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Q04656 (ATP7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase 1

EC=3.6.3.54
Alternative name(s):
Copper pump 1
Menkes disease-associated protein
Gene names
Name:ATP7A
Synonyms:MC1, MNK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.

Catalytic activity

ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

Subunit structure

Monomer. Interacts with PDZD11. Ref.16

Subcellular location

Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Cycles constitutively between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels. Ref.12 Ref.14 Ref.15

Isoform 3: Cytoplasmcytosol Probable Ref.12 Ref.14 Ref.15.

Isoform 5: Endoplasmic reticulum Ref.12 Ref.14 Ref.15.

Tissue specificity

Found in most tissues except liver. Isoform 3 is widely expressed including in liver cell lines. Isoform 1 is expressed in fibroblasts, choriocarcinoma, colon carcinoma and neuroblastoma cell lines. Isoform 2 is expressed in fibroblasts, colon carcinoma and neuroblastoma cell lines.

Domain

The C-terminal di-leucine, 1487-Leu-Leu-1488, is an endocytic targeting signal which functions in retrieving recycling from the plasma membrane to the TGN. Mutation of the di-leucine signal results in the accumulation of the protein in the plasma membrane.

Involvement in disease

Menkes disease (MNKD) [MIM:309400]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.32

Occipital horn syndrome (OHS) [MIM:304150]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.30

Distal spinal muscular atrophy, X-linked, 3 (DSMAX3) [MIM:300489]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 6 HMA domains.

Ontologies

Keywords
   Biological processCopper transport
Ion transport
Transport
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Copper
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT-helper cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

blood vessel development

Inferred from sequence or structural similarity. Source: UniProtKB

blood vessel remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

cartilage development

Inferred from sequence or structural similarity. Source: UniProtKB

catecholamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular copper ion homeostasis

Inferred from mutant phenotype PubMed 16397091. Source: UniProtKB

central nervous system neuron development

Inferred from sequence or structural similarity. Source: UniProtKB

cerebellar Purkinje cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

collagen fibril organization

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion export

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion import

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion transport

Inferred from mutant phenotype PubMed 11092760. Source: UniProtKB

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

detoxification of copper ion

Inferred from sequence or structural similarity. Source: UniProtKB

dopamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

elastic fiber assembly

Inferred from sequence or structural similarity. Source: UniProtKB

elastin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

epinephrine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix organization

Inferred from sequence or structural similarity. Source: UniProtKB

hair follicle morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

lactation

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

lung alveolus development

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of metalloenzyme activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

norepinephrine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

norepinephrine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-lysine modification

Inferred from sequence or structural similarity. Source: UniProtKB

pigmentation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metalloenzyme activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of oxidoreductase activity

Inferred from direct assay PubMed 11092760. Source: UniProtKB

pyramidal neuron development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

regulation of oxidative phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

removal of superoxide radicals

Inferred from sequence or structural similarity. Source: UniProtKB

response to iron(III) ion

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

serotonin metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

skin development

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

tryptophan metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

tyrosine metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.12. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 16397091. Source: UniProtKB

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay Ref.12. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

late endosome

Inferred from direct assay PubMed 8943055. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 10567439PubMed 16397091PubMed 8943055. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12812980. Source: UniProtKB

secretory granule

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from direct assay PubMed 12812980PubMed 8943055. Source: UniProtKB

trans-Golgi network transport vesicle

Inferred from mutant phenotype PubMed 9817923. Source: HGNC

   Molecular_functionATP binding

Traceable author statement PubMed 9817923. Source: HGNC

copper ion binding

Inferred from direct assay PubMed 15670166. Source: UniProtKB

copper ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

copper-dependent protein binding

Inferred from physical interaction PubMed 10497213. Source: UniProtKB

copper-exporting ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16884690PubMed 23563491. Source: UniProtKB

superoxide dismutase copper chaperone activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDZD11Q5EBL84EBI-7706409,EBI-1644207

