P-type ATPases [ATPasy typu P]
- Terms
-
ATPasa typu P
ATPáza typu P
ATPázy typu P
E1-E2 ATPasa
E1-E2 ATPasy
E1-E2 ATPáza
E1-E2 ATPázy
P-ATPasa
P-ATPasy
P-ATPázy
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E1-E2 ATPase
E1-E2 ATPases
P Type Atpase
P-type Adenosine Triphosphatase
P-type Adenosine Triphosphatases
P-type ATPase
Phosphorylation-type Adenosine Triphosphatases
Phosphorylation-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.
- DUI
- D000073779 MeSH Browser
- CUI
- M000623906
- Previous indexing
- Adenosine Triphosphatases (1992-2017)
- History note
- 2018
- Public note
- 2018
Allowable subheadings
- AD
- administration & dosage
- AE
- adverse effects
- AN
- analysis
- AI
- antagonists & inhibitors
- BI
- biosynthesis
- BL
- blood
- CF
- cerebrospinal fluid
- CS
- chemical synthesis
- CH
- chemistry
- CL
- classification
- DF
- deficiency
- DE
- drug effects
- EC
- economics
- GE
- genetics
- HI
- history
- IM
- immunology
- IP
- isolation & purification
- ME
- metabolism
- PK
- pharmacokinetics
- PD
- pharmacology
- PH
- physiology
- PO
- poisoning
- RE
- radiation effects
- ST
- standards
- SD
- supply & distribution
- TU
- therapeutic use
- TO
- toxicity
- UL
- ultrastructure
- UR
- urine
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