SCUBA

CASD1 — CAS1 domain containing 1

CASD1 belongs to a gene co-expression module in 1 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.

CASD1's module in each cell type

Cell typeModuleShares the module with
CD4⁺ T cellsT cell Coinhibition
Immune regulation
BTLA, CFAP36, DUSP14, FCHSD2, HIVEP2, IFNGR2, KLF7, NAP1L2 +7 moreView in SCUBA

About the gene

SynonymsC7orf12, FLJ21213, FLJ21879
Chromosome7: 94509219-94557019
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classEnzymes, Predicted intracellular proteins, Predicted membrane proteins
Molecular functionAcyltransferase, Transferase

Function

Key enzyme in the biosynthesis of O-acetylated (O-Ac) sialoglycans such as gangliosides O-AcGD3 and O-AcGD2, which affect various processes such as cell-cell interactions, host-pathogen recognition. Catalyzes the transfer of an acetyl group from a donor, the acetyl- coenzyme-A molecule (acetyl-CoA), to the C7/8/9 OH-position of a sialic acid residue. The primary site of O- acetyl group transfer on sialic acid seems to depend on cell type and can be C7, from which the O-acetyl group could subsequently migrate to the C8 and then to the C9 position, or at C9 with possibility of migrating to the C8 and then to the C7 position. Together with ST8SIA1 (GD3 synthase) it increases the levels of ganglioside Ac-O-7-GD3. Can transfer the acetyl group from acetyl-CoA to free sialate (N-acetylneuraminate, Neu5Ac) in vitro, but has preferred substrate specificity for CMP- activated sialate (CMP-Neu5Ac), resulting in the formation of 9-O- acetylated CMP-Neu5Ac (CMP-Neu5,9Ac2). CMP-Neu5,9Ac2 may be used by sialyltransferases as a sialate donor for glycoconjugate acceptors such as ganglioside GD3. O-acetylation at position C9 of ganglioside GD3 can counteract the pro-apoptotic effects of the ganglioside GD3 in tumor cells.

Human Protein Atlas · Open Targets · UniProt

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