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q04656-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q04656-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKLSIRKRDNNLLK
Isoform 2 (identifier: Q04656-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKLSIRKRD...EELAVHNECY
Isoform 3 (identifier: Q04656-4)

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.
Isoform 5 (identifier: Q04656-5)

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.
Isoform 6 (identifier: Q04656-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15001500Copper-transporting ATPase 1
PRO_0000046311

Regions

Topological domain1 – 653653Cytoplasmic Potential
Transmembrane654 – 67522Helical; Potential
Topological domain676 – 71439Extracellular Potential
Transmembrane715 – 73420Helical; Potential
Topological domain735 – 7417Cytoplasmic Potential
Transmembrane742 – 76221Helical; Potential
Topological domain763 – 78119Extracellular Potential
Transmembrane782 – 80221Helical; Potential
Topological domain803 – 936134Cytoplasmic Potential
Transmembrane937 – 95923Helical; Potential
Topological domain960 – 98930Extracellular Potential
Transmembrane990 – 101122Helical; Potential
Topological domain1012 – 1356345Cytoplasmic Potential
Transmembrane1357 – 137418Helical; Potential
Topological domain1375 – 138511Extracellular Potential
Transmembrane1386 – 140520Helical; Potential
Topological domain1406 – 150095Cytoplasmic Potential
Domain9 – 7567HMA 1
Domain172 – 23867HMA 2
Domain278 – 34467HMA 3
Domain378 – 44467HMA 4
Domain489 – 55567HMA 5
Domain565 – 63167HMA 6
Region1486 – 150015PDZD11-binding
Motif1487 – 14882Endocytosis signal
Compositional bias355 – 3628Poly-Ser

Sites

Active site104414-aspartylphosphate intermediate By similarity
Metal binding13011Magnesium By similarity
Metal binding13051Magnesium By similarity

