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Entry version 234 (02 Jun 2021)
Sequence version 4 (12 Sep 2018)
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Protein

Copper-transporting ATPase 1

Gene

ATP7A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

ATP-driven copper (Cu+) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643).

Within a catalytic cycle, acquires Cu+ ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu+ ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:31283225, PubMed:28389643).

Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu+ ions to cuproenzymes of the secretory pathway (PubMed:28389643, PubMed:11092760).

Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu+ ions (PubMed:10419525, PubMed:28389643).

May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu+ ions to enzymes such as PAM, TYR and SOD3 (PubMed:28389643) (By similarity).

In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity).

By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=4 µM for Cu+ ion1 Publication
  1. Vmax=1.15 nmol/min/mg enzyme toward Cu+ ion1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi18CopperCombined sources1 Publication1
Metal bindingi19Copper; via amino nitrogenCombined sources1 Publication1
Metal bindingi22CopperCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei10444-aspartylphosphate intermediateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1081ATP1 Publication1
Metal bindingi1301MagnesiumPROSITE-ProRule annotation1
Metal bindingi1305MagnesiumPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processCopper transport, Ion transport, Transport
LigandATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
7.2.2.8, 2681
7.2.2.9, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q04656

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3299685, Detoxification of Reactive Oxygen Species
R-HSA-6803544, Ion influx/efflux at host-pathogen interface
R-HSA-936837, Ion transport by P-type ATPases

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q04656

Protein family/group databases

Transport Classification Database

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TCDBi
3.A.3.5.6, the p-type atpase (p-atpase) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Copper-transporting ATPase 1 (EC:7.2.2.81 Publication1 Publication)
Alternative name(s):
Copper pump 1
Menkes disease-associated protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATP7A1 PublicationImported
Synonyms:MC1, MNK
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:869, ATP7A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300011, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q04656

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000165240.17

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 653CytoplasmicSequence analysisAdd BLAST653
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei654 – 675HelicalSequence analysisAdd BLAST22
Topological domaini676 – 714ExtracellularSequence analysisAdd BLAST39
Transmembranei715 – 734HelicalSequence analysisAdd BLAST20
Topological domaini735 – 741CytoplasmicSequence analysis7
Transmembranei742 – 762HelicalSequence analysisAdd BLAST21
Topological domaini763 – 781ExtracellularSequence analysisAdd BLAST19
Transmembranei782 – 802HelicalSequence analysisAdd BLAST21
Topological domaini803 – 936CytoplasmicSequence analysisAdd BLAST134
Transmembranei937 – 959HelicalSequence analysisAdd BLAST23
Topological domaini960 – 989ExtracellularSequence analysisAdd BLAST30
Transmembranei990 – 1011HelicalSequence analysisAdd BLAST22
Topological domaini1012 – 1356CytoplasmicSequence analysisAdd BLAST345
Transmembranei1357 – 1374HelicalSequence analysisAdd BLAST18
Topological domaini1375 – 1385ExtracellularSequence analysisAdd BLAST11
Transmembranei1386 – 1405HelicalSequence analysisAdd BLAST20
Topological domaini1406 – 1500CytoplasmicSequence analysisAdd BLAST95

