| Post Translational Modifications | N-glycosylated. N-linked glycosylation can affect trafficking to the membrane and function. |
| Function | May act as a modulatory subunit rather than a functional channel. Unlike other P2XRs members, P2RX6 does not seem to form functional homotrimers. P2RX6 requires the presence of P2RX4 or P2RX2 to shuttle it to the plasma membrane where it may form functional heterotrimeric receptors at the plasma membrane. P2RX6 can be translocated to the nucleus and functions as a nuclear regulator of post-transcriptional modifications in neurons. |
| Protein Name | P2x Purinoceptor 6P2x6Atp ReceptorP2xmPurinergic ReceptorPurinergic Receptor P2x-Like 1 |
| Database Links | Reactome: R-HSA-139853Reactome: R-HSA-418346 |
| Cellular Localisation | Cell MembraneMulti-Pass Membrane ProteinEndoplasmic ReticulumNucleusNucleus Inner MembraneHeteromerization Of P2rx6 Subunits With Either P2rx2 Or P2rx4 Subunits Guides The P2rx6 Subunit To The Plasma MembraneMonomers Remain Anchored To The Endoplasmic Reticulum (Er) Membrane By The Hydrophobic N-Terminal EndMainly Expressed In The Cell Body Of The Hippocampal Neurons |
| Alternative Protein Names | P2x Purinoceptor 6 proteinP2x6 proteinAtp Receptor proteinP2xm proteinPurinergic Receptor proteinPurinergic Receptor P2x-Like 1 proteinP2RX6 proteinP2RXL1 proteinP2X6 protein |
Information sourced from Uniprot.org