Amino acid modifications

Modified residue3391Phosphoserine Ref.18
Modified residue3571Phosphoserine By similarity
Modified residue12121Phosphothreonine By similarity
Modified residue14661Phosphoserine By similarity
Glycosylation6861N-linked (GlcNAc...) Potential
Glycosylation9751N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence11M → MRKLSIRKRDNNLLK in isoform 1.
VSP_000419
Alternative sequence11M → MRKLSIRKRDNNLLKPSSAS SLGIAVSLGRPVLSRSSSGT VNLLEEVGLHIRDTAFSSTK LLEAISTVSAQVEELAVHNE CY in isoform 2.
VSP_000420
Alternative sequence11M → MRKLSIRKRDNNLLKECNEE IK in isoform 6.
VSP_000421
Alternative sequence42 – 1038997Missing in isoform 3.
VSP_000424
Alternative sequence53 – 8129DPKLQ…NPDPL → AHWFGFAALDGICSNGCFIC FCSTFFSSL in isoform 6.
VSP_000422
Alternative sequence82 – 14991418Missing in isoform 6.
VSP_000423
Alternative sequence725 – 80278Missing in isoform 5.
VSP_000425
Natural variant6291A → P in MNKD. Ref.22
VAR_000699
Natural variant6371S → L in OHS. Ref.23
Corresponds to variant rs28936068 [ dbSNP | Ensembl ].
VAR_009999
Natural variant6691I → T. Ref.1 Ref.3
Corresponds to variant rs2234935 [ dbSNP | Ensembl ].
VAR_016119
Natural variant7031R → H.
Corresponds to variant rs2234936 [ dbSNP | Ensembl ].
VAR_016120
Natural variant7061L → R in MNKD. Ref.28
VAR_023261
Natural variant7271G → R in MNKD. Ref.22
VAR_000700
Natural variant7671V → L. Ref.21
Corresponds to variant rs2227291 [ dbSNP | Ensembl ].
VAR_010000
Natural variant8441R → H in MNKD. Ref.29
VAR_023262
Natural variant8531G → R in MNKD. Ref.29
VAR_023263
Natural variant8601G → V in MNKD. Ref.29
VAR_023264
Natural variant8731L → R in MNKD. Ref.25
VAR_010001
Natural variant8761G → E in MNKD. Ref.29
VAR_010002
Natural variant8761G → R in MNKD. Ref.29
VAR_023265
Natural variant9241Q → R in MNKD. Ref.29
VAR_023266
Natural variant9941T → 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. Ref.31
VAR_063882
Natural variant10001C → R in MNKD. Ref.29
VAR_010003
Natural variant10061L → P in MNKD. Ref.22
VAR_000701
Natural variant10071A → V in MNKD. Ref.29
VAR_023267
Natural variant10151G → D in MNKD. Ref.29
VAR_023268
Natural variant10191G → D in MNKD. Ref.22
VAR_000702
Natural variant10441D → G in MNKD. Ref.29
VAR_023269
Natural variant10481T → I in MNKD. Ref.32
VAR_068831
Natural variant11001L → P in MNKD. Ref.29
VAR_023270
Natural variant11181G → D in MNKD. Ref.28
VAR_023271
Natural variant12551G → R in MNKD. Ref.28
VAR_023272
Natural variant12821K → E in MNKD. Ref.29
VAR_023273
Natural variant13001G → E in MNKD. Ref.29
VAR_010004
Natural variant13021G → R in MNKD. Ref.21
VAR_010005
Natural variant13021G → V in MNKD. Ref.29
VAR_010006
Natural variant13041N → K in MNKD. Ref.29
VAR_023274
Natural variant13041N → S in OHS; has approximately 33% residual copper transport. Ref.30
VAR_063883
Natural variant13051D → A in MNKD. Ref.29
VAR_010007
Natural variant13151G → R in MNKD. Ref.29
VAR_023275
Natural variant13251A → V in MNKD. Ref.29
VAR_023276
Natural variant13441S → R in MNKD. Ref.27
VAR_023277
Natural variant13451I → F in MNKD. Ref.27
VAR_023278
Natural variant13621A → V in MNKD. Ref.24
VAR_010008
Natural variant13691G → R in MNKD. Ref.29
VAR_023279
Natural variant13861P → S in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper. Ref.31
VAR_063884
Natural variant13971S → F in MNKD. Ref.29
VAR_023280
Natural variant14641I → V.
Corresponds to variant rs2234938 [ dbSNP | Ensembl ].
VAR_016121

Experimental info

Mutagenesis1487 – 14882LL → AA: Loss of relocalization to the trans-Golgi. Ref.15
Sequence conflict101V → A no nucleotide entry Ref.4
Sequence conflict361V → E in AAA16974. Ref.10
Sequence conflict3361E → V in AAA35580. Ref.1
Sequence conflict3361E → V in AAA96010. Ref.8
Sequence conflict4461D → G in CAB08162. Ref.6
Sequence conflict6241S → G in CAB08162. Ref.6
Sequence conflict7251F → V in CAB08162. Ref.6
Sequence conflict8331S → R in CAB08162. Ref.6
Sequence conflict10991E → K no nucleotide entry Ref.4
Sequence conflict11711N → S in CAB08162. Ref.6
Sequence conflict11781Y → C no nucleotide entry Ref.4
Sequence conflict11781Y → H in AAA35580. Ref.1
Sequence conflict11781Y → H in CAB94714. Ref.3
Sequence conflict11781Y → H in AAA96010. Ref.8
Sequence conflict12201D → G in CAB08162. Ref.6
Sequence conflict12951R → W no nucleotide entry Ref.4
Sequence conflict13131N → D no nucleotide entry Ref.4
Sequence conflict13361N → D in CAB08162. Ref.6
Sequence conflict13501E → K in AAA35580. Ref.1
Sequence conflict13501E → K in CAB94714. Ref.3
Sequence conflict13501E → K in AAA96010. Ref.8
Sequence conflict13761V → M in CAB08162. Ref.6
Sequence conflict13961S → P no nucleotide entry Ref.4
Sequence conflict14091L → R in CAB08160. Ref.6
Sequence conflict14551R → W no nucleotide entry Ref.4

