML contains COG7/P83436 Golgi-apparatus localization in the examined cell lines. Original tagged human COG7 localization independently supports the broad compartment. Additional HPA locations are not manufactured as new assertions.

Summary: Human COG7 localizes near Golgi markers.

Reason: The genuine full variant of the original study describes tagged human 770-residue COG7 in HeLa cells and colocalization with a Golgi marker. Historical construct length is not substituted for an exact sequence alignment.

Summary: COG7 participates in intracellular protein transport.

Reason: The InterPro COG7-family mapping agrees with experimentally supported structural assembly of the COG complex and recycling of Golgi-resident proteins. Retain the broader transport assertion alongside the source-specific retrograde terms.

Summary: Human COG7 supports Golgi protein trafficking.

Reason: The original patient study measures delayed trafficking of pre-existing Golgi glycosylation machinery and restoration after wild-type COG7 expression. COG7 contributes the complex structure used by this traffic, rather than functioning as a transported glycoprotein substrate. Not every transport assay was abnormal, and intrinsic transporter or glycosyltransferase activity is not inferred.

Summary: COG7 participates in retrograde Golgi protein recycling.

Reason: The actually recovered original COG7-depletion Results report glycosyltransferase/SNARE redistribution and later partial ER localization. These are source-specific cellular recycling observations. The paper’s isolated-vesicle experiment and much of its detailed time course concern COG3; they are not transferred to COG7. COG7-specific patient-cell BFA experiments independently support the retained Golgi-to-ER process.

Summary: COG7 facilitates Golgi-to-ER retrograde transport.

Reason: Patient fibroblasts show delayed BFA-induced retrograde redistribution of multiple Golgi proteins, corrected by COG7 expression. Coat release is not detectably impaired, and anterograde traffic is less affected. This supports COG7’s structural contribution to retrograde machinery without equating BFA tubulation with an isolated vesicle-tethering reaction.

Summary: Conserved COG7 contribution to Golgi organization.

Reason: Current human and fly records include experimental Golgi-organization premises, and the plant donor has a source-specific developmental Golgi phenotype. Human COG7 interface/assembly and knockout morphology provide target-specific support. This is compatible with the inherited assertion; current donor records do not reconstruct the historical PAINT placement.

Summary: COG7 contributes to Golgi architecture.

Reason: The human HEK293T knockout directly changes COG5/COG6 abundance and produces dilated Golgi ministacks by EM, although several light-microscopy markers remain perinuclear. Human COG7 assembly-interface evidence supplies a performed structural role beyond an unexplained loss phenotype.

Summary: Retain contextual participation in glycoprotein biosynthesis.

Reason: The original patient study demonstrates altered glycan processing, Golgi enzyme traffic and source-specific sugar-transport/transferase measurements, with correction by wild-type COG7. The two patients do not share every biochemical defect. COG7 contributes structural trafficking machinery that positions Golgi enzymes for glycan synthesis. This is an indirect organizational contribution to the pathway, not intrinsic sugar-transfer chemistry; the integrated core is COG assembly and recycling.

Summary: Retain contextual participation in glycoprotein biosynthesis.

Reason: The original COG7-depletion section demonstrates altered glycosyltransferase localization and Lamp2 glycosylation; the more extensive COG3 time course is not presented as COG7 data. COG7 contributes structural trafficking machinery that positions Golgi enzymes for glycan synthesis. This is an indirect organizational contribution to the pathway, not intrinsic sugar-transfer chemistry; the integrated core is COG assembly and recycling.

Summary: COG7 is a conserved COG-complex subunit.

Reason: Current human and fly records support complex membership; the human target appearing among the descendants is legitimate experimental grounding. Human reconstruction and interface experiments independently establish COG7’s structural incorporation. Historical ancestral placement remains uninspected.

Summary: Human COG7 participates in reconstructed COG assemblies.

Reason: Human COG7 is translated and assembled with other COG subunits in rabbit reticulocyte lysate. COG5–COG7 cooperation supports incorporation of COG6 and optimal COG8. The assay establishes complex participation while possible endogenous factors limit a claim of purified binary affinity.

Summary: The COG7-family mapping identifies a COG component.

Reason: The InterPro assignment agrees with human COG7 assembly and interface evidence. It is not being used to transfer COG4-specific SNARE bridging or catalytic activity.

Summary: COG7 is an integral COG-complex component.

Reason: The complete human knockout study identifies the octamer and directly tests COG7-dependent lobe-B stability. Original reconstruction provides independent positive membership evidence.

Summary: COG7 associates with the trans-Golgi network machinery.

Reason: The actual Reactome physical-entity chain contains COG7/P83436 within the TGN-membrane COG complex. Retain this source-specific compartment context. It does not establish autonomous COG7 fusion or a single simultaneous GARP–COG tether.

Summary: COG7 associates with the trans-Golgi network machinery.

Reason: The actual Reactome physical-entity chain contains COG7/P83436 within the TGN-membrane COG complex. Retain this source-specific compartment context. It does not establish autonomous COG7 fusion or a single simultaneous GARP–COG tether.

Summary: COG7 supports organelle localization of Golgi proteins.

Reason: Actual COG7 knockdown redistributes GlcNAcT1 and GS15 while some Golgi markers remain positioned normally. The direct COG7 assembly role helps organize the machinery for such recycling and retention; this is participation in localization rather than COG7 merely being the cargo.

Summary: COG7 supports localization of proteins at the Golgi.

Reason: Patient fibroblasts show altered ERGIC-53 and SNARE distribution, restored in COG7-corrected cells. The phenotype is selective rather than global Golgi loss. COG7’s structural assembly contribution supplies a performed role in this localization machinery.

Summary: COG7 contributes to Golgi protein retention through recycling.

Reason: The current plant donor has an experimental source-specific premise, but that record is not a reconstruction of the PAINT node. Human COG7 depletion and corrected patient cells independently demonstrate displacement and restoration of Golgi residents, consistent with retention through recycling by the assembled COG machinery.

Summary: COG7 supports maintenance of selected Golgi proteins.

Reason: The original human HeLa COG7-knockdown Results and Figure 5 legend explicitly compare mock, COG3 and COG7 depletion: GM130 and syntaxin-5 abundance decrease in COG7-knockdown cells, and the short Golgi syntaxin-5 form is particularly affected. These are COG7 observations, not transferred COG3 results. The short literal excerpt and original DOI/section locator are provided in the source-evidence index because the publication cache contains only the abstract. This supports complex-mediated maintenance under the broad protein-stabilization definition, integrated with the scaffold core. It identifies neither direct protective contact nor a degradation pathway. Greater GlcNAcT1 instability after combined COG3/COG7 depletion remains a combined-perturbation result.

Summary: COG7 supports cellular maintenance of GS15.

Reason: COG7-deficient patient fibroblasts lose GS15 abundance and normal localization, both restored by COG7 correction. This supports complex-mediated protein maintenance within the scaffold core. The broad protein-stabilization process does not require isolated chaperone chemistry. Tested proteasomal and lysosomal inhibitors fail to restore GS15, leaving the depletion mechanism unresolved rather than contradicting maintenance. Variable changes in other residents are not generalized as uniformly COG7 dependent.