GORASP1

the Golgicomplex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is a membrane protein involved in establishing the stacked structure of the Golgiapparatus. It is a caspase-3 substrate, and cleavage of this encoded protein contributes to Golgi fragmentation in apoptosis. This encoded protein can form a complex with the Golgimatrix protein GOLGA2, and this complex binds to the vesicle docking protein p115. Alternative splicing results in multiple transcript variants of this gene.

golgi reassembly stacking protein 1

Plays an important role in assembly and membrane stacking of the Golgi cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (PubMed:26363069).

Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis (By similarity).

Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (PubMed:16489344).

Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936).

Establishment of protein localization to plasma membrane Source: UniProtKB
Golgi organization Source: UniProtKB
Negative regulation of dendrite morphogenesis Source: UniProtKB
Protein N-linked glycosylation Source: Ensembl
Protein transport Source: UniProtKB-KW

Cis-Golgi network membrane; Endoplasmic reticulum-Golgi intermediate compartment membrane

Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking.By similarity
Target for caspase-3 cleavage during apoptosis. The cleavage contributes to Golgi fragmentation and occurs very early in the execution phase of apoptosis.By similarity
Myristoylated.By similarity