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Q04656

- ATP7A_HUMAN

UniProt

Q04656 - ATP7A_HUMAN

Protein

Copper-transporting ATPase 1

Gene

ATP7A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 3 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1044 – 104414-aspartylphosphate intermediateBy similarity
    Metal bindingi1301 – 13011MagnesiumPROSITE-ProRule annotation
    Metal bindingi1305 – 13051MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: HGNC
    2. copper-dependent protein binding Source: UniProtKB
    3. copper-exporting ATPase activity Source: UniProtKB
    4. copper ion binding Source: UniProtKB
    5. copper ion transmembrane transporter activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. superoxide dismutase copper chaperone activity Source: UniProtKB

    GO - Biological processi

    1. blood vessel development Source: UniProtKB
    2. blood vessel remodeling Source: UniProtKB
    3. cartilage development Source: UniProtKB
    4. catecholamine metabolic process Source: UniProtKB
    5. cellular copper ion homeostasis Source: UniProtKB
    6. central nervous system neuron development Source: UniProtKB
    7. cerebellar Purkinje cell differentiation Source: UniProtKB
    8. collagen fibril organization Source: UniProtKB
    9. copper ion export Source: UniProtKB
    10. copper ion import Source: UniProtKB
    11. copper ion transport Source: UniProtKB
    12. dendrite morphogenesis Source: Ensembl
    13. detoxification of copper ion Source: UniProtKB
    14. dopamine metabolic process Source: UniProtKB
    15. elastic fiber assembly Source: UniProtKB
    16. elastin biosynthetic process Source: UniProtKB
    17. epinephrine metabolic process Source: UniProtKB
    18. extracellular matrix organization Source: UniProtKB
    19. hair follicle morphogenesis Source: UniProtKB
    20. in utero embryonic development Source: Ensembl
    21. ion transmembrane transport Source: Reactome
    22. lactation Source: Ensembl
    23. locomotory behavior Source: UniProtKB
    24. lung alveolus development Source: UniProtKB
    25. mitochondrion organization Source: UniProtKB
    26. negative regulation of metalloenzyme activity Source: UniProtKB
    27. negative regulation of neuron apoptotic process Source: Ensembl
    28. neuron projection morphogenesis Source: UniProtKB
    29. norepinephrine biosynthetic process Source: Ensembl
    30. norepinephrine metabolic process Source: UniProtKB
    31. peptidyl-lysine modification Source: UniProtKB
    32. pigmentation Source: UniProtKB
    33. positive regulation of catalytic activity Source: UniProtKB
    34. positive regulation of metalloenzyme activity Source: UniProtKB
    35. positive regulation of oxidoreductase activity Source: UniProtKB
    36. pyramidal neuron development Source: UniProtKB
    37. regulation of gene expression Source: Ensembl
    38. regulation of oxidative phosphorylation Source: UniProtKB
    39. release of cytochrome c from mitochondria Source: Ensembl
    40. removal of superoxide radicals Source: UniProtKB
    41. response to iron(III) ion Source: Ensembl
    42. response to zinc ion Source: Ensembl
    43. serotonin metabolic process Source: UniProtKB
    44. skin development Source: UniProtKB
    45. T-helper cell differentiation Source: UniProtKB
    46. transmembrane transport Source: Reactome
    47. tryptophan metabolic process Source: UniProtKB
    48. tyrosine metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Copper transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.6.3.4. 2681.
    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_25149. Ion transport by P-type ATPases.
    SABIO-RKQ04656.

