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Literature summary extracted from

  • Huang, Y.; Nokhrin, S.; Hassanzadeh-Ghassabeh, G.; Yu, C.H.; Yang, H.; Barry, A.N.; Tonelli, M.; Markley, J.L.; Muyldermans, S.; Dmitriev, O.Y.; Lutsenko, S.
    Interactions between metal-binding domains modulate intracellular targeting of Cu(I)-ATPase ATP7B, as revealed by nanobody binding (2014), J. Biol. Chem., 289, 32682-32693.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.8 recombinant expression of the N-terminal domain of human ATP7B (N-ATP7B) fused to maltose-binding protein, and FLAG-tagged enzyme in HEK293T-Rex cells, co-expression of GFP-tagged nanoparticle in HEK-293T cells, the nanobodies bind to the distinct regions of N-ATP7B, binding sites of 2R50 and 2R51 are located within metal binding domains MBD1-4, revealing transient inter-domain interactions in N-ATP7B Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.8 membrane
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Homo sapiens 16020
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7.2.2.8 additional information copper regulates the intracellular localization of copper transporter ATP7B, transient interactions between the N-terminal metal-binding domains and modulated intracellular localization of ATP7B, molecular mechanism Homo sapiens
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7.2.2.8 plasma membrane
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Homo sapiens 5886
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7.2.2.8 trans-Golgi network upon copper elevation, ATP7B moves from the trans-Golgi network to specialized vesicles, following copper depletion, ATP7B returns from vesicles to the trans-Golgi network Homo sapiens 5802
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7.2.2.8 vesicle upon copper elevation, ATP7B moves from the trans-Golgi network to specialized vesicles, following copper depletion, ATP7B returns from vesicles to the trans-Golgi network Homo sapiens 31982
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.8 ATP + H2O + Cu+[side 1] Homo sapiens ATP hydrolysis supplies energy for copper transport ADP + phosphate + Cu+[side 2]
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Organism

EC Number Organism UniProt Comment Textmining
7.2.2.8 Homo sapiens P35670 ATP7B
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.8 ATP + H2O + Cu+[side 1] ATP hydrolysis supplies energy for copper transport Homo sapiens ADP + phosphate + Cu+[side 2]
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7.2.2.8 ATP + H2O + Cu+[side 1] metal ion binding to the N-terminal copper-sensing domain of ATP7B Homo sapiens ADP + phosphate + Cu+[side 2]
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Synonyms

EC Number Synonyms Comment Organism
7.2.2.8 ATP7B
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Homo sapiens
7.2.2.8 Cu(I)-ATPase
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Homo sapiens
7.2.2.8 Cu(I)-transporting ATPase
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Homo sapiens

General Information

EC Number General Information Comment Organism
7.2.2.8 malfunction the loss of ATP7B activity is associated with Wilson disease, a severe hepato-neurological disorder Homo sapiens
7.2.2.8 additional information identification of spatial organization of N-terminal enzyme domain of ATP7B and transient functionally relevant interactions between metal-binding domains 1-3, modulation of these interactions by nanobodies in cells enhances relocalization of the endogenous enzyme toward the plasma membrane linking molecular and cellular dynamics of the transporter. Stimulation of enzyme trafficking by nanobodies in the absence of elevated copper provides direct evidence for the important role of the N-terminal enzyme domains structural dynamics in regulation of enzyme localization in a cell Homo sapiens
7.2.2.8 physiological function human Cu(I)-transporting ATPase ATP7B plays an essential role in maintaining cellular copper homeostasis. The enzyme transports copper to metalloenzymes undergoing functional maturation in this compartment. ATP hydrolysis supplies energy for copper transport. Upon copper elevation, enzyme ATP7B moves from the trans-Golgi network to specialized vesicles. In the vesicles, ATP7B sequesters excess copper for further export, which occurs via vesicle fusion at the plasma membrane. Following copper depletion, ATP7B returns from vesicles to the trans-Golgi network to resume its function in the biosynthesis of cuproenzymes. Role for domain dynamics in ATP7B trafficking Homo sapiens