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P35670 (ATP7B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase 2

EC=3.6.3.54
Alternative name(s):
Copper pump 2
Wilson disease-associated protein

Cleaved into the following chain:

  1. WND/140 kDa
Gene names
Name:ATP7B
Synonyms:PWD, WC1, WND
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.

Catalytic activity

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

Subunit structure

Monomer. Interacts with COMMD1/MURR1. Interacts with DCTN4, in a copper-dependent manner. Interacts with ATOX1. Ref.14 Ref.15 Ref.17

Subcellular location

Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein By similarity. Note: Predominantly found in the trans-Golgi network (TGN). Not redistributed to the plasma membrane in response to elevated copper levels. Ref.12

Isoform 2: Cytoplasm Ref.12.

WND/140 kDa: Mitochondrion Ref.12.

Tissue specificity

Most abundant in liver and kidney and also found in brain. Isoform 2 is expressed in brain but not in liver. The cleaved form WND/140 kDa is found in liver cell lines and other tissues.

Domain

Each HMA domain can bind a copper ion, they are tightly packed and closely interact with each other. Wild-type ATP7B can usually be loaded with an average 5.5 copper atoms per molecule. Ref.16

Post-translational modification

Isoform 1 may be proteolytically cleaved at the N-terminus to produce the WND/140 kDa form. Ref.13

Involvement in disease

Wilson disease (WD) [MIM:277900]: An autosomal recessive disorder of copper metabolism in which copper cannot be incorporated into ceruloplasmin in liver, and cannot be excreted from the liver into the bile. Copper accumulates in the liver and subsequently in the brain and kidney. The disease is characterized by neurologic manifestations and signs of cirrhosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.10 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66

Sequence similarities

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

Contains 6 HMA domains.

Sequence caution

The sequence AAA16173.1 differs from that shown. Reason: Frameshift at position 830.

The sequence AAA79211.1 differs from that shown. Reason: Frameshift at position 456.

The sequence AAA79212.1 differs from that shown. Reason: Frameshift at position 456.

Ontologies

Keywords
   Biological processCopper transport
Ion transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Copper
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular copper ion homeostasis

Traceable author statement Ref.15. Source: UniProtKB

cellular zinc ion homeostasis

Inferred from electronic annotation. Source: Ensembl

copper ion import

Inferred from direct assay PubMed 16472602. Source: UniProtKB

copper ion transport

Inferred from genetic interaction PubMed 12572677. Source: UniProtKB

intracellular copper ion transport

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

lactation

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from direct assay PubMed 15269005PubMed 16472602PubMed 16939419. Source: UniProtKB

sequestering of calcium ion

Inferred from direct assay PubMed 16472602. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

integral component of plasma membrane

Traceable author statement Ref.7. Source: UniProtKB

late endosome

Inferred from direct assay PubMed 15681833. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay PubMed 16567646. Source: UniProtKB

copper ion binding

Inferred from direct assay PubMed 12029094. Source: UniProtKB

copper-exporting ATPase activity

Non-traceable author statement PubMed 12763797. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35670-1)

Also known as: A;

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 2 (identifier: P35670-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     624-785: Missing.
     911-955: Missing.
Isoform 3 (identifier: P35670-3)

The sequence of this isoform differs from the canonical sequence as follows:
     269-379: Missing.
Isoform 4 (identifier: P35670-4)

The sequence of this isoform differs from the canonical sequence as follows:
     938-955: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14651465Copper-transporting ATPase 2
PRO_0000046314
Chain? – 1465WND/140 kDaPRO_0000296199

Regions

Topological domain1 – 653653Cytoplasmic Potential
Transmembrane654 – 67522Helical; Potential
Topological domain676 – 69722Extracellular Potential
Transmembrane698 – 71720Helical; Potential
Topological domain718 – 7247Cytoplasmic Potential
Transmembrane725 – 74521Helical; Potential
Topological domain746 – 76419Extracellular Potential
Transmembrane765 – 78521Helical; Potential
Topological domain786 – 919134Cytoplasmic Potential
Transmembrane920 – 94223Helical; Potential
Topological domain943 – 97230Extracellular Potential
Transmembrane973 – 99422Helical; Potential
Topological domain995 – 1322328Cytoplasmic Potential
Transmembrane1323 – 134018Helical; Potential
Topological domain1341 – 135111Extracellular Potential
Transmembrane1352 – 137120Helical; Potential
Topological domain1372 – 146594Cytoplasmic Potential
Domain59 – 12567HMA 1
Domain144 – 21067HMA 2
Domain258 – 32770HMA 3
Domain360 – 42667HMA 4
Domain489 – 55567HMA 5
Domain565 – 63167HMA 6
Compositional bias340 – 3456Poly-Ser

Sites

Active site102714-aspartylphosphate intermediate By similarity
Metal binding691Copper 1
Metal binding721Copper 1
Metal binding1541Copper 2
Metal binding1571Copper 2
Metal binding2681Copper 3
Metal binding2711Copper 3
Metal binding3701Copper 4
Metal binding3731Copper 4
Metal binding4991Copper 5
Metal binding5021Copper 5
Metal binding5751Copper 6
Metal binding5781Copper 6
Metal binding12671Magnesium By similarity
Metal binding12711Magnesium By similarity