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Menkes disease (MNK)11 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes. A mild form of the disease has been described, in which cerebellar ataxia and moderate developmental delay predominate.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_084344628E → V in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_000699629A → P in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554639EnsemblClinVar.1
Natural variantiVAR_084345633K → R in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_084346653S → Y in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_084347666G → R in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs797045344EnsemblClinVar.1
Natural variantiVAR_023261706L → R in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554642Ensembl.1
Natural variantiVAR_000700727G → R in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 PublicationsCorresponds to variant dbSNP:rs72554644EnsemblClinVar.1
Natural variantiVAR_084348728G → D in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs797045350EnsemblClinVar.1
Natural variantiVAR_084349761S → P in MNK; has no effect on copper-dependent trafficking from TGN to post-TGN compartments; impaired copper transport activity. 1 Publication1
Natural variantiVAR_084350802K → N in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_023262844R → H in MNK; loss of protein expression. 2 PublicationsCorresponds to variant dbSNP:rs367775730EnsemblClinVar.1
Natural variantiVAR_023263853G → R in MNK. 1 Publication1
Natural variantiVAR_023264860G → V in MNK; decreased protein abundance; impaired copper transport activity. 2 Publications1
Natural variantiVAR_010001873L → R in MNK; increased protein abundance; does not affect interaction with ATOX1; does not affect interaction with COMMD1; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion. 2 PublicationsCorresponds to variant dbSNP:rs72554646Ensembl.1
Natural variantiVAR_010002876G → E in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 2 Publications1
Natural variantiVAR_023265876G → R in MNK; loss of protein expression. 2 Publications1
Natural variantiVAR_0100031000C → R in MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity. 3 Publications1
Natural variantiVAR_0843511005G → R in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs1569550143EnsemblClinVar.1
Natural variantiVAR_0007011006L → P in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554651Ensembl.1
Natural variantiVAR_0232671007A → V in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0232681015G → D in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0007021019G → D in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554652EnsemblClinVar.1
Natural variantiVAR_0843521037K → N in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_0232691044D → G in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0688311048T → I in MNK. 1 Publication1
Natural variantiVAR_0232701100L → P in MNK. 1 Publication1
Natural variantiVAR_0232711118G → D in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554654Ensembl.1
Natural variantiVAR_0232721255G → R in MNK; decreased protein abundance; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 PublicationsCorresponds to variant dbSNP:rs72554655Ensembl.1
Natural variantiVAR_0232731282K → E in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0100041300G → E in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0843531301D → G in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs1557238588EnsemblClinVar.1
Natural variantiVAR_0843541302G → E in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0100051302G → R in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554657Ensembl.1
Natural variantiVAR_0100061302G → V in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0232741304N → K in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0100071305D → A in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0843551305D → G in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0843561308A → D in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0232751315G → R in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 PublicationsCorresponds to variant dbSNP:rs797045390EnsemblClinVar.1
Natural variantiVAR_0232761325A → V in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0232771344S → R in MNK. 1 Publication1
Natural variantiVAR_0232781345I → F in MNK. 1 Publication1
Natural variantiVAR_0100081362A → V in MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity. 3 Publications1
Natural variantiVAR_0232791369G → R in MNK; loss of protein expression. 2 Publications1
Natural variantiVAR_0843571373A → P in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_0843581393M → T in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0232801397S → F in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Occipital horn syndrome (OHS)5 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities include occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_009999637S → L in OHS. 1 PublicationCorresponds to variant dbSNP:rs151340631EnsemblClinVar.1
Natural variantiVAR_023266924Q → R in OHS; has no effect on copper-dependent trafficking; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0638831304N → S in OHS; has approximately 33% residual copper transport; increased protein abundance; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion; does not affect interaction with ATOX1; does not affect interaction with COMMD1. 2 PublicationsCorresponds to variant dbSNP:rs151340632EnsemblClinVar.1
Distal spinal muscular atrophy, X-linked, 3 (DSMAX3)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063882994T → I in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some of the mutant protein remaining in the Golgi apparatus after exposure to copper. 1 PublicationCorresponds to variant dbSNP:rs267606673EnsemblClinVar.1
Natural variantiVAR_0638841386P → S in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper. 1 PublicationCorresponds to variant dbSNP:rs267606672EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi22C → A: Impairs Cu(+)-bridged heterodimer formation with ATOX1 while increasing the reactivity toward cisplatin. 1 Publication1
Mutagenesisi1044D → E: Impairs tyrosinase activity involved in melanin synthesis. 1 Publication1
Mutagenesisi1487 – 1488LL → AA: Loss of relocalization to the trans-Golgi. 1 Publication2

Keywords - Diseasei

Disease variant, Neurodegeneration

Organism-specific databases

DisGeNET

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DisGeNETi
538

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ATP7A

MalaCards human disease database

More...
MalaCardsi
ATP7A
MIMi300489, phenotype
304150, phenotype
309400, phenotype

Open Targets

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OpenTargetsi
ENSG00000165240

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
565, Menkes disease
198, Occipital horn syndrome
139557, X-linked distal spinal muscular atrophy type 3

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA72

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q04656, Tbio

Chemistry databases

Drug and drug target database

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DrugBanki
DB00958, Carboplatin
DB00515, Cisplatin
DB09130, Copper
DB00526, Oxaliplatin

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ATP7A

Domain mapping of disease mutations (DMDM)

