Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

PMID:15047703

The binary interacting network of the conserved oligomeric Golgi tethering complex.

Human COG4 forms positive contacts with COG1, COG2, COG5 and COG7 in reticulocyte-lysate co-translation/co-immunoprecipitation; the assembly analysis supports its scaffold role. Direct binary affinity was not measured with purified proteins.

PMID:19536132

Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.

COG4 brings the COG complex into contact with SCFD1/Sly1 and has a separate STX5-binding surface. Purified human COG4 (1–231) binds rat rSly1; endogenous HeLa assays support the human association. Binding-selective mutants distinguish recruitment from complex incorporation and link the activity to retrograde trafficking.

PMID:27066481

COG Complex Complexities: Detailed Characterization of a Complete Set of HEK293T Cells Lacking Individual COG Subunits.

Human HEK293T COG4 knockout alters Golgi ultrastructure, subunit stability and glycan processing. Replacement COG4 localizes to the Golgi and reverses glycosylation defects. Pathway-level toxin assays support retrograde traffic while receptor-binding changes limit some probes.

PMID:32296183

A reference map of the human binary protein interactome.

HuRI supplies positive binary interaction records for COG4 (253–785) and eight exact partner products. The records include validated two-hybrid detections; orthogonal validation reported for the dataset is not automatically assigned to each target pair.

PMID:33961781

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

BioPlex detects COG4 associations with four COG subunits and MUL1 by AP-MS. Exact records preserve assay hosts, tags and partner identities; co-purification does not require a purified direct interface.

PMID:40205054

Multimodal cell maps as a foundation for structural and functional genomics.

The original U2OS AP-MS network contains a COG2-bait/COG4-prey edge, supporting the source-specific association. The multimodal cell map is not itself evidence for every inferred function of the pair.

Reactome:R-HSA-6809006

Vesicle is tethered through binding GOLGA2:GORASP1, GOLGB1 and the COG complex

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-6809010

COPI vesicle uncoating

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-6809011

cis-Golgi t-SNAREs bind YKT6 on tethered vesicle

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-6811431

RAB6:GTP binds the GARP and COG complexes, t-SNAREs and endosome-derived vesicles

The event includes the exact COG4-bearing COG complex at the trans-Golgi network membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-6811433

The COG tethering complex interacts with numerous SNAREs at the Golgi membrane

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-6814682

Fusion of early-endosome derived vesicles at the TGN

The event includes the exact COG4-bearing COG complex at the trans-Golgi network membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-8847544

The COG complex and CUX1 and GOLGA5 dimers contribute to intra-Golgi vesicle tethering

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-8847635

Formation of cis-SNARE complex and membrane fusion in intra-Golgi retrograde traffic

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

Reactome:R-HSA-8849748

The COG complex binds RABs at the Golgi membrane

The event includes the exact COG4-bearing COG complex at the Golgi membrane. This is curated complex-location support, not an assignment of every event operation to COG4.

PMID:19494034

Golgi function and dysfunction in the first COG4-deficient CDG type II patient.

Patient fibroblasts with p.R729W and a deletion have reduced COG4, altered Golgi architecture and delayed retrograde trafficking, yet retain complex formation. Fractionation supports a major cytosolic subcomplex pool and a membrane-associated pool. Overexpression also perturbs trafficking, complicating rescue.

PMID:19651599

Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.

A human COG4 C-terminal structure and HeLa experiments implicate the distal domain in normal glycosylation without making it necessary for incorporation into the COG complex. This is structural/assembly context, not intrinsic glycosyltransferase activity.

PMID:30290151

A Recurrent De Novo Heterozygous COG4 Substitution Leads to Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered Proteoglycan Glycosylation.

A recurrent de novo substitution causes Saul-Wilson syndrome with altered fibroblast trafficking and decorin glycosylation, distinct from biallelic COG4 deficiency. The paper reports p.Gly516Arg; these original coordinates are not silently equated to the selected UniProt product.

PMID:11703943

The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic.

The yeast Sec34/35 tethering complex and structural relationships to other tethering complexes provide evolutionary context. This abstract does not independently establish a human COG4-specific catalytic activity.