    Protein family/group databases

    TCDBi3.A.3.5.6. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Copper-transporting ATPase 1 (EC:3.6.3.54)
    Alternative name(s):
    Copper pump 1
    Menkes disease-associated protein
    Gene namesi
    Name:ATP7A
    Synonyms:MC1, MNK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:869. ATP7A.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB
    2. brush border membrane Source: Ensembl
    3. cytosol Source: UniProtKB-SubCell
    4. endoplasmic reticulum Source: UniProtKB
    5. Golgi apparatus Source: UniProtKB
    6. integral component of membrane Source: UniProtKB-KW
    7. late endosome Source: UniProtKB
    8. membrane Source: UniProtKB
    9. neuronal cell body Source: UniProtKB
    10. neuron projection Source: UniProtKB
    11. perinuclear region of cytoplasm Source: UniProtKB
    12. plasma membrane Source: UniProtKB
    13. secretory granule Source: Ensembl
    14. trans-Golgi network Source: UniProtKB
    15. trans-Golgi network transport vesicle Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti629 – 6291A → P in MNKD. 1 Publication
    VAR_000699
    Natural varianti706 – 7061L → R in MNKD. 1 Publication
    VAR_023261
    Natural varianti727 – 7271G → R in MNKD. 1 Publication
    VAR_000700
    Natural varianti844 – 8441R → H in MNKD. 1 Publication
    VAR_023262
    Natural varianti853 – 8531G → R in MNKD. 1 Publication
    VAR_023263
    Natural varianti860 – 8601G → V in MNKD. 1 Publication
    VAR_023264
    Natural varianti873 – 8731L → R in MNKD. 1 Publication
    VAR_010001
    Natural varianti876 – 8761G → E in MNKD. 1 Publication
    VAR_010002
    Natural varianti876 – 8761G → R in MNKD. 1 Publication
    VAR_023265
    Natural varianti924 – 9241Q → R in MNKD. 1 Publication
    VAR_023266
    Natural varianti1000 – 10001C → R in MNKD. 1 Publication
    VAR_010003
    Natural varianti1006 – 10061L → P in MNKD. 1 Publication
    VAR_000701
    Natural varianti1007 – 10071A → V in MNKD. 1 Publication
    VAR_023267
    Natural varianti1015 – 10151G → D in MNKD. 1 Publication
    VAR_023268
    Natural varianti1019 – 10191G → D in MNKD. 1 Publication
    VAR_000702
    Natural varianti1044 – 10441D → G in MNKD. 1 Publication
    VAR_023269
    Natural varianti1048 – 10481T → I in MNKD. 1 Publication
    VAR_068831
    Natural varianti1100 – 11001L → P in MNKD. 1 Publication
    VAR_023270
    Natural varianti1118 – 11181G → D in MNKD. 1 Publication
    VAR_023271
    Natural varianti1255 – 12551G → R in MNKD. 1 Publication
    VAR_023272
    Natural varianti1282 – 12821K → E in MNKD. 1 Publication
    VAR_023273
    Natural varianti1300 – 13001G → E in MNKD. 1 Publication
    VAR_010004
    Natural varianti1302 – 13021G → R in MNKD. 1 Publication
    VAR_010005
    Natural varianti1302 – 13021G → V in MNKD. 1 Publication
    VAR_010006
    Natural varianti1304 – 13041N → K in MNKD. 1 Publication
    VAR_023274
    Natural varianti1305 – 13051D → A in MNKD. 1 Publication
    VAR_010007
    Natural varianti1315 – 13151G → R in MNKD. 1 Publication
    VAR_023275
    Natural varianti1325 – 13251A → V in MNKD. 1 Publication
    VAR_023276
    Natural varianti1344 – 13441S → R in MNKD. 1 Publication
    VAR_023277
    Natural varianti1345 – 13451I → F in MNKD. 1 Publication
    VAR_023278
    Natural varianti1362 – 13621A → V in MNKD. 1 Publication
    VAR_010008
    Natural varianti1369 – 13691G → R in MNKD. 1 Publication
    VAR_023279
    Natural varianti1397 – 13971S → F in MNKD. 1 Publication
    VAR_023280
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti637 – 6371S → L in OHS. 1 Publication
    Corresponds to variant rs28936068 [ dbSNP | Ensembl ].
    VAR_009999
    Natural varianti1304 – 13041N → S in OHS; has approximately 33% residual copper transport. 1 Publication
    VAR_063883
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti994 – 9941T → I in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some of the mutant protein remaining in the Golgi apparatus after exposure to copper. 1 Publication
    VAR_063882
    Natural varianti1386 – 13861P → S in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper. 1 Publication
    VAR_063884

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1487 – 14882LL → AA: Loss of relocalization to the trans-Golgi. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi300489. phenotype.
    304150. phenotype.
    309400. phenotype.
    Orphaneti565. Menkes disease.
    198. Occipital horn syndrome.
    139557. X-linked distal spinal muscular atrophy.
    PharmGKBiPA72.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15001500Copper-transporting ATPase 1PRO_0000046311Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei339 – 3391Phosphoserine1 Publication
    Modified residuei357 – 3571PhosphoserineBy similarity
    Glycosylationi686 – 6861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi975 – 9751N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1212 – 12121PhosphothreonineBy similarity
    Modified residuei1466 – 14661PhosphoserineBy similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ04656.
    PaxDbiQ04656.
    PRIDEiQ04656.