Natural variations

Alternative sequence269 – 379111Missing in isoform 3.
VSP_016559
Alternative sequence624 – 785162Missing in isoform 2.
VSP_000426
Alternative sequence911 – 95545Missing in isoform 2.
VSP_000427
Alternative sequence938 – 95518Missing in isoform 4.
VSP_016560
Natural variant141A → D. Ref.51
VAR_023010
Natural variant411N → S in WD. Ref.53
VAR_023011
Natural variant851G → V in WD. Ref.30 Ref.51
VAR_000703
Natural variant961G → D. Ref.1
VAR_000704
Natural variant2901V → L. Ref.42
VAR_044453
Natural variant3901I → V.
VAR_000705
Natural variant4061S → A. Ref.2 Ref.41 Ref.42 Ref.45 Ref.51 Ref.58 Ref.64
Corresponds to variant rs1801243 [ dbSNP | Ensembl ].
VAR_000706
Natural variant4461V → L.
VAR_000707
Natural variant4561V → L. Ref.2 Ref.26 Ref.41 Ref.42 Ref.45 Ref.51 Ref.58 Ref.62 Ref.64
Corresponds to variant rs1801244 [ dbSNP | Ensembl ].
VAR_000708
Natural variant4661L → V.
VAR_000709
Natural variant4861A → S in WD. Ref.39
VAR_044454
Natural variant4921L → S in WD. Ref.30
VAR_000710
Natural variant5321Y → H in WD. Ref.61 Ref.65
VAR_044455
Natural variant5361V → A in WD. Ref.64
Corresponds to variant rs138427376 [ dbSNP | Ensembl ].
VAR_058925
Natural variant5491L → P in WD. Ref.66
VAR_067335
Natural variant5651N → S. Ref.27
VAR_000711
Natural variant5911G → D in WD. Ref.61
VAR_044456
Natural variant6041A → P in WD. Ref.61
VAR_044457
Natural variant608 – 6092FD → Y in WD.
VAR_010009
Natural variant6161R → Q in WD. Ref.59 Ref.60
VAR_009004
Natural variant6161R → W in WD. Ref.45
VAR_023012
Natural variant6261G → A in WD. Ref.59 Ref.65
VAR_000712
Natural variant6391H → Y in WD. Ref.60
VAR_044458
Natural variant6411L → S in WD. Ref.61 Ref.62
Corresponds to variant rs186924074 [ dbSNP | Ensembl ].
VAR_023013
Natural variant6421D → H in WD. Ref.30 Ref.65 Ref.66
VAR_000713
Natural variant6451M → R in WD. Ref.27 Ref.30 Ref.58
VAR_000714
Natural variant6531S → Y in WD. Ref.60
VAR_044459
Natural variant6571S → R in WD. Ref.64
VAR_058926
Natural variant6651M → I in WD. Ref.30
Corresponds to variant rs72552259 [ dbSNP | Ensembl ].
VAR_000715
Natural variant670 – 6712Missing in WD.
VAR_009005
Natural variant6901P → L in WD. Ref.58
VAR_023014
Natural variant6911G → R in WD. Ref.30 Ref.63
VAR_000716
Natural variant6931S → C in WD. Ref.23
VAR_023015
Natural variant7031C → Y in WD. Ref.61 Ref.66
VAR_044460
Natural variant7081L → P in WD. Ref.40
VAR_000717
Natural variant7101G → A in WD. Ref.26 Ref.45
VAR_010010
Natural variant7101G → R in WD.
VAR_000718
Natural variant7101G → S in WD. Ref.37 Ref.45 Ref.62
VAR_000719
Natural variant7101G → V in WD. Ref.61
VAR_044461
Natural variant7111G → E in WD.
VAR_000720
Natural variant7111G → R in WD. Ref.37
VAR_009006
Natural variant7111G → W in WD.
VAR_009007
Natural variant7131Y → C in WD.
VAR_000721
Natural variant7211S → P in WD. Ref.49
VAR_023016
Natural variant7231R → G. Ref.27
VAR_000722
Natural variant7371T → R in WD. Ref.62
VAR_023017
Natural variant7411Y → C in WD. Ref.26
VAR_010011
Natural variant7441S → P in WD. Ref.66
VAR_009008
Natural variant7471I → F in WD. Ref.30
VAR_000723
Natural variant7561A → G in WD. Ref.61
VAR_044462
Natural variant7601P → L in WD. Ref.44 Ref.45
VAR_023018
Natural variant7651D → G in WD. Ref.51
VAR_023019
Natural variant7651D → N in WD. Ref.27 Ref.45 Ref.66
Corresponds to variant rs28942075 [ dbSNP | Ensembl ].
VAR_000724
Natural variant7661T → M in WD. Ref.61
VAR_044463
Natural variant7661T → R in WD. Ref.54
VAR_044464
Natural variant7681P → H in WD. Ref.48
VAR_023020
Natural variant7691M → I in WD. Ref.41
VAR_023021
Natural variant7691M → R in WD.
VAR_009009
Natural variant7691M → V in WD. Ref.45
VAR_000725
Natural variant7761L → P in WD. Ref.60
VAR_044465
Natural variant7761L → V Possible polymorphism.
VAR_000726
Natural variant7781R → G in WD. Ref.39 Ref.59 Ref.60 Ref.62 Ref.66
VAR_000727
Natural variant7781R → L in WD; most common mutation. Ref.21 Ref.28 Ref.29 Ref.38 Ref.41 Ref.42 Ref.48 Ref.50 Ref.51 Ref.55
Corresponds to variant rs28942074 [ dbSNP | Ensembl ].
VAR_000728
Natural variant7781R → Q in WD. Ref.21
VAR_000729
Natural variant7781R → W in WD. Ref.30 Ref.41 Ref.46 Ref.59
VAR_000730
Natural variant7951L → F in WD.
VAR_000731
Natural variant7951L → R in WD.
VAR_009010
Natural variant8321K → R. Ref.8 Ref.9 Ref.27 Ref.28 Ref.42 Ref.45 Ref.51 Ref.58 Ref.62 Ref.64
Corresponds to variant rs1061472 [ dbSNP | Ensembl ].
VAR_000732
Natural variant8401P → L in WD. Ref.30 Ref.37
VAR_000733
Natural variant8571I → T in WD.
VAR_000734
Natural variant8611A → T in WD. Ref.61
VAR_044466
Natural variant8641V → I. Ref.28
VAR_000735
Natural variant8691G → R in WD. Ref.58
Corresponds to variant rs191312027 [ dbSNP | Ensembl ].
VAR_000736
Natural variant8691G → V in WD.
VAR_009011
Natural variant8741A → V in WD. Ref.28 Ref.29 Ref.37 Ref.38 Ref.41 Ref.42 Ref.48 Ref.50 Ref.59
VAR_000737
Natural variant8751G → R. Ref.1 Ref.7
VAR_023022
Natural variant8751G → V in WD; requires 2 nucleotide substitutions.
VAR_044467
Natural variant8901V → M in WD. Ref.39 Ref.51
VAR_023023
Natural variant8911G → V in WD.
VAR_010012
Natural variant8981Q → R in WD. Ref.46
VAR_023024
Natural variant9181D → E in WD. Ref.62
VAR_023025
Natural variant9181D → N in WD. Ref.30
VAR_000738
Natural variant9191R → G in WD. Ref.29 Ref.38 Ref.41 Ref.50 Ref.51
VAR_000739
Natural variant9191R → W in WD. Ref.30
VAR_000740
Natural variant9211S → N in WD. Ref.30
VAR_000741
Natural variant9331T → P in WD. Ref.30
VAR_000742
Natural variant9351T → M in WD. Ref.51
VAR_000743
Natural variant9431G → C in WD. Ref.61
VAR_044468
Natural variant9431G → D in WD. Ref.55
VAR_000744
Natural variant9431G → S in WD. Ref.58
Corresponds to variant rs28942076 [ dbSNP | Ensembl ].
VAR_000745
Natural variant9491V → G in WD. Ref.26 Ref.53
VAR_023026
Natural variant9521R → K. Ref.1 Ref.2 Ref.5 Ref.64
Corresponds to variant rs732774 [ dbSNP | Ensembl ].
VAR_000746
Natural variant9671I → F in WD. Ref.19
Corresponds to variant rs60003608 [ dbSNP | Ensembl ].
VAR_010013
Natural variant9691R → Q in WD. Ref.27 Ref.37 Ref.39 Ref.45 Ref.59 Ref.62
VAR_000747
Natural variant9711A → V in WD. Ref.64
VAR_058927
Natural variant9741T → M in WD. Ref.64
VAR_058928
Natural variant9751S → Y in WD. Ref.51
VAR_023027
Natural variant9771T → M in WD. Ref.19 Ref.58 Ref.60 Ref.62 Ref.66
VAR_000748
Natural variant9851C → Y in WD. Ref.33
VAR_009012
Natural variant9881G → R in WD. Ref.60
VAR_044469
Natural variant9911T → M in WD. Ref.61
Corresponds to variant rs41292782 [ dbSNP | Ensembl ].
VAR_044470
Natural variant9921P → H in WD. Ref.57
VAR_044471
Natural variant9921P → L in WD; common mutation. Ref.30 Ref.45 Ref.51 Ref.60
VAR_000749
Natural variant9951V → A.
VAR_000750
Natural variant9961M → T in WD. Ref.61
VAR_044472
Natural variant9981G → D in WD. Ref.66
VAR_067336
Natural variant10001G → R in WD. Ref.61
VAR_044473
Natural variant10031A → T in WD. Ref.30 Ref.41 Ref.57 Ref.59
Corresponds to variant rs201497300 [ dbSNP | Ensembl ].
VAR_000751
Natural variant10031A → V in WD. Ref.37
VAR_009013
Natural variant10041Q → P in WD. Ref.64
VAR_058929
Natural variant10181A → V in WD. Ref.30 Ref.62