Secondary structure

.................................................................................................................................................................. 1500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified February 10, 2009. Version 3.
Checksum: CF8FF9EA061D463B

FASTA1,500163,374
        10         20         30         40         50         60 
MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK 

        70         80         90        100        110        120 
TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP 

       130        140        150        160        170        180 
QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM 

       190        200        210        220        230        240 
TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK 

       250        260        270        280        290        300 
QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS 

       310        320        330        340        350        360 
ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS 

       370        380        390        400        410        420 
SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE 

       430        440        450        460        470        480 
YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD 

       490        500        510        520        530        540 
KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP 

       550        560        570        580        590        600 
MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA 

       610        620        630        640        650        660 
TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF 

       670        680        690        700        710        720 
CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC 

       730        740        750        760        770        780 
VPVQFFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITF 

       790        800        810        820        830        840 
FDTPPMLFVF IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE 

       850        860        870        880        890        900 
LVQRGDIIKV VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL 

       910        920        930        940        950        960 
LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI ATLLVWIVIG 

       970        980        990       1000       1010       1020 
FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA 

      1030       1040       1050       1060       1070       1080 
QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLTESNRISH HKILAIVGTA 

      1090       1100       1110       1120       1130       1140 
ESNSEHPLGT AITKYCKQEL DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN 

      1150       1160       1170       1180       1190       1200 
NIKNASLVQI DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN 

      1210       1220       1230       1240       1250       1260 
DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV VLMTGDNSKT 

      1270       1280       1290       1300       1310       1320 
ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT 

      1330       1340       1350       1360       1370       1380 
GTDVAIEAAD VVLIRNDLLD VVASIDLSRE TVKRIRINFV FALIYNLVGI PIAAGVFMPI 

      1390       1400       1410       1420       1430       1440 
GLVLQPWMGS AAMAASSVSV VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI 

      1450       1460       1470       1480       1490       1500 
DDTSRNSPKL GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL 

« Hide

Isoform 1 [UniParc].

Checksum: B4FFD7472742EB62
Show »

FASTA1,514165,110
Isoform 2 [UniParc].

Checksum: FDE210402FD79C4B
Show »

FASTA1,581172,078
Isoform 3 (2-16) [UniParc].

Checksum: B81B1F9FFB00B832
Show »

FASTA50354,318
Isoform 5 [UniParc].

Checksum: EEB740B5F6841813
Show »

FASTA1,422154,357
Isoform 6 (NML45) [UniParc].

Checksum: 1F3873EFB0EA6CC2
Show »