    PTM databases

    PhosphoSiteiQ04656.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    BgeeiQ04656.
    CleanExiHS_ATP7A.
    GenevestigatoriQ04656.

    Organism-specific databases

    HPAiHPA012887.

    Interactioni

    Subunit structurei

    Monomer. Interacts with PDZD11.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDZD11Q5EBL84EBI-7706409,EBI-1644207

    Protein-protein interaction databases

    BioGridi107020. 6 interactions.
    IntActiQ04656. 1 interaction.
    MINTiMINT-106053.
    STRINGi9606.ENSP00000345728.

    Structurei

    Secondary structure

    1
    1500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Beta strandi8 – 147
    Helixi20 – 3112
    Beta strandi33 – 353
    Beta strandi36 – 427
    Turni43 – 464
    Beta strandi47 – 526
    Turni54 – 563
    Helixi59 – 6810
    Beta strandi73 – 775
    Beta strandi165 – 1695
    Beta strandi171 – 1777
    Turni180 – 1823
    Helixi187 – 1948
    Beta strandi199 – 2046
    Turni207 – 2093
    Beta strandi210 – 2156
    Turni217 – 2193
    Helixi222 – 23110
    Beta strandi236 – 2383
    Turni242 – 2443
    Beta strandi277 – 2859
    Helixi288 – 29912
    Beta strandi305 – 3117
    Turni312 – 3154
    Beta strandi316 – 3216
    Beta strandi324 – 3263
    Helixi329 – 3368
    Turni340 – 3423
    Beta strandi344 – 3463
    Beta strandi377 – 3848
    Helixi388 – 40013
    Beta strandi408 – 4114
    Turni412 – 4154
    Beta strandi416 – 4216
    Turni423 – 4253
    Helixi428 – 43811
    Beta strandi441 – 4466
    Beta strandi488 – 4958
    Helixi497 – 4993
    Helixi502 – 5109
    Beta strandi513 – 5186
    Turni523 – 5264
    Beta strandi527 – 5326
    Turni534 – 5363
    Helixi539 – 54911
    Beta strandi553 – 5575
    Beta strandi566 – 5716
    Turni575 – 5773
    Helixi578 – 5869
    Beta strandi592 – 5987
    Turni599 – 6024
    Beta strandi603 – 6086
    Turni610 – 6134
    Helixi614 – 62613
    Beta strandi628 – 6336
    Helixi808 – 8147
    Beta strandi818 – 8247
    Beta strandi826 – 8283
    Beta strandi833 – 8386
    Turni839 – 8413
    Beta strandi847 – 8493
    Beta strandi860 – 8623
    Beta strandi868 – 8703
    Turni872 – 8754
    Beta strandi887 – 8893
    Beta strandi894 – 8985
    Beta strandi901 – 9044
    Turni908 – 9103
    Helixi912 – 9198
    Turni920 – 9234
    Beta strandi1055 – 10617
    Turni1065 – 10673
    Helixi1070 – 107910
    Helixi1080 – 10823
    Beta strandi1083 – 10853
    Helixi1087 – 110014
    Beta strandi1112 – 11143
    Turni1115 – 11173
    Beta strandi1118 – 11236
    Helixi1127 – 11293
    Turni1135 – 11395
    Turni1150 – 11534
    Beta strandi1161 – 11666
    Turni1167 – 11715
    Helixi1172 – 11743
    Beta strandi1178 – 11836
    Helixi1185 – 11917
    Helixi1197 – 120812
    Beta strandi1212 – 12187
    Beta strandi1221 – 12299

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00282.
    ProteinModelPortaliQ04656.
    SMRiQ04656. Positions 1-633, 645-1413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04656.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 653653CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini676 – 71439ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini735 – 7417CytoplasmicSequence Analysis
    Topological domaini763 – 78119ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini803 – 936134CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini960 – 98930ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1012 – 1356345CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1375 – 138511ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1406 – 150095CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei654 – 67522HelicalSequence AnalysisAdd
    BLAST
    Transmembranei715 – 73420HelicalSequence AnalysisAdd
    BLAST
    Transmembranei742 – 76221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei782 – 80221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei937 – 95923HelicalSequence AnalysisAdd
    BLAST
    Transmembranei990 – 101122HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1357 – 137418HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1386 – 140520HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 7567HMA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini172 – 23867HMA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini278 – 34467HMA 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 44467HMA 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 55567HMA 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini565 – 63167HMA 6PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1486 – 150015PDZD11-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1487 – 14882Endocytosis signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi355 – 3628Poly-Ser

    Domaini

    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.