VAR_000752
Natural variant10291T → I in WD. Ref.38
VAR_044474
Natural variant10311T → I in WD. Ref.26
VAR_010014
Natural variant10331T → A in WD.
VAR_009014
Natural variant10331T → S in WD. Ref.62
VAR_023028
Natural variant10351G → V in WD. Ref.38
VAR_000753
Natural variant10381R → K in WD. Ref.25
Corresponds to variant rs59959366 [ dbSNP | Ensembl ].
VAR_010015
Natural variant10411R → P in WD. Ref.32 Ref.37
VAR_009015
Natural variant10411R → W in WD; unknown pathological significance. Ref.30 Ref.37 Ref.62 Ref.65
VAR_000754
Natural variant10431L → P in WD.
VAR_000755
Natural variant10521P → L in WD.
VAR_009016
Natural variant10611G → E in WD. Ref.37 Ref.39 Ref.58
VAR_009017
Natural variant10631A → V in WD. Ref.37 Ref.62 Ref.66
VAR_009018
Natural variant10641E → A in WD. Ref.27
VAR_000756
Natural variant10641E → K in WD; marked impairment in copper transport. Ref.62 Ref.65
VAR_000757
Natural variant10651A → P in WD.
VAR_044475
Natural variant10681E → G in WD; common mutation. Ref.37
VAR_009019
Natural variant10691H → Q in WD; common mutation. Ref.7 Ref.26 Ref.27 Ref.36 Ref.37 Ref.39 Ref.45 Ref.46 Ref.58 Ref.59 Ref.60 Ref.62 Ref.66
VAR_000758
Natural variant10831L → F in WD; marked impairment in copper transport. Ref.28 Ref.41 Ref.47 Ref.48 Ref.65
VAR_000759
Natural variant10891G → E in WD. Ref.37
VAR_000760
Natural variant10891G → V in WD. Ref.30
VAR_000761
Natural variant10941F → L in WD. Ref.53
VAR_023029
Natural variant10951Q → P in WD. Ref.60
VAR_009020
Natural variant10981P → R in WD. Ref.51
VAR_023030
Natural variant10991G → S in WD. Ref.39 Ref.58
VAR_023031
Natural variant11011G → R in WD.
VAR_000762
Natural variant11021I → T in WD. Ref.46 Ref.57 Ref.62
VAR_000763
Natural variant11041C → F in WD. Ref.37
VAR_009021
Natural variant11041C → Y in WD. Ref.57
VAR_044476
Natural variant11061V → D in WD; marked impairment in copper transport. Ref.19 Ref.65
VAR_010017
Natural variant11061V → I in WD. Ref.55
VAR_044477
Natural variant11091V → M. Ref.28
VAR_000764
Natural variant11111G → D in WD. Ref.62
Corresponds to variant rs182659444 [ dbSNP | Ensembl ].
VAR_023032
Natural variant11401V → A. Ref.2 Ref.9 Ref.26 Ref.27 Ref.28 Ref.41 Ref.42 Ref.51 Ref.55 Ref.58 Ref.62 Ref.64 Ref.65 Ref.67
Corresponds to variant rs1801249 [ dbSNP | Ensembl ].
VAR_000765
Natural variant11421Q → H in WD.
VAR_000766
Natural variant11431T → N. Ref.51
VAR_023033
Natural variant11461V → M in WD. Ref.30
VAR_000767
Natural variant11481I → T in WD. Ref.33 Ref.39 Ref.51 Ref.56 Ref.62
Corresponds to variant rs60431989 [ dbSNP | Ensembl ].
VAR_000768
Natural variant11491G → A in WD. Ref.64
VAR_058930
Natural variant11511R → H in WD. Ref.37
VAR_009022
Natural variant11531W → C in WD.
VAR_000769
Natural variant11531W → R in WD. Ref.19
VAR_010018
Natural variant11641D → N in WD. Ref.64
VAR_058931
Natural variant11681A → S in WD. Ref.48
VAR_023034
Natural variant11691M → T in WD. Ref.37
VAR_009023
Natural variant11691M → V in WD; moderate impairment in copper transport. Ref.65
VAR_000770
Natural variant11731E → G in WD. Ref.64
VAR_058932
Natural variant11731E → K in WD. Ref.37 Ref.51
VAR_009024
Natural variant11761G → E in WD. Ref.61
VAR_044478
Natural variant11761G → R in WD. Ref.26 Ref.56 Ref.62
VAR_010019
Natural variant11831A → G in WD. Ref.30 Ref.49
VAR_000771
Natural variant11831A → T in WD; possibly not disease-causing. Ref.30 Ref.65
VAR_000772
Natural variant11861G → C in WD.
VAR_000773
Natural variant11861G → S in WD; possibly not disease-causing. Ref.29 Ref.38 Ref.41 Ref.62 Ref.65
VAR_000774
Natural variant12071H → R. Ref.37 Ref.66
Corresponds to variant rs7334118 [ dbSNP | Ensembl ].
VAR_009025
Natural variant12131G → V in WD. Ref.27
VAR_000775
Natural variant1216 – 12172Missing in WD.
VAR_000777
Natural variant12161V → M in WD. Ref.30 Ref.55 Ref.58
VAR_000776
Natural variant1217 – 12182Missing in WD.
VAR_044479
Natural variant12201T → M in WD. Ref.60
VAR_000778
Natural variant12211G → E in WD. Ref.61
VAR_044480
Natural variant12221D → N in WD. Ref.38
VAR_044481
Natural variant12221D → V in WD. Ref.37
VAR_010020
Natural variant12221D → Y in WD.
VAR_000779
Natural variant12281R → T in WD. Ref.64
VAR_058933
Natural variant12301I → V in WD. Ref.64
Corresponds to variant rs200911496 [ dbSNP | Ensembl ].
VAR_058934
Natural variant12321T → P in WD. Ref.53 Ref.58
VAR_023035
Natural variant12391V → G in WD.
VAR_009026
Natural variant12451P → S. Ref.51
VAR_023036
Natural variant12481K → N in WD. Ref.51
VAR_023037
Natural variant12521V → I in WD.
VAR_044482
Natural variant12551L → I in WD. Ref.48
VAR_023038
Natural variant12561Q → R in WD. Ref.57
VAR_044483
Natural variant12621V → F in WD. Ref.37
VAR_009027
Natural variant12661G → R in WD; common mutation. Ref.46
VAR_009028
Natural variant12661G → V in WD.
VAR_000781
Natural variant12671D → A in WD. Ref.29 Ref.41 Ref.48
VAR_000782
Natural variant12671D → V in WD. Ref.64
VAR_058935
Natural variant12701N → S in WD. Ref.7 Ref.29 Ref.41 Ref.45 Ref.48 Ref.59
VAR_000783
Natural variant12711D → N in WD. Ref.62
VAR_023039
Natural variant12731P → L in WD. Ref.60 Ref.62 Ref.66
VAR_000784
Natural variant12781A → V in WD; unknown pathological significance. Ref.24
VAR_000785
Natural variant12791D → G in WD. Ref.43
VAR_023040
Natural variant12791D → Y in WD. Ref.59
VAR_044484
Natural variant1285 – 12928Missing in WD.
VAR_000786
Natural variant12871G → S in WD. Ref.61
VAR_044485
Natural variant12961D → N in WD. Ref.47
Corresponds to variant rs199821556 [ dbSNP | Ensembl ].
VAR_044486
Natural variant12971V → I. Ref.37
Corresponds to variant rs148399850 [ dbSNP | Ensembl ].
VAR_009029
Natural variant12971Missing in WD. Ref.42
VAR_044487
Natural variant13051L → P in WD. Ref.44 Ref.62
VAR_023041
Natural variant13101S → R in WD.
VAR_000787
Natural variant13221R → P in WD.
VAR_000788
Natural variant13271L → V in WD. Ref.37
VAR_009030
Natural variant13281A → T in WD. Ref.64
VAR_058936
Natural variant13311Y → S in WD. Ref.61
VAR_044488
Natural variant13321N → D in WD. Ref.66
VAR_067337
Natural variant13361I → T in WD. Ref.41
VAR_023042
Natural variant13411G → D in WD. Ref.30 Ref.59 Ref.60 Ref.62 Ref.66
VAR_000789
Natural variant13411G → R in WD. Ref.66
VAR_067338
Natural variant13411G → S in WD. Ref.52
VAR_044489
Natural variant13411G → V in WD. Ref.61
VAR_044490
Natural variant13521P → S in WD. Ref.59
VAR_044491
Natural variant13531W → R in WD.
VAR_000790
Natural variant13551G → C in WD. Ref.62
VAR_023043
Natural variant13551G → S in WD. Ref.19
VAR_010021
Natural variant13581A → S in WD. Ref.30
VAR_000791
Natural variant13591M → I in WD. Ref.64
VAR_058937
Natural variant13631S → F in WD. Ref.37
VAR_009031
Natural variant13681L → P in WD. Ref.59
VAR_044492
Natural variant13731L → P in WD. Ref.41
VAR_023044
Natural variant13731L → R in WD. Ref.53
VAR_023045
Natural variant13751C → S in WD. Ref.61
VAR_044493
Natural variant13791P → S in WD. Ref.61
Corresponds to variant rs181250704 [ dbSNP | Ensembl ].
VAR_044494
Natural variant14071D → E. Ref.42
VAR_044495
Natural variant14341T → M in WD. Ref.37
Corresponds to variant rs60986317 [ dbSNP | Ensembl ].
VAR_009032