FASTA10311,522

References

« Hide 'large scale' references
[1]"Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase."
Vulpe C.D., Levinson B., Whitney S., Packman S., Gitschier J.
Nat. Genet. 3:7-13(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT THR-669.
Tissue: Fibroblast.
[2]Erratum
Vulpe C.D., Levinson B., Whitney S., Packman S., Gitschier J.
Nat. Genet. 3:273-273(1993)
[3]"Characterization of the exon structure of the Menkes disease gene using vectorette PCR."
Tuemer Z., Vural B., Toennesen T., Chelly J., Monaco A.P., Horn N.
Genomics 26:437-442(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4), VARIANT THR-669.
[4]"Multiple transcripts coding for the menkes gene: evidence for alternative splicing of Menkes mRNA."
Reddy M.C., Harris E.D.
Biochem. J. 334:71-77(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fibroblast.
[5]"Multiple forms of the Menkes Cu-ATPase."
Harris E.D., Reddy M.C., Qian Y., Tiffany-Castiglioni E., Majumdar S., Nelson J.
Adv. Exp. Med. Biol. 448:39-51(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Colon carcinoma and Fibroblast.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Molecular structure of the Menkes disease gene (ATP7A)."
Dierick H.A., Ambrosini L., Spencer J., Glover T.W., Mercer J.F.B.
Genomics 28:462-469(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1447 (ISOFORM 4).
[9]"Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein."
Chelly J., Tuemer Z., Toennesen T., Petterson A., Ishikawa-Brush Y., Tommerup N., Horn N., Monaco A.P.
Nat. Genet. 3:14-19(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-626 (ISOFORM 4).
Tissue: Kidney.
[10]"Isolation of a partial candidate gene for Menkes disease by positional cloning."
Mercer J.F.B., Livingston J., Hall B., Paynter J.A., Begy C., Chandrasekharappa S., Lockhart P., Grimes A., Bhave M., Siemieniak D., Glover T.W.
Nat. Genet. 3:20-25(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-529 (ISOFORM 4).
Tissue: Endothelial cell.
[11]"Molecular phylogenetics and the origins of placental mammals."
Murphy W.J., Eizirik E., Johnson W.E., Zhang Y.-P., Ryder O.A., O'Brien S.J.
Nature 409:614-618(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-437.
[12]"Constitutive skipping of alternatively spliced exon 10 in the ATP7A gene abolishes Golgi localization of the menkes protein and produces the occipital horn syndrome."
Qi M., Byers P.H.
Hum. Mol. Genet. 7:465-469(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 5), SUBCELLULAR LOCATION.
[13]"Evidence for a Menkes-like protein with a nuclear targeting sequence."
Reddy M.C., Majumdar S., Harris E.D.
Biochem. J. 350:855-863(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 6).
Tissue: Neuroblastoma.
[14]"Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network."
Dierick H.A., Adam A.N., Escara-Wilke J.F., Glover T.W.
Hum. Mol. Genet. 6:409-416(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"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."
Petris M.J., Mercer J.F.B.
Hum. Mol. Genet. 8:2107-2115(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEUCINE RESIDUES.
[16]"A single PDZ domain protein interacts with the Menkes copper ATPase, ATP7A. A new protein implicated in copper homeostasis."
Stephenson S.E., Dubach D., Lim C.M., Mercer J.F., La Fontaine S.
J. Biol. Chem. 280:33270-33279(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZD11.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase."
Gitschier J., Moffat B., Reilly D., Wood W.I., Fairbrother W.J.
Nat. Struct. Biol. 5:47-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 375-446.
[20]"Mutation spectrum of ATP7A, the gene defective in Menkes disease."
Tuemer Z., Moeller L.B., Horn N.
Adv. Exp. Med. Biol. 448:83-95(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, VARIANTS MNKD.
[21]"Diverse mutations in patients with Menkes disease often lead to exon skipping."
Das S., Levinson B., Whitney S., Vulpe C., Packman S., Gitschier J.
Am. J. Hum. Genet. 55:883-889(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-767, VARIANT MNKD ARG-1302.
[22]"Identification of point mutations in 41 unrelated patients affected with Menkes disease."
Tuemer Z., Lund C., Tolshave J., Vural B., Toennesen T., Horn N.
Am. J. Hum. Genet. 60:63-71(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MNKD PRO-629; ARG-727; PRO-1006 AND ASP-1019.
[23]"A C2055T transition in exon 8 of the ATP7A gene is associated with exon skipping in an occipital horn syndrome family."
Ronce N., Moizard M.P., Robb L., Toutain A., Villard L., Moraine C.
Am. J. Hum. Genet. 61:233-238(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHS LEU-637.
[24]"Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease."