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DMDMi
223590241

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000463111 – 1500Copper-transporting ATPase 1Add BLAST1500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei152PhosphothreonineCombined sources1
Modified residuei270PhosphoserineCombined sources1
Modified residuei327PhosphothreonineCombined sources1
Modified residuei339PhosphoserineCombined sources1
Modified residuei353PhosphoserineBy similarity1
Modified residuei357PhosphoserineCombined sources1
Modified residuei362PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi686N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi975N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1212PhosphothreonineBy similarity1
Modified residuei1430PhosphoserineCombined sources1
Modified residuei1432PhosphoserineCombined sources1
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1463PhosphoserineCombined sources1
Modified residuei1466PhosphoserineCombined sources1
Modified residuei1469PhosphoserineCombined sources1
Modified residuei1473PhosphoserineCombined sources1
Modified residuei1476PhosphoserineBy similarity1
Modified residuei1486PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q04656

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q04656

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q04656

PeptideAtlas

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PeptideAtlasi
Q04656

PRoteomics IDEntifications database

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PRIDEi
Q04656

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
58255 [Q04656-1]
58256 [Q04656-2]
58257 [Q04656-3]
58258 [Q04656-4]
58259 [Q04656-5]
58260 [Q04656-6]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
Q04656, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q04656

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q04656

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed including in heart, brain, lung, muscle, kidney, pancreas, and to a lesser extent placenta (PubMed:8490646, PubMed:8490659). Expressed in fibroblasts, aortic smooth muscle cells, aortic endothelial cells and umbilical vein endothelial cells (at protein level) (PubMed:16371425).3 Publications
Expressed in cerebellum and brain cortex.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000165240, Expressed in oviduct epithelium and 232 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q04656, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q04656, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000165240, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Interacts with PDZD11 (PubMed:16051599).

Interacts with ATOX1 and COMMD1 (PubMed:21667063, PubMed:19453293, PubMed:31283225).

Interacts with TYRP1 (By similarity).

Interacts with SOD3; this interaction is copper-dependent and is required for SOD3 activity.

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
107020, 53 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q04656

Protein interaction database and analysis system

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IntActi
Q04656, 20 interactors

Molecular INTeraction database

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MINTi
Q04656

STRING: functional protein association networks

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STRINGi
9606.ENSP00000345728

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q04656, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

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BMRBi
Q04656

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q04656

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q04656

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini9 – 75HMA 1PROSITE-ProRule annotationAdd BLAST67
Domaini172 – 238HMA 2PROSITE-ProRule annotationAdd BLAST67
Domaini278 – 344HMA 3PROSITE-ProRule annotationAdd BLAST67
Domaini378 – 444HMA 4PROSITE-ProRule annotationAdd BLAST67
Domaini489 – 555HMA 5PROSITE-ProRule annotationAdd BLAST67
Domaini565 – 631HMA 6PROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1486 – 1500PDZD11-bindingAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1467 – 1468Endocytosis signalBy similarity2
Motifi1487 – 1488Endocytosis signalBy similarity2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The nucleotide-binding domain consists of a twisted six-stranded antiparallel beta-sheet flanked by two pairs of alpha-helices, forming an hydrophobic pocket that interacts with the adenine ring of ATP. The ATP binding site comprises residues located in alpha-1 and alpha-2 helices and beta-2 and beta-3 strands, which are involved in van der Waal's interactions, and Glu-1081 which forms an hydrogen bond with the adenine ring.1 Publication
The heavy-metal-associated domain (HMA) coordinates a Cu+ ion via the cysteine residues within the CXXC motif. The transfer of Cu+ ion from ATOX1 to ATP7A involves the formation of a three-coordinate Cu+-bridged heterodimer where the metal is shared between the two metal binding sites of ATOX1 and ATP7A. The Cu+ ion appears to switch between two coordination modes, forming two links with one protein and one with the other. Cisplatin, a chemotherapeutic drug, can bind the CXXC motif and hinder the release of Cu+ ion.3 Publications
Contains three di-leucine motifs in the C-terminus which are required for recycling from the plasma membrane to the TGN. The di-leucine 1487-Leu-Leu-1488 motif mediates endocytosis at the plasma membrane, whereas the di-leucine 1467-Leu-Leu-1468 motif is a sorting signal for retrograde trafficking to TGN via early endosomes.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0207, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000159568

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_001771_0_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q04656

Identification of Orthologs from Complete Genome Data

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OMAi
KTGYEAR

Database of Orthologous Groups

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OrthoDBi
649559at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q04656