Experimental info

Sequence conflict4881Q → G in AAA16173. Ref.8
Sequence conflict6351N → T in AAA16173. Ref.8
Sequence conflict7671P → L in AAA16173. Ref.8
Sequence conflict8371G → A in AAA16173. Ref.8

Secondary structure

....................................................................................................... 1465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified June 16, 2009. Version 4.
Checksum: 419145448F9E959A

FASTA1,465157,263
        10         20         30         40         50         60 
MPEQERQITA REGASRKILS KLSLPTRAWE PAMKKSFAFD NVGYEGGLDG LGPSSQVATS 

        70         80         90        100        110        120 
TVRILGMTCQ SCVKSIEDRI SNLKGIISMK VSLEQGSATV KYVPSVVCLQ QVCHQIGDMG 

       130        140        150        160        170        180 
FEASIAEGKA ASWPSRSLPA QEAVVKLRVE GMTCQSCVSS IEGKVRKLQG VVRVKVSLSN 

       190        200        210        220        230        240 
QEAVITYQPY LIQPEDLRDH VNDMGFEAAI KSKVAPLSLG PIDIERLQST NPKRPLSSAN 

       250        260        270        280        290        300 
QNFNNSETLG HQGSHVVTLQ LRIDGMHCKS CVLNIEENIG QLLGVQSIQV SLENKTAQVK 

       310        320        330        340        350        360 
YDPSCTSPVA LQRAIEALPP GNFKVSLPDG AEGSGTDHRS SSSHSPGSPP RNQVQGTCST 

       370        380        390        400        410        420 
TLIAIAGMTC ASCVHSIEGM ISQLEGVQQI SVSLAEGTAT VLYNPSVISP EELRAAIEDM 

       430        440        450        460        470        480 
GFEASVVSES CSTNPLGNHS AGNSMVQTTD GTPTSVQEVA PHTGRLPANH APDILAKSPQ 

       490        500        510        520        530        540 
STRAVAPQKC FLQIKGMTCA SCVSNIERNL QKEAGVLSVL VALMAGKAEI KYDPEVIQPL 

       550        560        570        580        590        600 
EIAQFIQDLG FEAAVMEDYA GSDGNIELTI TGMTCASCVH NIESKLTRTN GITYASVALA 

       610        620        630        640        650        660 
TSKALVKFDP EIIGPRDIIK IIEEIGFHAS LAQRNPNAHH LDHKMEIKQW KKSFLCSLVF 

       670        680        690        700        710        720 
GIPVMALMIY MLIPSNEPHQ SMVLDHNIIP GLSILNLIFF ILCTFVQLLG GWYFYVQAYK 

       730        740        750        760        770        780 
SLRHRSANMD VLIVLATSIA YVYSLVILVV AVAEKAERSP VTFFDTPPML FVFIALGRWL 

       790        800        810        820        830        840 
EHLAKSKTSE ALAKLMSLQA TEATVVTLGE DNLIIREEQV PMELVQRGDI VKVVPGGKFP 

       850        860        870        880        890        900 
VDGKVLEGNT MADESLITGE AMPVTKKPGS TVIAGSINAH GSVLIKATHV GNDTTLAQIV 

       910        920        930        940        950        960 
KLVEEAQMSK APIQQLADRF SGYFVPFIII MSTLTLVVWI VIGFIDFGVV QRYFPNPNKH 

       970        980        990       1000       1010       1020 
ISQTEVIIRF AFQTSITVLC IACPCSLGLA TPTAVMVGTG VAAQNGILIK GGKPLEMAHK 

      1030       1040       1050       1060       1070       1080 
IKTVMFDKTG TITHGVPRVM RVLLLGDVAT LPLRKVLAVV GTAEASSEHP LGVAVTKYCK 

      1090       1100       1110       1120       1130       1140 
EELGTETLGY CTDFQAVPGC GIGCKVSNVE GILAHSERPL SAPASHLNEA GSLPAEKDAV 

      1150       1160       1170       1180       1190       1200 
PQTFSVLIGN REWLRRNGLT ISSDVSDAMT DHEMKGQTAI LVAIDGVLCG MIAIADAVKQ 

      1210       1220       1230       1240       1250       1260 
EAALAVHTLQ SMGVDVVLIT GDNRKTARAI ATQVGINKVF AEVLPSHKVA KVQELQNKGK 

      1270       1280       1290       1300       1310       1320 
KVAMVGDGVN DSPALAQADM GVAIGTGTDV AIEAADVVLI RNDLLDVVAS IHLSKRTVRR 

      1330       1340       1350       1360       1370       1380 
IRINLVLALI YNLVGIPIAA GVFMPIGIVL QPWMGSAAMA ASSVSVVLSS LQLKCYKKPD 

      1390       1400       1410       1420       1430       1440 
LERYEAQAHG HMKPLTASQV SVHIGMDDRW RDSPRATPWD QVSYVSQVSL SSLTSDKPSR 

      1450       1460 
HSAAADDDGD KWSLLLNGRD EEQYI 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 43346B705BDAFDE7
Show »

FASTA1,258133,617
Isoform 3 [UniParc].

