CCDC93 — Coiled-coil domain containing 93
CCDC93 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.
CCDC93's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | IFN-gamma Receptor Signaling Inflammation | BORCS5, CDC42SE2, DHCR7, EML4, IFNGR1, PDE4B, PGRMC2, PLEKHA2 +3 more | |
| Mucosal-associated invariant T cell | Post-translational Regulation Housekeeping | CD55, FBXO33, GALC, KCTD20, KDM2B, MGAT4A, MSL2, PDE4D +8 more |
About the gene
| Synonyms | FLJ10996 |
|---|---|
| Chromosome | 2: 117915478-118014133 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Predicted intracellular proteins, Transporters |
| Biological process | Protein transport, Transport |
Function
Component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of composed of the CCC subcomplex and the retriever subcomplex. Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1. Involved in copper- dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with WASHC2C. (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.