TreeFam database of animal gene trees

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TreeFami
TF300460

Family and domain databases

Conserved Domains Database

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CDDi
cd00371, HMA, 6 hits

Database of protein disorder

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DisProti
DP00282

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.1110.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR023299, ATPase_P-typ_cyto_dom_N
IPR018303, ATPase_P-typ_P_site
IPR023298, ATPase_P-typ_TM_dom_sf
IPR008250, ATPase_P-typ_transduc_dom_A_sf
IPR036412, HAD-like_sf
IPR017969, Heavy-metal-associated_CS
IPR006122, HMA_Cu_ion-bd
IPR006121, HMA_dom
IPR036163, HMA_dom_sf
IPR027256, P-typ_ATPase_IB
IPR001757, P_typ_ATPase
IPR044492, P_typ_ATPase_HD_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00403, HMA, 6 hits

Structure-Function Linkage Database

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SFLDi
SFLDF00027, p-type_atpase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55008, SSF55008, 6 hits
SSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01525, ATPase-IB_hvy, 1 hit
TIGR01494, ATPase_P-type, 2 hits
TIGR00003, TIGR00003, 6 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154, ATPASE_E1_E2, 1 hit
PS01047, HMA_1, 6 hits
PS50846, HMA_2, 6 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 4 (identifier: Q04656-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI
60 70 80 90 100
IYDPKLQTPK TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW
110 120 130 140 150
DHIQSTLLKT KGVTDIKIYP QKRTVAVTII PSIVNANQIK ELVPELSLDT
160 170 180 190 200
GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM TCHSCTSTIE GKIGKLQGVQ
210 220 230 240 250
RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK QPKYLKLGAI
260 270 280 290 300
DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS
310 320 330 340 350
ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE
360 370 380 390 400
VESTSNSPSS SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS
410 420 430 440 450
KKPGVKSIRV SLANSNGTVE YDPLLTSPET LRGAIEDMGF DATLSDTNEP
460 470 480 490 500
LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD KEEGKNSSKC YIQVTGMTCA
510 520 530 540 550
SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP MIAEFIRELG
560 570 580 590 600
FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA
610 620 630 640 650
TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW
660 670 680 690 700
RRSFLVSLFF CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF
710 720 730 740 750
LERQILPGLS VMNLLSFLLC VPVQFFGGWY FYIQAYKALK HKTANMDVLI
760 770 780 790 800
VLATTIAFAY SLIILLVAMY ERAKVNPITF FDTPPMLFVF IALGRWLEHI
810 820 830 840 850
AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE LVQRGDIIKV
860 870 880 890 900
VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL
910 920 930 940 950
LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI
960 970 980 990 1000
ATLLVWIVIG FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC
1010 1020 1030 1040 1050
PCSLGLATPT AVMVGTGVGA QNGILIKGGE PLEMAHKVKV VVFDKTGTIT
1060 1070 1080 1090 1100
HGTPVVNQVK VLTESNRISH HKILAIVGTA ESNSEHPLGT AITKYCKQEL
1110 1120 1130 1140 1150
DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN NIKNASLVQI
1160 1170 1180 1190 1200
DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN
1210 1220 1230 1240 1250
DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV
1260 1270 1280 1290 1300
VLMTGDNSKT ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG
1310 1320 1330 1340 1350
DGINDSPALA MANVGIAIGT GTDVAIEAAD VVLIRNDLLD VVASIDLSRK
1360 1370 1380 1390 1400
TVKRIRINFV FALIYNLVGI PIAAGVFMPI GLVLQPWMGS AAMAASSVSV
1410 1420 1430 1440 1450
VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI DDTSRNSPKL
1460 1470 1480 1490 1500
GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL
Length:1,500
Mass (Da):163,373
Last modified:September 12, 2018 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA54F17EA08FDACDB
GO
Isoform 1 (identifier: Q04656-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKLSIRKRDNNLLK

Show »
Length:1,514
Mass (Da):165,109
Checksum:iDE3F394729A20182
GO
Isoform 2 (identifier: Q04656-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKLSIRKRD...EELAVHNECY

Show »
Length:1,581
Mass (Da):172,077
Checksum:i9722FE40213776AB
GO
Isoform 3 (identifier: Q04656-4) [UniParc]FASTAAdd to basket
Also known as: 2-16

The sequence of this isoform differs from the canonical sequence as follows:
     42-1038: Missing.