Checksum: E0581E07091B1C9C
Show »

FASTA1,354145,818
Isoform 4 [UniParc].

Checksum: C6A6A7C4BB2AC61D
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FASTA1,447155,125

References

« Hide 'large scale' references
[1]"Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: genomic organization, alternative splicing, and structure/function predictions."
Petrukhin K., Lutsenko S., Chernov I., Ross B.M., Kaplan J.H., Gilliam T.C.
Hum. Mol. Genet. 3:1647-1656(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-96; ARG-875 AND LYS-952.
[2]"Molecular cloning of mutant ATP7B."
Carlini E.J., Booth-Genthe C.L.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS ALA-406; LEU-456; LYS-952 AND ALA-1140.
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Cloning and characterization of the promoter region of the Wilson disease gene."
Oh W.J., Kim E.K., Park K.D., Hahn S.H., Yoo O.J.
Biochem. Biophys. Res. Commun. 259:206-211(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[5]"The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene."
Bull P.C., Thomas G.R., Rommens J.M., Forbes J.R., Cox D.W.
Nat. Genet. 5:327-337(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-1465 (ISOFORM 1), VARIANT LYS-952.
[6]Cox D.W.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[7]"The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene."
Tanzi R.E., Petrukhin K., Chernov I., Pellequer J.L., Wasco W., Ross B., Romano D.M., Parano E., Pavone L., Brzustowicz L.M., Devoto M., Peppercorn J., Bush A.I., Sternlieb I., Pirastu M., Gusella J.F., Evgrafov O., Penchaszadeh G.K. expand/collapse author list , Honig B., Edelman I.S., Soares M.B., Scheinberg I.H., Gilliam T.C.
Nat. Genet. 5:344-350(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-1465 (ISOFORM 2), VARIANTS WD GLN-1069 AND SER-1270, VARIANT ARG-875.
[8]"Isolation and characterization of a human liver cDNA as a candidate gene for Wilson disease."
Yamaguchi Y., Heiny M.E., Gitlin J.D.
Biochem. Biophys. Res. Commun. 197:271-277(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 488-837 (ISOFORM 4), VARIANT ARG-832.
Tissue: Liver.
[9]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 786-1465, VARIANTS ARG-832 AND ALA-1140.
Tissue: Brain.
[10]"The Wilson disease gene: spectrum of mutations and their consequences."
Thomas G.R., Forbes J.R., Roberts E.A., Walshe J.M., Cox D.W.
Nat. Genet. 9:210-216(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS WD, VARIANTS.
[11]Erratum
Thomas G.R., Forbes J.R., Roberts E.A., Walshe J.M., Cox D.W.
Nat. Genet. 9:451-451(1995)
[12]"Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments."
Yang X.-L., Miura N., Kawarada Y., Terada K., Petrukhin K., Gilliam T.C., Sugiyama T.
Biochem. J. 326:897-902(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
[13]"Localization of the Wilson's disease protein product to mitochondria."
Lutsenko S., Cooper M.J.
Proc. Natl. Acad. Sci. U.S.A. 95:6004-6009(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE PROTEOLYTIC CLEAVAGE.
[14]"The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein."
Tao T.Y., Liu F., Klomp L., Wijmenga C., Gitlin J.D.
J. Biol. Chem. 278:41593-41596(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COMMD1.
[15]"Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A."
Lim C.M., Cater M.A., Mercer J.F., La Fontaine S.
J. Biol. Chem. 281:14006-14014(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCTN4.
[16]"Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B."
LeShane E.S., Shinde U., Walker J.M., Barry A.N., Blackburn N.J., Ralle M., Lutsenko S.
J. Biol. Chem. 285:6327-6336(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING SITES, DOMAINS HMA.
[17]"Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1."
Banci L., Bertini I., Cantini F., Rosenzweig A.C., Yatsunyk L.A.
Biochemistry 47:7423-7429(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 238-439, COPPER-BINDING SITES, INTERACTION WITH ATOX1.
[18]"Molecular pathology and haplotype analysis of Wilson disease in Mediterranean populations."
Figus A., Angius A., Loudianos G., Bertini C., Dessi V., Loi A., Deiana M., Lovicu M., Olla N., Sole G., de Virgiliis S., Lilliu F., Farci A.M.G., Nurchi A., Giacchino R., Barabino A., Marazzi M., Zancan L. expand/collapse author list , Greggio N.A., Macellini M., Solinas A., Deplano A., Barbera C., Devoto M., Ozsoylu S., Kocak N., Akar N., Karayalcin S., Mokini V., Cullufi P., Balestrieri A., Cao A., Pirastu M.
Am. J. Hum. Genet. 57:1318-1324(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD, VARIANTS.
[19]"Efficient detection of mutations in Wilson disease by manifold sequencing."
Waldenstroem E., Lagerkvist A., Dahlman T., Westermark K., Landegren U.
Genomics 37:303-309(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD PHE-967; MET-977; ASP-1106; ARG-1153 AND SER-1355.
[20]"Wilson disease mutations associated with uncommon haplotypes in Mediterranean patients."
Loudianos G., Dessi V., Angius A., Lovicu M., Loi A., Deiana M., Akar N., Vajro P., Figus A., Cao A., Pirastu M.
Hum. Genet. 98:640-642(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD.
[21]"High frequency of two mutations in codon 778 in exon 8 of the ATP7B gene in Taiwanese families with Wilson disease."
Chuang L.-M., Wu H.-P., Jang M.-H., Wang T.-R., Sue W.-C., Lin B.J., Cox D.W., Tai T.-Y.
J. Med. Genet. 33:521-523(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD GLN-778 AND LEU-778.
[22]"Identification and analysis of mutations in the Wilson disease gene (ATP7B): population frequencies, genotype-phenotype correlation, and functional analyses."
Shah A.B., Chernov I., Zhang H.T., Ross B.M., Das K., Lutsenko S., Parano E., Pavone L., Evgrafov O., Ivanova-Smolenskaya I.A., Anneren G., Westermark K., Urrutia F.H., Penchaszadeh G.K., Sternlieb I., Scheinberg I.H., Gilliam T.C., Petrukhin K.
Am. J. Hum. Genet. 61:317-328(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD.
[23]"Identification of a novel missense mutation in Wilson's disease gene."
Fan Y., Yang R., Yu L., Wu M., Shi S., Ren M., Han Y., Hu J., Zhao S.
Chin. Med. J. 110:887-890(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD CYS-693.
[24]"24 bp deletion and Ala1278 to Val mutation of the ATP7B gene in a Sardinian family with Wilson disease."
Orru S., Thomas G., Loizedda A., Cox D.W., Contu L.
Hum. Mutat. 10:84-85(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD VAL-1278 AND 1285-GLY--ILE-1292 DEL.
[25]"A homozygous nonsense mutation and a combination of two mutations of the Wilson disease gene in patients with different lysyl oxidase activities in cultured fibroblasts."
Kemppainen R., Palatsi R., Kallioinen M., Oikarinen A.
J. Invest. Dermatol. 108:35-39(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD LYS-1038.
[26]"His1069Gln and six novel Wilson disease mutations: analysis of relevance for early diagnosis and phenotype."
Ha-Hao D., Hefter H., Stremmel W., Castaneda-Guillot C., Hernandez Hernandez A., Cox D.W., Auburger G.
Eur. J. Hum. Genet. 6:616-623(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD ALA-710; CYS-741; ILE-1031; GLN-1069 AND ARG-1176, VARIANTS LEU-456; GLY-949 AND ALA-1140.
[27]"Novel ATP7B mutations causing Wilson disease in several Israeli ethnic groups."
Kalinsky H., Funes A., Zeldin A., Pel-Or Y., Korostishevsky M., Gershoni-Baruch R., Farrer L.A., Bonne-Tamir B.
Hum. Mutat. 11:145-151(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD ARG-645; ASN-765; GLN-969; ALA-1064; GLN-1069; VAL-1213 AND 1216-VAL-VAL-1217 DEL, VARIANTS SER-565; GLY-723; ARG-832 AND ALA-1140.
[28]"Identification of three novel mutations and a high frequency of the Arg778Leu mutation in Korean patients with Wilson disease."
