| Descriptor English: | P-type ATPases | ||||||
| Descriptor Spanish: |
ATPasas Tipo P
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| Descriptor Portuguese: | ATPases do Tipo-P | ||||||
| Descriptor French: | P-type ATPases | ||||||
| Entry term(s): |
ATPase, P-type ATPases, E1-E2 ATPases, P-type ATPases, Phosphorylation-type Adenosine Triphosphatase, P-type Adenosine Triphosphatases, P-type Adenosine Triphosphatases, Phosphorylation-type E1 E2 ATPases E1-E2 ATPase E1-E2 ATPases P Type Atpase P type ATPase P type ATPases P type Adenosine Triphosphatase P type Adenosine Triphosphatases P-type ATPase P-type Adenosine Triphosphatase P-type Adenosine Triphosphatases Phosphorylation type ATPases Phosphorylation type Adenosine Triphosphatases Phosphorylation-type ATPases Phosphorylation-type Adenosine Triphosphatases Triphosphatase, P-type Adenosine Triphosphatases, P-type Adenosine Triphosphatases, Phosphorylation-type Adenosine |
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| Tree number(s): |
D08.811.277.040.025.314 D12.776.157.530.813 D12.776.543.585.813 |
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| RDF Unique Identifier: | https://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. |
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| Allowable Qualifiers: |
AD administration & dosage AE adverse effects AI antagonists & inhibitors AN analysis BI biosynthesis BL blood CF cerebrospinal fluid CH chemistry CL classification CS chemical synthesis DE drug effects DF deficiency EC economics GE genetics HI history IM immunology IP isolation & purification ME metabolism PD pharmacology PH physiology PK pharmacokinetics PO poisoning RE radiation effects SD supply & distribution ST standards TO toxicity TU therapeutic use UL ultrastructure UR urine |
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| Registry Number: | EC 3.6.3.- | ||||||
| Previous Indexing: |
Adenosine Triphosphatases (1992-2017) |
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| Public MeSH Note: | 2018 |
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| History Note: | 2018 |
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| DeCS ID: | 56997 | ||||||
| Unique ID: | D000073779 | ||||||
| Documents indexed in the Virtual Health Library (VHL): | Click here to access the VHL documents | ||||||
| Date Established: | 2018/01/01 | ||||||
| Date of Entry: | 2017/07/11 | ||||||
| Revision Date: | 2020/05/27 |
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CHEMICALS AND DRUGS
Enzymes and Coenzymes [D08]Enzymes and Coenzymes -
CHEMICALS AND DRUGS
Amino Acids, Peptides, and Proteins [D12]Amino Acids, Peptides, and Proteins -
CHEMICALS AND DRUGS
Amino Acids, Peptides, and Proteins [D12]Amino Acids, Peptides, and Proteins
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P-type ATPases
- Preferred
| Concept UI |
M000623906 |
| 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. |
| Preferred term | P-type ATPases |
| Entry term(s) |
ATPase, P-type ATPases, E1-E2 ATPases, P-type ATPases, Phosphorylation-type Adenosine Triphosphatase, P-type Adenosine Triphosphatases, P-type Adenosine Triphosphatases, Phosphorylation-type E1 E2 ATPases E1-E2 ATPase E1-E2 ATPases P Type Atpase P type ATPase P type ATPases P type Adenosine Triphosphatase P type Adenosine Triphosphatases P-type ATPase P-type Adenosine Triphosphatase P-type Adenosine Triphosphatases Phosphorylation type ATPases Phosphorylation type Adenosine Triphosphatases Phosphorylation-type ATPases Phosphorylation-type Adenosine Triphosphatases Triphosphatase, P-type Adenosine Triphosphatases, P-type Adenosine Triphosphatases, Phosphorylation-type Adenosine |
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