Note: Lacks 6 transmembrane regions and 5 heavy-metal-associated (HMA) domains.Curated
Show »
Length:503
Mass (Da):54,317
Checksum:iD2DBF19FF5E052D2
GO
Isoform 5 (identifier: Q04656-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     725-802: Missing.

Note: Lacks the transmembrane domains 3 and 4. Expressed at a low level in several tissues of normal individuals and is the only isoform found in patients with OHS.Curated
Show »
Length:1,422
Mass (Da):154,356
Checksum:i8477AEB5F864F2F3
GO
Isoform 6 (identifier: Q04656-6) [UniParc]FASTAAdd to basket
Also known as: NML45

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKLSIRKRDNNLLKECNEEIK
     53-81: DPKLQTPKTLQEAIDDMGFDAVIHNPDPL → AHWFGFAALDGICSNGCFICFCSTFFSSL
     82-1499: Missing.

Note: Lacks all transmembrane regions and 5 heavy-metal-associated (HMA) domains, but has a putative nuclear localization signal attached at the N-terminus.Curated
Show »
Length:103
Mass (Da):11,522
Checksum:i1F3873EFB0EA6CC2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8YD60A0A2R8YD60_HUMAN
Copper-transporting ATPase 1
ATP7A
49Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti10V → A no nucleotide entry (PubMed:9693104).Curated1
Sequence conflicti36V → E in AAA16974 (PubMed:8490647).Curated1
Sequence conflicti336E → V in AAA35580 (PubMed:8490659).Curated1
Sequence conflicti336E → V in AAA96010 (PubMed:7490081).Curated1
Sequence conflicti446D → G in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti624S → G in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti725F → V in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti833S → R in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti1099E → K no nucleotide entry (PubMed:9693104).Curated1
Sequence conflicti1171N → S in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti1178Y → C no nucleotide entry (PubMed:9693104).Curated1
Sequence conflicti1178Y → H in AAA35580 (PubMed:8490659).Curated1
Sequence conflicti1178Y → H in CAB94714 (PubMed:7607665).Curated1
Sequence conflicti1178Y → H in AAA96010 (PubMed:7490081).Curated1
Sequence conflicti1220D → G in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti1295R → W no nucleotide entry (PubMed:9693104).Curated1
Sequence conflicti1313N → D no nucleotide entry (PubMed:9693104).Curated1
Sequence conflicti1336N → D in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti1376V → M in CAB08162 (PubMed:15772651).Curated1
Sequence conflicti1396S → P no nucleotide entry (PubMed:9693104).Curated1
Sequence conflicti1409L → R in CAB08160 (PubMed:15772651).Curated1
Sequence conflicti1455R → W no nucleotide entry (PubMed:9693104).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_084344628E → V in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_000699629A → P in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554639EnsemblClinVar.1
Natural variantiVAR_084345633K → R in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_009999637S → L in OHS. 1 PublicationCorresponds to variant dbSNP:rs151340631EnsemblClinVar.1
Natural variantiVAR_084346653S → Y in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_084347666G → R in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs797045344EnsemblClinVar.1
Natural variantiVAR_016119669I → T2 PublicationsCorresponds to variant dbSNP:rs2234935EnsemblClinVar.1
Natural variantiVAR_016120703R → H. Corresponds to variant dbSNP:rs2234936Ensembl.1
Natural variantiVAR_023261706L → R in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554642Ensembl.1
Natural variantiVAR_000700727G → R in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 PublicationsCorresponds to variant dbSNP:rs72554644EnsemblClinVar.1
Natural variantiVAR_084348728G → D in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs797045350EnsemblClinVar.1
Natural variantiVAR_084349761S → P in MNK; has no effect on copper-dependent trafficking from TGN to post-TGN compartments; impaired copper transport activity. 1 Publication1
Natural variantiVAR_010000767V → L1 PublicationCorresponds to variant dbSNP:rs2227291EnsemblClinVar.1
Natural variantiVAR_084350802K → N in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_023262844R → H in MNK; loss of protein expression. 2 PublicationsCorresponds to variant dbSNP:rs367775730EnsemblClinVar.1
Natural variantiVAR_023263853G → R in MNK. 1 Publication1
Natural variantiVAR_023264860G → V in MNK; decreased protein abundance; impaired copper transport activity. 2 Publications1
Natural variantiVAR_010001873L → R in MNK; increased protein abundance; does not affect interaction with ATOX1; does not affect interaction with COMMD1; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion. 2 PublicationsCorresponds to variant dbSNP:rs72554646Ensembl.1