Kim E.K., Yoo O.J., Song K.Y., Yoo H.W., Choi S.Y., Cho S.W., Hahn S.H.
Hum. Mutat. 11:275-278(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-778; VAL-874 AND PHE-1083, VARIANTS ARG-832; ILE-864; MET-1109 AND ALA-1140.
[29]"Mutations of ATP7B gene in Wilson disease in Japan: identification of nine mutations and lack of clear founder effect in a Japanese population."
Yamaguchi A., Matsuura A., Arashima S., Kikuchi Y., Kikuchi K.
Hum. Mutat. Suppl. 1:S320-S322(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-778; VAL-874; GLY-919; SER-1186; ALA-1267 AND SER-1270.
[30]"Further delineation of the molecular pathology of Wilson disease in the Mediterranean population."
Loudianos G., Dessi V., Lovicu M., Angius A., Nurchi A., Sturniolo G.C., Marcellini M., Zancan L., Bragetti P., Akar N., Yagci R., Vegnente A., Cao A., Pirastu M.
Hum. Mutat. 12:89-94(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD VAL-85; SER-492; 608-PHE-ASP-609 DELINS TYR; HIS-642; ARG-645; ILE-665; ARG-691; PHE-747; TRP-778; LEU-840; ASN-918; TRP-919; ASN-921; PRO-933; LEU-992; THR-1003; VAL-1018; TRP-1041; VAL-1089; MET-1146; GLY-1183; THR-1183; MET-1216; ASP-1341 AND SER-1358.
[31]"Mutation analysis of Wilson disease in Taiwan and description of six new mutations."
Tsai C.-H., Tsai F.-J., Wu J.-Y., Chang J.-G., Lee C.-C., Lin S.-P., Yang C.-F., Jong Y.-J., Lo M.-C.
Hum. Mutat. 12:370-376(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD.
[32]"Missense mutations of exons 14 and 18 of Wilson's disease gene in Chinese patients."
Wu Z., Wang N., Murong S., Lin M.
Zhonghua Yi Xue Yi Chuan Xue Za Zhi 16:91-93(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD PRO-1041.
[33]"Mutation analysis in patients with Wilson disease: identification of 4 novel mutations."
Haas R., Gutierrez-Rivero B., Knoche J., Boeker K., Manns M.P., Schmidt H.H.-J.
Hum. Mutat. 14:88-88(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD 670-TYR-MET-671 DEL; TYR-985 AND THR-1148.
[34]"Molecular characterization of Wilson disease in the Sardinian population -- evidence of a founder effect."
Loudianos G., Dessi V., Lovicu M., Angius A., Figus A., Lilliu F., De Virgiliis S., Nurchi A.M., Deplano A., Moi P., Pirastu M., Cao A.
Hum. Mutat. 14:294-303(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD.
[35]"A study of Wilson disease mutations in Britain."
Curtis D., Durkie M., Balac P., Sheard D., Goodeve A., Peake I., Quarrell O., Tanner S.
Hum. Mutat. 14:304-311(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD.
[36]"The His1069Gln mutation in the ATP7B gene in Russian patients with Wilson disease."
Ivanova-Smolenskaya I.A., Ovchinnikov I.V., Karabanov A.V., Deineko N.L., Poleshchuk V.V., Markova E.D., Illarioshkin S.N.
J. Med. Genet. 36:174-174(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD GLN-1069.
[37]"Mutation analysis in patients of Mediterranean descent with Wilson disease: identification of 19 novel mutations."
Loudianos G., Dessi V., Lovicu M., Angius A., Altuntas B., Giacchino R., Marazzi M., Marcellini M., Sartorelli M.R., Sturniolo G.C., Kocak N., Yuce A., Akar N., Pirastu M., Cao A.
J. Med. Genet. 36:833-836(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD SER-710; ARG-711; LEU-840; VAL-874; GLN-969; VAL-1003; TRP-1041; PRO-1041; GLU-1061; VAL-1063; GLY-1068; GLN-1069; GLU-1089; PHE-1104; HIS-1151; THR-1169; LYS-1173; VAL-1222; PHE-1262; VAL-1327; PHE-1363 AND MET-1434, VARIANTS ARG-1207 AND ILE-1297.
[38]"Molecular analysis and diagnosis in Japanese patients with Wilson's disease."
Shimizu N., Nakazono H., Takeshita Y., Ikeda C., Fujii H., Watanabe A., Yamaguchi Y., Hemmi H., Shimatake H., Aoki T.
Pediatr. Int. 41:409-413(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-778; VAL-874; GLY-919; ILE-1029; VAL-1035; SER-1186 AND ASN-1222.
[39]"Delineation of the spectrum of Wilson disease mutations in the Greek population and the identification of six novel mutations."
Loudianos G., Lovicu M., Solinas P., Kanavakis E., Tzetis M., Manolaki N., Panagiotakaki E., Karpathios T., Cao A.
Genet. Test. 4:399-402(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD SER-486; GLY-778; MET-890; GLN-969; GLU-1061; GLN-1069; SER-1099 AND THR-1148.
[40]"High prevalence of the very rare Wilson disease gene mutation Leu708Pro in the Island of Gran Canaria (Canary Islands, Spain): a genetic and clinical study."
Garcia-Villarreal L., Daniels S., Shaw S.H., Cotton D., Galvin M., Geskes J., Bauer P., Sierra-Hernandez A., Buckler A., Tugores A.
Hepatology 32:1329-1336(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD PRO-708.
[41]"Mutational analysis of ATP7B and genotype-phenotype correlation in Japanese with Wilson's disease."
Okada T., Shiono Y., Hayashi H., Satoh H., Sawada T., Suzuki A., Takeda Y., Yano M., Michitaka K., Onji M., Mabuchi H.
Hum. Mutat. 15:454-462(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD ILE-769; LEU-778; TRP-778; VAL-874; GLY-919; THR-1003; PHE-1083; SER-1186; ALA-1267; SER-1270; THR-1336 AND PRO-1373, VARIANTS ALA-406; LEU-456 AND ALA-1140.
[42]"Novel mutations of the ATP7B gene in Japanese patients with Wilson disease."
Kusuda Y., Hamaguchi K., Mori T., Shin R., Seike M., Sakata T.
J. Hum. Genet. 45:86-91(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-778; VAL-874 AND VAL-1297 DEL, VARIANTS LEU-290; ALA-406; LEU-456; ARG-832; ALA-1140 AND GLU-1407.
[43]"Molecular analysis of Wilson disease in Taiwan: identification of one novel mutation and evidence of haplotype-mutation association."
Lee C.C., Wu J.Y., Tsai F.J., Kodama H., Abe T., Yang C.F., Tsai C.H.
J. Hum. Genet. 45:275-279(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD GLY-1279.
[44]"Three novel mutations (P760L, L1305P, Q1351Stop) causing Wilson disease."
Genschel J., Czlonkowska A., Sommer G., Buettner C., Bochow B., Lochs H., Schmidt H.
Hum. Mutat. 17:156-156(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-760 AND PRO-1305.
[45]"High prevalence of the H1069Q mutation in East German patients with Wilson disease: rapid detection of mutations by limited sequencing and phenotype-genotype analysis."
Caca K., Ferenci P., Kuehn H.-J., Polli C., Willgerodt H., Kunath B., Hermann W., Moessner J., Berr F.
J. Hepatol. 35:575-581(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD TRP-616; ALA-710; SER-710; LEU-760; ASN-765; VAL-769; GLN-969; LEU-992; GLN-1069 AND SER-1270, VARIANTS ALA-406; LEU-456 AND ARG-832.
[46]"Molecular diagnosis of Wilson disease."
Butler P., McIntyre N., Mistry P.K.
Mol. Genet. Metab. 72:223-230(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD TRP-778; ARG-898; GLN-1069; THR-1102 AND ARG-1266.
[47]"Presymptomatic diagnosis of Wilson disease associated with a novel mutation of the ATP7B gene."
Ohya K., Abo W., Tamaki H., Sugawara C., Endo T., Nomachi S., Fukushi M., Kinebuchi M., Matsuura A.
Eur. J. Pediatr. 161:124-126(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD PHE-1083 AND ASN-1296.
[48]"Identification of novel mutations and the three most common mutations in the human ATP7B gene of Korean patients with Wilson disease."
Yoo H.-W.
Genet. Med. 4:43S-48S(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD HIS-768; LEU-778; VAL-874; PHE-1083; SER-1168; ILE-1255; ALA-1267 AND SER-1270.
[49]"Abnormal mRNA splicing resulting from consensus sequence splicing mutations of ATP7B."
Loudianos G., Lovicu M., Dessi V., Tzetis M., Kanavakis E., Zancan L., Zelante L., Galvez-Galvez C., Cao A.
Hum. Mutat. 20:260-266(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD PRO-721 AND GLY-1183.
[50]"Two families with Wilson disease in which siblings showed different phenotypes."
Takeshita Y., Shimizu N., Yamaguchi Y., Nakazono H., Saitou M., Fujikawa Y., Aoki T.
