PROSITE documentation PDOC00139
P-type ATPases phosphorylation site
Description
P-type ATPases (also known as E1-E2) are cation transport ATPases which form
an aspartyl phosphate intermediate in the course of ATP hydrolysis. ATPases
which belong to this family are listed below [1 ,2 ,3 ].
Fungal and plant plasma membrane (H+) ATPases (EC 3.6.3.6 ).
Vertebrate (Na+, K+) ATPases (sodium pump) (EC 3.6.3.9 ).
Gastric (K+, H+) ATPases (proton pump) (EC 3.6.3.10 ).
Calcium (Ca++) ATPases (calcium pump) (EC 3.6.3.8 ) from the sarcoplasmic
reticulum (SR), the endoplasmic reticulum (ER) and the plasma membrane.
Copper (Cu++) ATPases (copper pump) (EC 3.6.3.4 ) which are involved in two
human genetic disorders: Menkes syndrome and Wilson disease.
Bacterial cadmium efflux (Cd++) ATPases (EC 3.6.3.3 ).
Bacterial magnesium (Mg++) ATPases (EC 3.6.3.2 ).
Bacterial potassium (K+) ATPases (EC 3.6.3.12 ).
Bacterial zinc (Zn+) ATPases (EC 3.6.3.5 ).
Fungal ENA sodium ATPases (EC 3.6.3.7 ).
fixI, a probable cation ATPase from Rhizobacea, involved in nitrogen
fixation.
The region around the phosphorylated aspartate residue is perfectly conserved
in all these ATPases and can be used as a signature pattern.
Last update:
November 2002 / Text revised.
Expert(s) to contact by email:
Axelsen K.B.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
ATPASE_E1_E2, PS00154 ; E1-E2 ATPases phosphorylation site (PATTERN)
References
1 Authors Fagan M.J. Saier M.H. Jr.
Title P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees.
Source J. Mol. Evol. 38:57-99(1994).
PubMed ID 8151716
2 Authors Palmgren M.G. Axelsen K.B.
Title Evolution of P-type ATPases.
Source Biochim. Biophys. Acta 1365:37-45(1998).
PubMed ID 9693719
3 Authors Axelsen K.B. Palmgren M.G.
Title Evolution of substrate specificities in the P-type ATPase superfamily.
Source J. Mol. Evol. 46:84-101(1998).
PubMed ID 9419228
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