    Sequence similaritiesi

    Contains 6 HMA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2217.
    HOGENOMiHOG000250397.
    HOVERGENiHBG050616.
    KOiK17686.
    OMAiSAIEDCG.
    OrthoDBiEOG7C2R0G.
    PhylomeDBiQ04656.
    TreeFamiTF300460.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. 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]
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 6 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF55008. SSF55008. 6 hits.
    SSF56784. SSF56784. 2 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    TIGR00003. TIGR00003. 6 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 6 hits.
    PS50846. HMA_2. 6 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

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

    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.

    « Hide

    MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI     50
    IYDPKLQTPK TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW 100
    DHIQSTLLKT KGVTDIKIYP QKRTVAVTII PSIVNANQIK ELVPELSLDT 150
    GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM TCHSCTSTIE GKIGKLQGVQ 200
    RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK QPKYLKLGAI 250
    DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS 300
    ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE 350
    VESTSNSPSS SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS 400
    KKPGVKSIRV SLANSNGTVE YDPLLTSPET LRGAIEDMGF DATLSDTNEP 450
    LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD KEEGKNSSKC YIQVTGMTCA 500
    SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP MIAEFIRELG 550
    FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA 600
    TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW 650
    RRSFLVSLFF CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF 700
    LERQILPGLS VMNLLSFLLC VPVQFFGGWY FYIQAYKALK HKTANMDVLI 750
    VLATTIAFAY SLIILLVAMY ERAKVNPITF FDTPPMLFVF IALGRWLEHI 800
    AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE LVQRGDIIKV 850
    VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL 900
    LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI 950
    ATLLVWIVIG FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC 1000
    PCSLGLATPT AVMVGTGVGA QNGILIKGGE PLEMAHKVKV VVFDKTGTIT 1050
    HGTPVVNQVK VLTESNRISH HKILAIVGTA ESNSEHPLGT AITKYCKQEL 1100
    DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN NIKNASLVQI 1150
    DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN 1200
    DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV 1250
    VLMTGDNSKT ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG 1300
    DGINDSPALA MANVGIAIGT GTDVAIEAAD VVLIRNDLLD VVASIDLSRE 1350
    TVKRIRINFV FALIYNLVGI PIAAGVFMPI GLVLQPWMGS AAMAASSVSV 1400
    VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI DDTSRNSPKL 1450
    GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL 1500
    Length:1,500
    Mass (Da):163,374
    Last modified:February 10, 2009 - v3
    Checksum:iCF8FF9EA061D463B
    GO
    Isoform 1 (identifier: Q04656-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,514
    Mass (Da):165,110
    Checksum:iB4FFD7472742EB62
    GO
    Isoform 2 (identifier: Q04656-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,581
    Mass (Da):172,078
    Checksum:iFDE210402FD79C4B
    GO
    Isoform 3 (identifier: Q04656-4) [UniParc]FASTAAdd to Basket

    Also known as: 2-16

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

    Note: Lacks 6 transmembrane regions and 5 heavy-metal-associated (HMA) domains.

    Show »
    Length:503
    Mass (Da):54,318
    Checksum:iB81B1F9FFB00B832
    GO
    Isoform 5 (identifier: Q04656-5) [UniParc]FASTAAdd to Basket

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

    Note: Lacks the transmembrane domains 3 and 4. Expressed at a low level in several tissues of normal individuals and is the only isoform found in patients with OHS.

    Show »
    Length:1,422
    Mass (Da):154,357
    Checksum:iEEB740B5F6841813
    GO
    Isoform 6 (identifier: Q04656-6) [UniParc]FASTAAdd to Basket

    Also known as: NML45

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

    Note: Lacks all transmembrane regions and 5 heavy-metal-associated (HMA) domains, but has a putative nuclear localization signal attached at the N-terminus.

