Because of a lapse in government funding, the information on this website may not be up to date, transactions submitted via the website may not be processed, and the agency may not be able to respond to inquiries until appropriations are enacted. The NIH Clinical Center (the research hospital of NIH) is open. For more details about its operating status, please visit cc.nih.gov. Updates regarding government operating status and resumption of normal operations can be found at opm.gov.

NLM Logo

P-type ATPases MeSH Descriptor Data 2025


MeSH Heading
P-type ATPases
Tree Number(s)
D08.811.277.040.025.314
D12.776.157.530.813
D12.776.543.585.813
Unique ID
D000073779
RDF Unique Identifier
http://id.nlm.nih.gov/mesh/D000073779
Scope Note
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.
Entry Term(s)
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
Registry Numbers
EC 3.6.3.-
Previous Indexing
Adenosine Triphosphatases (1992-2017)
Public MeSH Note
2018
History Note
2018
Date Established
2018/01/01
Date of Entry
2017/07/11
Revision Date
2021/06/30
P-type ATPases Preferred
page delivered in 0.149s