Literature summary for 7.2.2.8 extracted from

Jayakanthan, S.; Braiterman, L.T.; Hasan, N.M.; Unger, V.M.; Lutsenko, S.
Human copper transporter ATP7B (Wilson disease protein) forms stable dimers in vitro and in cells (2017), J. Biol. Chem., 292, 18760-18774 .

Search for more literature for 7.2.2.8

Cloned(Commentary)

Cloned (Comment)	Organism
adenovirus-mediated expression in HEK293 cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structural model of a deletion mutant lacking the four N-terminal metal-binding domains	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of the four N-terminal metal-binding domains does not disrupt dimerization. Unlike the full-length ATP7B, the truncated protein is targeted primarily to vesicles	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
trans-Golgi network	the dimeric structure is retained during ATP7B trafficking between the intracellular compartments	Homo sapiens	5802	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
240000	-	and 480000, PAGE and gel filtration, streptavidin-tagged recombinant protein	Homo sapiens
480000	-	and 240000, PAGE and gel filtration, streptavidin-tagged recombinant protein	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35670	-	-

Purification (Commentary)

Purification (Comment)	Organism
in eukaryotic cells, human ATP7B forms dimers that can be purified following solubilization	Homo sapiens

Subunits

Subunits	Comment	Organism
dimer	and monomer, 2 * 230000, streptavidin-tagged recombinant protein, calculated from sequence	Homo sapiens
monomer	and dimer, 1 * 230000, streptavidin-tagged recombinant protein, calculated from sequence	Homo sapiens

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Release 2023.1 (January 2023)