Ambrosini L., Mercer J.F.B.
Hum. Mol. Genet. 8:1547-1555(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MNKD VAL-1362.
[25]"Identification of three novel mutations in the MNK gene in three unrelated Japanese patients with classical Menkes disease."
Ogawa A., Yamamoto S., Takayanagi M., Kogo T., Kanazawa M., Kohno Y.
J. Hum. Genet. 44:206-209(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MNKD ARG-873.
[26]"A novel frameshift mutation in exon 23 of ATP7A (MNK) results in occipital horn syndrome and not in Menkes disease."
Dagenais S.L., Adam A.N., Innis J.W., Glover T.W.
Am. J. Hum. Genet. 69:420-427(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN OCCIPITAL HORN SYNDROME.
[27]"ATP7A gene mutations in 16 patients with Menkes disease and a patient with occipital horn syndrome."
Gu Y.-H., Kodama H., Murata Y., Mochizuki D., Yanagawa Y., Ushijima H., Shiba T., Lee C.-C.
Am. J. Med. Genet. 99:217-222(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MNKD ARG-1344 AND PHE-1345.
[28]"Identification of four novel mutations in classical Menkes disease and successful prenatal DNA diagnosis."
Hahn S., Cho K., Ryu K., Kim J., Pai K., Kim M., Park H., Yoo O.
Mol. Genet. Metab. 73:86-90(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MNKD ARG-706; ASP-1118 AND ARG-1255.
[29]"Identification and analysis of 21 novel disease-causing amino acid substitutions in the conserved part of ATP7A."
Moeller L.B., Bukrinsky J.T., Moelgaard A., Paulsen M., Lund C., Tuemer Z., Larsen S., Horn N.
Hum. Mutat. 26:84-93(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MNKD HIS-844; ARG-853; VAL-860; ARG-876; GLU-876; ARG-924; ARG-1000; VAL-1007; ASP-1015; GLY-1044; PRO-1100; GLU-1282; GLU-1300; VAL-1302; LYS-1304; ALA-1305; ARG-1315; VAL-1325; ARG-1369 AND PHE-1397.
[30]"Functional copper transport explains neurologic sparing in occipital horn syndrome."
Tang J., Robertson S., Lem K.E., Godwin S.C., Kaler S.G.
Genet. Med. 8:711-718(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OHS SER-1304, CHARACTERIZATION OF VARIANT OHS SER-1304.
[31]"Missense mutations in the copper transporter gene ATP7A cause X-linked distal hereditary motor neuropathy."
Kennerson M.L., Nicholson G.A., Kaler S.G., Kowalski B., Mercer J.F.B., Tang J., Llanos R.M., Chu S., Takata R.I., Speck-Martins C.E., Baets J., Almeida-Souza L., Fischer D., Timmerman V., Taylor P.E., Scherer S.S., Ferguson T.A., Bird T.D. expand/collapse author list , De Jonghe P., Feely S.M.E., Shy M.E., Garbern J.Y.
Am. J. Hum. Genet. 86:343-352(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DSMAX3 ILE-994 AND SER-1386, CHARACTERIZATION OF VARIANTS DSMAX3 ILE-994 AND SER-1386.
[32]"The T1048I mutation in ATP7A gene causes an unusual Menkes disease presentation."
De Leon-Garcia G., Santana A., Villegas-Sepulveda N., Perez-Gonzalez C., Henrriquez-Esquiroz J.M., De Leon-Garcia C., Wong C., Baeza I.
BMC Pediatr. 12:150-150(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MNKD ILE-1048.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Heavy metal - Issue 79 of February 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06133 mRNA. Translation: AAA35580.1.
X82336 expand/collapse EMBL AC list , X82337, X82338, X82339, X82340, X82341, X82342, X82343, X82344, X82345, X82346, X82347, X82348, X82349, X82350, X82351, X82352, X82353, X82354, X82355, X82356 Genomic DNA. Translation: CAB94714.1.
AL645821 Genomic DNA. Translation: CAI42806.1.
CH471104 Genomic DNA. Translation: EAW98605.1.
U27381 expand/collapse EMBL AC list , U27361, U27362, U27363, U27365, U27366, U27367, U27368, U27369, U27370, U27371, U27372, U27373, U27374, U27375, U27376, U27377, U27378, U27379, U27380 Genomic DNA. Translation: AAA96010.1.
X69208 mRNA. Translation: CAA49145.1.
L06476 mRNA. Translation: AAA16974.1.
Z94801 Genomic DNA. Translation: CAB08162.2.
Z94753 Genomic DNA. Translation: CAB08160.1.
AY011418 Genomic DNA. Translation: AAG47452.1.
CCDSCCDS35339.1. [Q04656-1]
PIRS36149.
RefSeqNP_000043.4. NM_000052.6.
NP_001269153.1. NM_001282224.1.
UniGeneHs.496414.
Hs.733232.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW0NMR-A375-446[»]
1KVINMR-A1-79[»]
1KVJNMR-A1-79[»]
1Q8LNMR-A164-246[»]
1S6ONMR-A169-240[»]
1S6UNMR-A169-240[»]
1Y3JNMR-A486-558[»]
1Y3KNMR-A486-558[»]
1YJRNMR-A562-633[»]
1YJTNMR-A562-633[»]
1YJUNMR-A562-633[»]
1YJVNMR-A562-633[»]
2AW0NMR-A375-446[»]
2G9ONMR-A275-352[»]
2GA7NMR-A275-352[»]
2K1RNMR-A5-77[»]
2KIJNMR-A806-924[»]
2KMVNMR-A1051-1231[»]
2KMXNMR-A1051-1231[»]
3CJKX-ray1.80B7-77[»]
DisProtDP00282.
ProteinModelPortalQ04656.
SMRQ04656. Positions 1-633, 645-1413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107020. 6 interactions.
IntActQ04656. 1 interaction.
MINTMINT-106053.
STRING9606.ENSP00000345728.

