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Literature summary for 7.2.2.9 extracted from

  • Dmitriev, O.Y.; Bhattacharjee, A.; Nokhrin, S.; Uhlemann, E.M.; Lutsenko, S.
    Difference in stability of the N-domain underlies distinct intracellular properties of the E1064A and H1069Q mutants of copper-transporting ATPase ATP7B (2011), J. Biol. Chem., 286, 16355-16362.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.9

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
E1064A the mutation abolishes ATP binding to the N-domain. In the cell, neither the stability nor targeting of mutant E1064A to the trans-Golgi network differs significantly from the wild type enzyme Homo sapiens
H1069Q thermolabile mutant with impaired ATP binding. The mutation greatly destabilizes protein both in vitro and in cells Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus trans-Golgi network Homo sapiens 5794
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P35670
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cu2+/in
-
 Homo sapiens ADP + phosphate + Cu2+/out
-
 ?

Synonyms

Synonyms Comment Organism
ATP7B
-
 Homo sapiens
copper-transporting ATPase
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction Wilson disease is caused by mutations in the Cu-transporting ATPase ATP7B Homo sapiens