ATP9A — ATPase phospholipid transporting 9A (putative)
ATP9A belongs to a gene co-expression module in 3 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.
ATP9A's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Endothelial | Venous EC Identity Endothelial cell development | ALDH1A1, ALDH3A2, ASGR1, BMP2K, DSP, FAM107B, KIAA1522, LIMD2 +12 more | View in SCUBA |
| Fibroblasts | Intestinal Fibroblast Identity Developmental | ABR, AFF3, ATP8A1, CAMK4, DSE, ENPP2, GLP2R, MRPS6 +7 more | View in SCUBA |
| Lymphatic endothelial | Endosomal Vesicle Trafficking Housekeeping | ADAM10, APC, APP, GLG1, MTR, NCOA3, PCNX4, PDCD6IP +5 more | View in SCUBA |
About the gene
| Synonyms | ATPIIA, KIAA0611 |
|---|---|
| Chromosome | 20: 51596514-51768390 |
| Predicted location | Membrane |
| Essential gene | No |
| Protein class | Enzymes, Predicted membrane proteins, Transporters |
| Molecular function | Translocase |
| Biological process | Lipid transport, Transport |
Function
Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling, probably acting through RAB5 and RAB11 activation. Also involved in endosome to trans-Golgi network retrograde transport. In complex with MON2 and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS, a transporter of Wnt morphogens in developing tissues. Participates in the formation of endosomal carriers that direct WLS trafficking back to Golgi, away from lysosomal degradation. Appears to be implicated in intercellular communication by negatively regulating the release of exosomes. The flippase activity towards membrane lipids and its role in membrane asymmetry remains to be proved. Required for the maintenance of neurite morphology and synaptic transmission (By similarity).
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.