Protein family/group databases

TCDB3.A.3.5.6. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteQ04656.

Polymorphism databases

DMDM223590241.

Proteomic databases

MaxQBQ04656.
PaxDbQ04656.
PRIDEQ04656.

Protocols and materials databases

DNASU538.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341514; ENSP00000345728; ENSG00000165240. [Q04656-1]
ENST00000343533; ENSP00000343026; ENSG00000165240. [Q04656-5]
ENST00000350425; ENSP00000343678; ENSG00000165240. [Q04656-4]
GeneID538.
KEGGhsa:538.
UCSCuc004ecx.4. human. [Q04656-1]

Organism-specific databases

CTD538.
GeneCardsGC0XP077166.
GeneReviewsATP7A.
HGNCHGNC:869. ATP7A.
HPAHPA012887.
MIM300011. gene.
300489. phenotype.
304150. phenotype.
309400. phenotype.
neXtProtNX_Q04656.
Orphanet565. Menkes disease.
198. Occipital horn syndrome.
139557. X-linked distal spinal muscular atrophy.
PharmGKBPA72.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250397.
HOVERGENHBG050616.
KOK17686.
OMASAIEDCG.
OrthoDBEOG7C2R0G.
PhylomeDBQ04656.
TreeFamTF300460.

Enzyme and pathway databases

BRENDA3.6.3.4. 2681.
ReactomeREACT_120956. Cellular responses to stress.
REACT_15518. Transmembrane transport of small molecules.
SABIO-RKQ04656.

Gene expression databases

BgeeQ04656.
CleanExHS_ATP7A.
GenevestigatorQ04656.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
[Graphical view]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF55008. SSF55008. 6 hits.
SSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 6 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 6 hits.
PS50846. HMA_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP7A. human.
EvolutionaryTraceQ04656.
GeneWikiATP7A.
GenomeRNAi538.
NextBio2231.
PROQ04656.
SOURCESearch...

Entry information

Entry nameATP7A_HUMAN
AccessionPrimary (citable) accession number: Q04656
Secondary accession number(s): B1AT72 expand/collapse secondary AC list , O00227, O00745, Q9BYY8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM