Falcon deep research report for human ATP7B

Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene.

Functional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant?

Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity.

Copper-induced trafficking of the cU-ATPases: a key mechanism for copper homeostasis.

Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1.

The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein.

Binding of copper(I) by the Wilson disease protein and its copper chaperone.

The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F.

Signals regulating trafficking of Menkes (MNK; ATP7A) copper-translocating P-type ATPase in polarized MDCK cells.

The Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 protein.

ATP7B mediates vesicular sequestration of copper: insight into biliary copper excretion.

Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A.

Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations.

A new hepatocytic isoform of PLZF lacking the BTB domain interacts with ATP7B, the Wilson disease protein, and positively regulates ERK signal transduction.

Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases.

Copper binding to the N-terminal metal-binding sites or the CPC motif is not essential for copper-induced trafficking of the human Wilson protein (ATP7B).

Distinct Wilson's disease mutations in ATP7B are associated with enhanced binding to COMMD1 and reduced stability of ATP7B.

Defining the membrane proteome of NK cells.

Diverse functional properties of Wilson disease ATP7B variants.

Functional characterization of new mutations in Wilson disease gene (ATP7B) using the yeast model.

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

Ion transport by P-type ATPases

ATP7B transports cytosolic Cu1+ to Golgi lumen

UniProtKB P35670 (ATP7B_HUMAN), copper-transporting ATPase 2

Regulation of the apico-basolateral trafficking polarity of the homologous copper-ATPases ATP7A and ATP7B.

Localization of the Wilson's disease protein product to mitochondria.