SCUBA

COPG1 — COPI coat complex subunit gamma 1

COPG1 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

COPG1's module in each cell type

Cell typeModuleShares the module with
Gamma-delta T cellsVesicular Trafficking
Housekeeping
ADD1, ANAPC5, EFCAB14, EXOC7, GANAB, MAN2B2, MCM3AP, MED1 +10 more
Goblet cellsProtein trafficking & glycosylation
Mucus production & secretion
COPA, COPB1, COPB2, EDEM3, FAM114A1, GALNT3, GALNT7, TM9SF2 +1 moreView in SCUBA

About the gene

SynonymsCOPG
Chromosome3: 129249606-129277773
Predicted locationIntracellular
Essential geneYes
Protein classEssential proteins, Metabolic proteins, Plasma proteins, Predicted intracellular proteins
Biological processER-Golgi transport, Protein transport, Transport

Function

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity)

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.