Golgin subfamily B member 1 (GOLGB1)

Golgin subfamily B member 1 (GOLGB1), commonly known as giantin, is a large, coiled-coil Golgi matrix protein anchored to the Golgi membrane by its C-terminal transmembrane domain[1][2]. It is essential for the proper localization and glycosylation of proteins, acting in membrane trafficking, vesicle tethering, and the organization of the Golgi structure and function[1][2][3]. GOLGB1 interacts with other Golgi proteins such as p115 (Uso1), GM130, and small GTPases (Rab1, Rab6), facilitating the tethering and docking of vesicles[1][2]. Mutations in GOLGB1 disrupt glycosylation and lead to developmental defects, notably including cleft palate, dwarfism, and osteochondrodysplasia in animal models[1]. In humans, variants or loss-of-function in GOLGB1 have been implicated in congenital disorders of glycosylation, craniofacial defects, and immunodeficiencies[3]. GOLGB1 is not classified as a druggable or therapeutic target and has no known approved interacting drugs.

Other names

Golgin B1GiantinGCPGCP372MacrogolginGolgi integral membrane protein 1GOLIM1Golgi autoantigenGolgi subfamily B member 1372 kDa Golgi complex-associated protein