Chemicals and Drugs

P-type ATPases

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.

National Library of MedicineMedical Subject Headings2026

Structured Summary

Abstract

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.

MeSH Record

Classification

Broader headings

Narrower headings

Related Concepts

Knowledge Graph

Loading graph…

Drag nodes to rearrange; hover to trace links; click a node to open its page.

MeSH Record

Synonyms

28 entry terms
  • E1-E2 ATPase
  • E1-E2 ATPases
  • P Type Atpase
  • P-type ATPase
  • P-type Adenosine Triphosphatase
  • P-type Adenosine Triphosphatases
  • Phosphorylation-type ATPases
  • Phosphorylation-type Adenosine Triphosphatases
  • ATPase, E1-E2
  • ATPase, P-type
  • ATPases, E1-E2
  • ATPases, P-type
  • ATPases, Phosphorylation-type
  • Adenosine Triphosphatase, P-type
  • Adenosine Triphosphatases, P-type
  • Adenosine Triphosphatases, Phosphorylation-type
  • Atpase, P Type
  • E1 E2 ATPase
  • E1 E2 ATPases
  • P type ATPases
  • P type Adenosine Triphosphatase
  • P type Adenosine Triphosphatases
  • Phosphorylation type ATPases
  • Phosphorylation type Adenosine Triphosphatases
  • Triphosphatase, P-type Adenosine
  • Triphosphatases, P-type Adenosine
  • Triphosphatases, Phosphorylation-type Adenosine
  • Type Atpase, P

MeSH Record

Aspects Covered

29 allowable subheadings

Indexed with the subheadings administration & dosage, adverse effects, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.

MeSH Record

History Note

2018

MeSH Record

Previous Indexing

  • Adenosine Triphosphatases (1992-2017)

MeSH Hierarchy

Tree Numbers

  1. D08.811w.277w.040w.025w.314w
  2. D12.776w.157w.530w.813w
  3. D12.776w.543w.585w.813w

AMA Style

References

  1. National Library of Medicine. P-type ATPases. Medical Subject Headings (MeSH). 2026. Unique ID D000073779. http://id.nlm.nih.gov/mesh/2026/D000073779
  2. P-type ATPases. In: Wikipedia. https://en.wikipedia.org/wiki/P-type_ATPase
  3. P-type ATPases. In: Wikidata. https://www.wikidata.org/wiki/Q11903647