TRPM7 — Transient receptor potential cation channel subfamily M member 7
TRPM7 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.
TRPM7's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | NK/T Cell Identity T cell maturation | AFTPH, ARHGAP17, ASXL2, ATF7IP, CALCOCO2, CD244, CLK3, GDI1 +24 more | |
| Macrophages | Endosomal Vesicle Trafficking Vesicular traficking | ADAM17, AP3B1, ARFGEF1, ARID1B, ARK2N, ASAP1, ATF6, ATP11A +48 more | View in SCUBA |
About the gene
| Synonyms | CHAK1, LTRPC7, TRP-PLIK |
|---|---|
| Chromosome | 15: 50552473-50686797 |
| Predicted location | Intracellular, Membrane |
| Essential gene | Yes |
| Protein class | Disease related genes, Enzymes, Essential proteins, FDA approved drug targets, Human disease related genes, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins, Transporters, Voltage-gated ion channels |
| Molecular function | Calcium channel, Ion channel, Kinase, Serine/threonine-protein kinase, Transferase |
| Biological process | Calcium transport, Ion transport, Necrosis, Transport |
Function
Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx. Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7. In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions. The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.