    Show »
    Length:103
    Mass (Da):11,522
    Checksum:i1F3873EFB0EA6CC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101V → A no nucleotide entry (PubMed:9693104)Curated
    Sequence conflicti36 – 361V → E in AAA16974. (PubMed:8490647)Curated
    Sequence conflicti336 – 3361E → V in AAA35580. (PubMed:8490659)Curated
    Sequence conflicti336 – 3361E → V in AAA96010. (PubMed:7490081)Curated
    Sequence conflicti446 – 4461D → G in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti624 – 6241S → G in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti725 – 7251F → V in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti833 – 8331S → R in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti1099 – 10991E → K no nucleotide entry (PubMed:9693104)Curated
    Sequence conflicti1171 – 11711N → S in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti1178 – 11781Y → C no nucleotide entry (PubMed:9693104)Curated
    Sequence conflicti1178 – 11781Y → H in AAA35580. (PubMed:8490659)Curated
    Sequence conflicti1178 – 11781Y → H in CAB94714. (PubMed:7607665)Curated
    Sequence conflicti1178 – 11781Y → H in AAA96010. (PubMed:7490081)Curated
    Sequence conflicti1220 – 12201D → G in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti1295 – 12951R → W no nucleotide entry (PubMed:9693104)Curated
    Sequence conflicti1313 – 13131N → D no nucleotide entry (PubMed:9693104)Curated
    Sequence conflicti1336 – 13361N → D in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti1350 – 13501E → K in AAA35580. (PubMed:8490659)Curated
    Sequence conflicti1350 – 13501E → K in CAB94714. (PubMed:7607665)Curated
    Sequence conflicti1350 – 13501E → K in AAA96010. (PubMed:7490081)Curated
    Sequence conflicti1376 – 13761V → M in CAB08162. (PubMed:15772651)Curated
    Sequence conflicti1396 – 13961S → P no nucleotide entry (PubMed:9693104)Curated
    Sequence conflicti1409 – 14091L → R in CAB08160. (PubMed:15772651)Curated
    Sequence conflicti1455 – 14551R → W no nucleotide entry (PubMed:9693104)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti629 – 6291A → P in MNKD. 1 Publication
    VAR_000699
    Natural varianti637 – 6371S → L in OHS. 1 Publication
    Corresponds to variant rs28936068 [ dbSNP | Ensembl ].
    VAR_009999
    Natural varianti669 – 6691I → T.2 Publications
    Corresponds to variant rs2234935 [ dbSNP | Ensembl ].
    VAR_016119
    Natural varianti703 – 7031R → H.
    Corresponds to variant rs2234936 [ dbSNP | Ensembl ].
    VAR_016120
    Natural varianti706 – 7061L → R in MNKD. 1 Publication
    VAR_023261
    Natural varianti727 – 7271G → R in MNKD. 1 Publication
    VAR_000700
    Natural varianti767 – 7671V → L.1 Publication
    Corresponds to variant rs2227291 [ dbSNP | Ensembl ].
    VAR_010000
    Natural varianti844 – 8441R → H in MNKD. 1 Publication
    VAR_023262
    Natural varianti853 – 8531G → R in MNKD. 1 Publication
    VAR_023263
    Natural varianti860 – 8601G → V in MNKD. 1 Publication
    VAR_023264
    Natural varianti873 – 8731L → R in MNKD. 1 Publication
    VAR_010001
    Natural varianti876 – 8761G → E in MNKD. 1 Publication
    VAR_010002
    Natural varianti876 – 8761G → R in MNKD. 1 Publication
    VAR_023265
    Natural varianti924 – 9241Q → R in MNKD. 1 Publication
    VAR_023266
    Natural varianti994 – 9941T → I in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some of the mutant protein remaining in the Golgi apparatus after exposure to copper. 1 Publication
    VAR_063882
    Natural varianti1000 – 10001C → R in MNKD. 1 Publication
    VAR_010003
    Natural varianti1006 – 10061L → P in MNKD. 1 Publication
    VAR_000701
    Natural varianti1007 – 10071A → V in MNKD. 1 Publication
    VAR_023267
    Natural varianti1015 – 10151G → D in MNKD. 1 Publication
    VAR_023268
    Natural varianti1019 – 10191G → D in MNKD. 1 Publication
    VAR_000702
    Natural varianti1044 – 10441D → G in MNKD. 1 Publication
    VAR_023269
    Natural varianti1048 – 10481T → I in MNKD. 1 Publication
    VAR_068831
    Natural varianti1100 – 11001L → P in MNKD. 1 Publication
    VAR_023270
    Natural varianti1118 – 11181G → D in MNKD. 1 Publication
    VAR_023271
    Natural varianti1255 – 12551G → R in MNKD. 1 Publication
    VAR_023272
    Natural varianti1282 – 12821K → E in MNKD. 1 Publication
    VAR_023273
    Natural varianti1300 – 13001G → E in MNKD. 1 Publication
    VAR_010004
    Natural varianti1302 – 13021G → R in MNKD. 1 Publication
    VAR_010005
    Natural varianti1302 – 13021G → V in MNKD. 1 Publication
    VAR_010006
    Natural varianti1304 – 13041N → K in MNKD. 1 Publication
    VAR_023274
    Natural varianti1304 – 13041N → S in OHS; has approximately 33% residual copper transport. 1 Publication
    VAR_063883
    Natural varianti1305 – 13051D → A in MNKD. 1 Publication
    VAR_010007
    Natural varianti1315 – 13151G → R in MNKD. 1 Publication
    VAR_023275
    Natural varianti1325 – 13251A → V in MNKD. 1 Publication
    VAR_023276
    Natural varianti1344 – 13441S → R in MNKD. 1 Publication
    VAR_023277
    Natural varianti1345 – 13451I → F in MNKD. 1 Publication
    VAR_023278
    Natural varianti1362 – 13621A → V in MNKD. 1 Publication
    VAR_010008
    Natural varianti1369 – 13691G → R in MNKD. 1 Publication
    VAR_023279
    Natural varianti1386 – 13861P → S in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper. 1 Publication
    VAR_063884
    Natural varianti1397 – 13971S → F in MNKD. 1 Publication
    VAR_023280
    Natural varianti1464 – 14641I → V.
    Corresponds to variant rs2234938 [ dbSNP | Ensembl ].
    VAR_016121