J. Hum. Genet. 47:543-547(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-778; VAL-874 AND GLY-919.
[51]"Mutation spectrum and polymorphisms in ATP7B identified on direct sequencing of all exons in Chinese Han and Hui ethnic patients with Wilson's disease."
Gu Y.-H., Kodama H., Du S.-L., Gu Q.-J., Sun H.-J., Ushijima H.
Clin. Genet. 64:479-484(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD VAL-85; GLY-765; LEU-778; MET-890; GLY-919; MET-935; TYR-975; LEU-992; ARG-1098; THR-1148; LYS-1173 AND ASN-1248, VARIANTS ASP-14; ALA-406; LEU-456; ARG-832; ALA-1140; ASN-1143 AND SER-1245.
[52]"A rare homozygous missense mutation in ATP7B exon 19 in a case of Wilson disease."
Majumdar R., Al Jumah M., Zaidan R.
Eur. Neurol. 51:52-54(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD SER-1341.
[53]"Wilson disease: novel mutations in the ATP7B gene and clinical correlation in Brazilian patients."
Deguti M.M., Genschel J., Cancado E.L.R., Barbosa E.R., Bochow B., Mucenic M., Porta G., Lochs H., Carrilho F.J., Schmidt H.H.-J.
Hum. Mutat. 23:398-398(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD SER-41; GLY-949; LEU-1094; PRO-1232 AND ARG-1373.
[54]"Strokelike presentation of Wilson disease with homozygosity for a novel T766R mutation."
Pendlebury S.T., Rothwell P.M., Dalton A., Burton E.A.
Neurology 63:1982-1983(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD ARG-766.
[55]"Correlation of ATP7B genotype with phenotype in Chinese patients with Wilson disease."
Liu X.-Q., Zhang Y.-F., Liu T.-T., Hsiao K.-J., Zhang J.-M., Gu X.-F., Bao K.-R., Yu L.-H., Wang M.-X.
World J. Gastroenterol. 10:590-593(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD LEU-778; ASP-943; ILE-1106; ALA-1140 AND MET-1216.
[56]"Wilson disease: high prevalence in a mountainous area of Crete."
Dedoussis G.V.Z., Genschel J., Sialvera T.-E., Bochow B., Manolaki N., Manios Y., Tsafantakis E., Schmidt H.
Ann. Hum. Genet. 69:268-274(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD THR-1148 AND ARG-1176.
[57]"Identification and molecular characterization of 18 novel mutations in the ATP7B gene from Indian Wilson disease patients: genotype."
Kumar S., Thapa B.R., Kaur G., Prasad R.
Clin. Genet. 67:443-445(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD HIS-992; THR-1003; THR-1102; TYR-1104 AND ARG-1256.
[58]"Mutation analysis of Wilson disease in the Spanish population -identification of a prevalent substitution and eight novel mutations in the ATP7B gene."
Margarit E., Bach V., Gomez D., Bruguera M., Jara P., Queralt R., Ballesta F.
Clin. Genet. 68:61-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD ARG-645; LEU-690; ARG-869; SER-943; MET-977; GLU-1061; GLN-1069; SER-1099; MET-1216 AND PRO-1232, VARIANTS ALA-406; LEU-456; ARG-832 AND ALA-1140.
[59]"Spectrum of mutations in the Wilson disease gene (ATP7B) in the Bulgarian population."
Todorov T., Savov A., Jelev H., Panteleeva E., Konstantinova D., Krustev Z., Mihaylova V., Tournev I., Tankova L., Tzolova N., Kremensky I.
Clin. Genet. 68:474-476(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD GLN-616; ALA-626; TRP-778; GLY-778; VAL-874; GLN-969; THR-1003; GLN-1069; 1217-VAL-LEU-1218 DEL; SER-1270; TYR-1279; ASP-1341; SER-1352 AND PRO-1368.
[60]"Frameshift and nonsense mutations in the gene for ATPase7B are associated with severe impairment of copper metabolism and with an early clinical manifestation of Wilson's disease."
Gromadzka G., Schmidt H.H.-J., Genschel J., Bochow B., Rodo M., Tarnacka B., Litwin T., Chabik G., Czlonkowska A.
Clin. Genet. 68:524-532(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD GLN-616; TYR-639; TYR-653; PRO-776; GLY-778; MET-977; ARG-988; LEU-992; GLN-1069; PRO-1095; MET-1220; LEU-1273 AND ASP-1341.
[61]"Twenty-four novel mutations in Wilson disease patients of predominantly European ancestry."
Cox D.W., Prat L., Walshe J.M., Heathcote J., Gaffney D.
Hum. Mutat. 26:280-280(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD HIS-532; ASP-591; PRO-604; SER-641; TYR-703; VAL-710; GLY-756; MET-766; THR-861; CYS-943; MET-991; THR-996; ARG-1000; GLU-1176; GLU-1221; SER-1287; SER-1331; VAL-1341; SER-1375 AND SER-1379.
[62]"Mutation analysis of the ATP7B gene and genotype/phenotype correlation in 227 patients with Wilson disease."
Vrabelova S., Letocha O., Borsky M., Kozak L.
Mol. Genet. Metab. 86:277-285(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD SER-641; SER-710; ARG-737; GLY-778; GLU-918; GLN-969; MET-977; VAL-1018; SER-1033; TRP-1041; VAL-1063; LYS-1064; GLN-1069; THR-1102; ASP-1111; THR-1148; ARG-1176; SER-1186; ASN-1271; LEU-1273; PRO-1305; ASP-1341 AND CYS-1355, VARIANTS LEU-456; ARG-832 AND ALA-1140.
[63]"Early and severe liver disease associated with homozygosity for an exon 7 mutation, G691R, in Wilson's disease."
Barada K., Nemer G., ElHajj I.I., Touma J., Cortas N., Boustany R.-M., Usta J.
Clin. Genet. 72:264-267(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WD ARG-691.
[64]"New mutations in the Wilson disease gene, ATP7B: implications for molecular testing."
Davies L.P., Macintyre G., Cox D.W.
Genet. Test. 12:139-145(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD ALA-536; ARG-657; VAL-971; MET-974; PRO-1004; ALA-1149; ASN-1164; GLY-1173; THR-1228; VAL-1230; VAL-1267; THR-1328 AND ILE-1359, VARIANTS ALA-406; LEU-456; ARG-832; LYS-952 AND ALA-1140.
[65]"Sequence variation in the ATP-binding domain of the Wilson disease transporter, ATP7B, affects copper transport in a yeast model system."
Hsi G., Cullen L.M., Macintyre G., Chen M.M., Glerum D.M., Cox D.W.
Hum. Mutat. 29:491-501(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS WD HIS-532; ALA-626; HIS-642; TRP-1041; LYS-1064; PHE-1083; ASP-1106; ALA-1140; VAL-1169; THR-1183 AND SER-1186.
[66]"Phenotypic and genetic characterization of a cohort of pediatric Wilson disease patients."
Abdel Ghaffar T.Y., Elsayed S.M., Elnaghy S., Shadeed A., Elsobky E.S., Schmidt H.
BMC Pediatr. 11:56-56(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WD PRO-549; HIS-642; TYR-703; PRO-744; ASN-765; GLY-778; MET-977; ASP-998; VAL-1063; GLN-1069; ARG-1207; LEU-1273; ASP-1332; ARG-1341 AND ASP-1341.
[67]"Diagnostic challenges of Wilson's disease presenting as acute pancreatitis, cholangitis, and jaundice."
Nussinson E., Shahbari A., Shibli F., Chervinsky E., Trougouboff P., Markel A.
World J. Hepatol. 5:649-653(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-1140.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11700 mRNA. Translation: AAA92667.1.
DQ015922 mRNA. Translation: AAY41166.1.
AL139082, AL138821, AL162377 Genomic DNA. Translation: CAI12888.1.
AL162377, AL138821, AL139082 Genomic DNA. Translation: CAI13428.1.
AL138821, AL139082, AL162377 Genomic DNA. Translation: CAI13743.1.
AF034838 Genomic DNA. Translation: AAD01998.1.
U03464 mRNA. Translation: AAB52902.1.
L25591 mRNA. Translation: AAA79211.1. Frameshift.
L25591 mRNA. Translation: AAA79212.1. Frameshift.
L25442 mRNA. Translation: AAA16173.1. Frameshift.
AB209461 mRNA. Translation: BAD92698.1.
S77446 Genomic DNA. Translation: AAD14987.1.
S77447 Genomic DNA. Translation: AAB34086.1.
S77450 Genomic DNA. Translation: AAB34087.1.
PIRI78536.
I78537.
S78555.
RefSeqNP_000044.2. NM_000053.3.
NP_001230111.1. NM_001243182.1.
XP_005266487.1. XM_005266430.2.
UniGeneHs.492280.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ARFNMR-A1036-1196[»]
2EW9NMR-A486-633[»]
2KOYNMR-A1036-1196[»]
2LQBNMR-A141-212[»]
2ROPNMR-A238-439[»]
ProteinModelPortalP35670.
SMRP35670. Positions 58-1379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107022. 9 interactions.
MINTMINT-105941.
STRING9606.ENSP00000242839.

