A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting five functionally distinct domains: three cytoplasmic domains A, N, and P which contain the catalytic sites, and two transmembrane domains. The N domain phosphorylates the P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by the A domain. The phosphorylation and dephosphorylation cycles drive conformational changes in the protein between two states (E1 and E2), which allow the substrate to access the other side of the membrane.
P Type Atpases has been studied across 9 research domains including ⚡ Energy & Fatigue, 🦴 Bone & Joint, 🔥 Metabolic, 🫁 Liver & Detox, 🧠 Focus & Attention. The primary research focus is ⚡ Energy & Fatigue with 85% of studies addressing this area.
This evidence profile for P Type Atpases is generated deterministically from 300 PubMed-indexed studies. All data is corpus-verified with Merkle proofs. BiohacksAI does not provide medical advice. Always consult a healthcare professional before starting any supplement regimen.
Data source: PubMed/MEDLINE (NLM). Corpus version: current. Patent pending (EVE-PAT-2026-001). © 2026 Organiq Sweden AB.