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRKLSIRKRDNNLLK in isoform 1. 1 PublicationVSP_000419
    Alternative sequencei1 – 11M → MRKLSIRKRDNNLLKPSSAS SLGIAVSLGRPVLSRSSSGT VNLLEEVGLHIRDTAFSSTK LLEAISTVSAQVEELAVHNE CY in isoform 2. 1 PublicationVSP_000420
    Alternative sequencei1 – 11M → MRKLSIRKRDNNLLKECNEE IK in isoform 6. CuratedVSP_000421
    Alternative sequencei42 – 1038997Missing in isoform 3. 2 PublicationsVSP_000424Add
    BLAST
    Alternative sequencei53 – 8129DPKLQ…NPDPL → AHWFGFAALDGICSNGCFIC FCSTFFSSL in isoform 6. CuratedVSP_000422Add
    BLAST
    Alternative sequencei82 – 14991418Missing in isoform 6. CuratedVSP_000423Add
    BLAST
    Alternative sequencei725 – 80278Missing in isoform 5. CuratedVSP_000425Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06133 mRNA. Translation: AAA35580.1.
    X82336
    , 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
    , 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.
    CCDSiCCDS35339.1. [Q04656-1]
    PIRiS36149.
    RefSeqiNP_000043.4. NM_000052.6.
    NP_001269153.1. NM_001282224.1.
    UniGeneiHs.496414.
    Hs.733232.

    Genome annotation databases

    EnsembliENST00000341514; ENSP00000345728; ENSG00000165240. [Q04656-1]
    ENST00000343533; ENSP00000343026; ENSG00000165240. [Q04656-5]
    ENST00000350425; ENSP00000343678; ENSG00000165240. [Q04656-4]
    GeneIDi538.
    KEGGihsa:538.
    UCSCiuc004ecx.4. human. [Q04656-1]

    Polymorphism databases

    DMDMi223590241.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Heavy metal - Issue 79 of February 2007