Protein family/group databases

TCDB3.A.3.5.3. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP35670.

Polymorphism databases

DMDM239938919.

Proteomic databases

PaxDbP35670.
PRIDEP35670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242839; ENSP00000242839; ENSG00000123191. [P35670-1]
ENST00000344297; ENSP00000342559; ENSG00000123191. [P35670-2]
ENST00000400366; ENSP00000383217; ENSG00000123191. [P35670-3]
GeneID540.
KEGGhsa:540.
UCSCuc001vfv.2. human. [P35670-1]
uc001vfx.2. human. [P35670-2]
uc001vfy.2. human. [P35670-3]

Organism-specific databases

CTD540.
GeneCardsGC13M052506.
HGNCHGNC:870. ATP7B.
HPAHPA013187.
MIM277900. phenotype.
606882. gene.
neXtProtNX_P35670.
Orphanet905. Wilson disease.
PharmGKBPA73.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250397.
HOVERGENHBG050616.
InParanoidP35670.
KOK17686.
OMAMRRNGLT.
OrthoDBEOG7C2R0G.
PhylomeDBP35670.
TreeFamTF300460.

Enzyme and pathway databases

BRENDA3.6.3.4. 2681.
ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP35670.
BgeeP35670.
CleanExHS_ATP7B.
GenevestigatorP35670.

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.
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

EvolutionaryTraceP35670.
GeneWikiWilson_disease_protein.
GenomeRNAi540.
NextBio2239.
PROP35670.
SOURCESearch...

Entry information

Entry nameATP7B_HUMAN
AccessionPrimary (citable) accession number: P35670
Secondary accession number(s): Q16318 expand/collapse secondary AC list , Q16319, Q4U3V3, Q59FJ9, Q5T7X7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 164 of the entry and version 4 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM