Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

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

Functional analysis of the N-terminal CXXC metal-binding motifs in the human Menkes copper-transporting P-type ATPase expressed in cultured mammalian cells.

The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal.

Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p.

Expression of menkes copper-transporting ATPase, MNK, in the lactating human breast: possible role in copper transport into milk.

The Menkes copper transporter is required for the activation of tyrosinase.

The Menkes disease ATPase (ATP7A) is internalized via a Rac1-regulated, clathrin- and caveolae-independent pathway.

Structure and metal binding studies of the second copper binding domain of the Menkes ATPase.

Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A.

An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.

A single PDZ domain protein interacts with the Menkes copper ATPase, ATP7A. A new protein implicated in copper homeostasis.

Essential role for the Menkes ATPase in activation of extracellular superoxide dismutase: implication for vascular oxidative stress.

Alteration of copper physiology in mice overexpressing the human Menkes protein ATP7A.

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

The binding mode of ATP revealed by the solution structure of the N-domain of human ATP7A.

Defining the membrane proteome of NK cells.

The copper-transporting capacity of ATP7A mutants associated with Menkes disease is ameliorated by COMMD1 as a result of improved protein expression.

A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport.

Neuronal copper homeostasis susceptibility by genetic defects in dysbindin, a schizophrenia susceptibility factor.

Multiple di-leucines in the ATP7A copper transporter are required for retrograde trafficking to the trans-Golgi network.

Characterization of ATP7A missense mutants suggests a correlation between intracellular trafficking and severity of Menkes disease.

Mechanistic and Structural Basis for Inhibition of Copper Trafficking by Platinum Anticancer Drugs.

Biochemical characterization and intracellular localization of the Menkes disease protein.

Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network.

Constitutive skipping of alternatively spliced exon 10 in the ATP7A gene abolishes Golgi localization of the menkes protein and produces the occipital horn syndrome.

A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network.

ATP7A transports cytosolic Cu2+ to phagosomal lumen

ATP7A transports cytosolic Cu1+ to extracellular region