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06133 mRNA. Translation: AAA35580.1 .
    X82336
    , 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
    , 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 .
    CCDSi CCDS35339.1. [Q04656-1 ]
    PIRi S36149.
    RefSeqi NP_000043.4. NM_000052.6.
    NP_001269153.1. NM_001282224.1.
    UniGenei Hs.496414.
    Hs.733232.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AW0 NMR - A 375-446 [» ]
    1KVI NMR - A 1-79 [» ]
    1KVJ NMR - A 1-79 [» ]
    1Q8L NMR - A 164-246 [» ]
    1S6O NMR - A 169-240 [» ]
    1S6U NMR - A 169-240 [» ]
    1Y3J NMR - A 486-558 [» ]
    1Y3K NMR - A 486-558 [» ]
    1YJR NMR - A 562-633 [» ]
    1YJT NMR - A 562-633 [» ]
    1YJU NMR - A 562-633 [» ]
    1YJV NMR - A 562-633 [» ]
    2AW0 NMR - A 375-446 [» ]
    2G9O NMR - A 275-352 [» ]
    2GA7 NMR - A 275-352 [» ]
    2K1R NMR - A 5-77 [» ]
    2KIJ NMR - A 806-924 [» ]
    2KMV NMR - A 1051-1231 [» ]
    2KMX NMR - A 1051-1231 [» ]
    3CJK X-ray 1.80 B 7-77 [» ]
    DisProti DP00282.
    ProteinModelPortali Q04656.
    SMRi Q04656. Positions 1-633, 645-1413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107020. 6 interactions.
    IntActi Q04656. 1 interaction.
    MINTi MINT-106053.
    STRINGi 9606.ENSP00000345728.

    Chemistry

    DrugBanki DB00958. Carboplatin.
    DB00515. Cisplatin.
    DB00526. Oxaliplatin.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q04656.

    Polymorphism databases

    DMDMi 223590241.

    Proteomic databases

    MaxQBi Q04656.
    PaxDbi Q04656.
    PRIDEi Q04656.

    Protocols and materials databases

    DNASUi 538.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341514 ; ENSP00000345728 ; ENSG00000165240 . [Q04656-1 ]
    ENST00000343533 ; ENSP00000343026 ; ENSG00000165240 . [Q04656-5 ]
    ENST00000350425 ; ENSP00000343678 ; ENSG00000165240 . [Q04656-4 ]
    GeneIDi 538.
    KEGGi hsa:538.
    UCSCi uc004ecx.4. human. [Q04656-1 ]

    Organism-specific databases

    CTDi 538.
    GeneCardsi GC0XP077166.
    GeneReviewsi ATP7A.
    HGNCi HGNC:869. ATP7A.
    HPAi HPA012887.
    MIMi 300011. gene.
    300489. phenotype.
    304150. phenotype.
    309400. phenotype.
    neXtProti NX_Q04656.
    Orphaneti 565. Menkes disease.
    198. Occipital horn syndrome.
    139557. X-linked distal spinal muscular atrophy.
    PharmGKBi PA72.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2217.
    HOGENOMi HOG000250397.
    HOVERGENi HBG050616.
    KOi K17686.
    OMAi SAIEDCG.
    OrthoDBi EOG7C2R0G.
    PhylomeDBi Q04656.
    TreeFami TF300460.

    Enzyme and pathway databases

    BRENDAi 3.6.3.4. 2681.
    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_25149. Ion transport by P-type ATPases.
    SABIO-RK Q04656.

    Miscellaneous databases

    ChiTaRSi ATP7A. human.
    EvolutionaryTracei Q04656.
    GeneWikii ATP7A.
    GenomeRNAii 538.
    NextBioi 2231.
    PROi Q04656.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04656.
    CleanExi HS_ATP7A.
    Genevestigatori Q04656.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. 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 ]
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 6 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF55008. SSF55008. 6 hits.
    SSF56784. SSF56784. 2 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    TIGR00003. TIGR00003. 6 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 6 hits.
    PS50846. HMA_2. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: VARIANTS DSMAX3 ILE-994 AND SER-1386, CHARACTERIZATION OF VARIANTS DSMAX3 ILE-994 AND SER-1386.
    32. Cited for: VARIANT MNKD ILE-1048.

    Entry informationi

    Entry nameiATP7A_HUMAN
    AccessioniPrimary (citable) accession number: Q04656
    Secondary accession number(s): B1AT72
    , O00227, O00745, Q9BYY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 176 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3