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 (PubMed:14576148, PubMed:16636202, PubMed:18258429, PubMed:18365021). Crucial for Mg(2+) homeostasis. Has an important role in epithelial Mg(2+) transport and in the active Mg(2+) absorption in the gut and kidney (PubMed:14576148). However, whether TRPM6 forms functional homomeric channels by itself or functions primarily as a subunit of heteromeric TRPM6-TRPM7 channels, is still under debate (PubMed:14576148, PubMed:16636202, PubMed:24385424). {ECO:0000269|PubMed:14576148, ECO:0000269|PubMed:16636202, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18365021, ECO:0000269|PubMed:24385424}. [TRPM6 kinase, cleaved form]: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and development. . This is the function of Ensembl gene identifier ENSG00000119121 (TRPM6, transient receptor potential cation channel subfamily M member 6).