Natural variantiVAR_010002876G → E in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 2 Publications1
Natural variantiVAR_023265876G → R in MNK; loss of protein expression. 2 Publications1
Natural variantiVAR_023266924Q → R in OHS; has no effect on copper-dependent trafficking; impaired copper transport activity. 2 Publications1
Natural variantiVAR_063882994T → I in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some of the mutant protein remaining in the Golgi apparatus after exposure to copper. 1 PublicationCorresponds to variant dbSNP:rs267606673EnsemblClinVar.1
Natural variantiVAR_0100031000C → R in MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity. 3 Publications1
Natural variantiVAR_0843511005G → R in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs1569550143EnsemblClinVar.1
Natural variantiVAR_0007011006L → P in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554651Ensembl.1
Natural variantiVAR_0232671007A → V in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0232681015G → D in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0007021019G → D in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554652EnsemblClinVar.1
Natural variantiVAR_0843521037K → N in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_0232691044D → G in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0688311048T → I in MNK. 1 Publication1
Natural variantiVAR_0232701100L → P in MNK. 1 Publication1
Natural variantiVAR_0232711118G → D in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554654Ensembl.1
Natural variantiVAR_0232721255G → R in MNK; decreased protein abundance; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 PublicationsCorresponds to variant dbSNP:rs72554655Ensembl.1
Natural variantiVAR_0232731282K → E in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0100041300G → E in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0843531301D → G in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 PublicationCorresponds to variant dbSNP:rs1557238588EnsemblClinVar.1
Natural variantiVAR_0843541302G → E in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0100051302G → R in MNK. 1 PublicationCorresponds to variant dbSNP:rs72554657Ensembl.1
Natural variantiVAR_0100061302G → V in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0232741304N → K in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0638831304N → S in OHS; has approximately 33% residual copper transport; increased protein abundance; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion; does not affect interaction with ATOX1; does not affect interaction with COMMD1. 2 PublicationsCorresponds to variant dbSNP:rs151340632EnsemblClinVar.1
Natural variantiVAR_0100071305D → A in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0843551305D → G in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0843561308A → D in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0232751315G → R in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 PublicationsCorresponds to variant dbSNP:rs797045390EnsemblClinVar.1
Natural variantiVAR_0232761325A → V in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0232771344S → R in MNK. 1 Publication1
Natural variantiVAR_0232781345I → F in MNK. 1 Publication1
Natural variantiVAR_0806631350K → E2 PublicationsCorresponds to variant dbSNP:rs4826245Ensembl.1
Natural variantiVAR_0100081362A → V in MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity. 3 Publications1
Natural variantiVAR_0232791369G → R in MNK; loss of protein expression. 2 Publications1
Natural variantiVAR_0843571373A → P in MNK; loss of protein expression. 1 Publication1
Natural variantiVAR_0638841386P → S in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper. 1 PublicationCorresponds to variant dbSNP:rs267606672EnsemblClinVar.1
Natural variantiVAR_0843581393M → T in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 1 Publication1
Natural variantiVAR_0232801397S → F in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity. 2 Publications1
Natural variantiVAR_0161211464I → V. Corresponds to variant dbSNP:rs2234938EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0004191M → MRKLSIRKRDNNLLK in isoform 1. 1 Publication1
Alternative sequenceiVSP_0004201M → MRKLSIRKRDNNLLKPSSAS SLGIAVSLGRPVLSRSSSGT VNLLEEVGLHIRDTAFSSTK LLEAISTVSAQVEELAVHNE CY in isoform 2. 1 Publication1
Alternative sequenceiVSP_0004211M → MRKLSIRKRDNNLLKECNEE IK in isoform 6. Curated1
Alternative sequenceiVSP_00042442 – 1038Missing in isoform 3. 2 PublicationsAdd BLAST997
Alternative sequenceiVSP_00042253 – 81DPKLQ…NPDPL → AHWFGFAALDGICSNGCFIC FCSTFFSSL in isoform 6. CuratedAdd BLAST29
Alternative sequenceiVSP_00042382 – 1499Missing in isoform 6. CuratedAdd BLAST1418
Alternative sequenceiVSP_000425725 – 802Missing in isoform 5. CuratedAdd BLAST