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Q04656

- ATP7A_HUMAN

UniProt

Q04656 - ATP7A_HUMAN

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Protein

Copper-transporting ATPase 1

Gene

ATP7A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 653653CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei654 – 67522HelicalSequence AnalysisAdd
BLAST
Topological domaini676 – 71439ExtracellularSequence AnalysisAdd
BLAST
Transmembranei715 – 73420HelicalSequence AnalysisAdd
BLAST
Topological domaini735 – 7417CytoplasmicSequence Analysis
Transmembranei742 – 76221HelicalSequence AnalysisAdd
BLAST
Topological domaini763 – 78119ExtracellularSequence AnalysisAdd
BLAST
Transmembranei782 – 80221HelicalSequence AnalysisAdd
BLAST
Topological domaini803 – 936134CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei937 – 95923HelicalSequence AnalysisAdd
BLAST
Topological domaini960 – 98930ExtracellularSequence AnalysisAdd
BLAST
Transmembranei990 – 101122HelicalSequence AnalysisAdd
BLAST
Topological domaini1012 – 1356345CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1357 – 137418HelicalSequence AnalysisAdd
BLAST
Topological domaini1375 – 138511ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1386 – 140520HelicalSequence AnalysisAdd
BLAST
Topological domaini1406 – 150095CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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.
ExpressionAtlasiQ04656. baseline and differential.
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. 9 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 – 63Combined sources
Beta strandi8 – 147Combined sources
Helixi20 – 3112Combined sources
Beta strandi33 – 353Combined sources
Beta strandi36 – 427Combined sources
Turni43 – 464Combined sources
Beta strandi47 – 526Combined sources
Turni54 – 563Combined sources
Helixi59 – 6810Combined sources
Beta strandi73 – 775Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi171 – 1777Combined sources
Turni180 – 1823Combined sources
Helixi187 – 1948Combined sources
Beta strandi199 – 2046Combined sources
Turni207 – 2093Combined sources
Beta strandi210 – 2156Combined sources
Turni217 – 2193Combined sources
Helixi222 – 23110Combined sources
Beta strandi236 – 2383Combined sources
Turni242 – 2443Combined sources
Beta strandi277 – 2859Combined sources
Helixi288 – 29912Combined sources
Beta strandi305 – 3117Combined sources
Turni312 – 3154Combined sources
Beta strandi316 – 3216Combined sources
Beta strandi324 – 3263Combined sources
Helixi329 – 3368Combined sources
Turni340 – 3423Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi377 – 3848Combined sources
Helixi388 – 40013Combined sources
Beta strandi408 – 4114Combined sources
Turni412 – 4154Combined sources
Beta strandi416 – 4216Combined sources
Turni423 – 4253Combined sources
Helixi428 – 43811Combined sources
Beta strandi441 – 4466Combined sources
Beta strandi488 – 4958Combined sources
Helixi497 – 4993Combined sources
Helixi502 – 5109Combined sources
Beta strandi513 – 5186Combined sources
Turni523 – 5264Combined sources
Beta strandi527 – 5326Combined sources
Turni534 – 5363Combined sources
Helixi539 – 54911Combined sources
Beta strandi553 – 5575Combined sources
Beta strandi566 – 5716Combined sources
Turni575 – 5773Combined sources
Helixi578 – 5869Combined sources
Beta strandi592 – 5987Combined sources
Turni599 – 6024Combined sources
Beta strandi603 – 6086Combined sources
Turni610 – 6134Combined sources
Helixi614 – 62613Combined sources
Beta strandi628 – 6336Combined sources
Helixi808 – 8147Combined sources
Beta strandi818 – 8247Combined sources
Beta strandi826 – 8283Combined sources
Beta strandi833 – 8386Combined sources
Turni839 – 8413Combined sources
Beta strandi847 – 8493Combined sources
Beta strandi860 – 8623Combined sources
Beta strandi868 – 8703Combined sources
Turni872 – 8754Combined sources
Beta strandi887 – 8893Combined sources
Beta strandi894 – 8985Combined sources
Beta strandi901 – 9044Combined sources
Turni908 – 9103Combined sources
Helixi912 – 9198Combined sources
Turni920 – 9234Combined sources
Beta strandi1055 – 10617Combined sources
Turni1065 – 10673Combined sources
Helixi1070 – 107910Combined sources
Helixi1080 – 10823Combined sources
Beta strandi1083 – 10853Combined sources
Helixi1087 – 110014Combined sources
Beta strandi1112 – 11143Combined sources
Turni1115 – 11173Combined sources
Beta strandi1118 – 11236Combined sources
Helixi1127 – 11293Combined sources
Turni1135 – 11395Combined sources
Turni1150 – 11534Combined sources
Beta strandi1161 – 11666Combined sources
Turni1167 – 11715Combined sources
Helixi1172 – 11743Combined sources
Beta strandi1178 – 11836Combined sources
Helixi1185 – 11917Combined sources
Helixi1197 – 120812Combined sources
Beta strandi1212 – 12187Combined sources
Beta strandi1221 – 12299Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 713-1413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04656.

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.
InParanoidiQ04656.
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

        10         20         30         40         50
MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI
60 70 80 90 100
IYDPKLQTPK TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW
110 120 130 140 150
DHIQSTLLKT KGVTDIKIYP QKRTVAVTII PSIVNANQIK ELVPELSLDT
160 170 180 190 200
GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM TCHSCTSTIE GKIGKLQGVQ
210 220 230 240 250
RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK QPKYLKLGAI
260 270 280 290 300
DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS
310 320 330 340 350
ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE
360 370 380 390 400
VESTSNSPSS SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS
410 420 430 440 450
KKPGVKSIRV SLANSNGTVE YDPLLTSPET LRGAIEDMGF DATLSDTNEP
460 470 480 490 500
LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD KEEGKNSSKC YIQVTGMTCA
510 520 530 540 550
SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP MIAEFIRELG
560 570 580 590 600
FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA
610 620 630 640 650
TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW
660 670 680 690 700
RRSFLVSLFF CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF
710 720 730 740 750
LERQILPGLS VMNLLSFLLC VPVQFFGGWY FYIQAYKALK HKTANMDVLI
760 770 780 790 800
VLATTIAFAY SLIILLVAMY ERAKVNPITF FDTPPMLFVF IALGRWLEHI
810 820 830 840 850
AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE LVQRGDIIKV
860 870 880 890 900
VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL
910 920 930 940 950
LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI
960 970 980 990 1000
ATLLVWIVIG FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC
1010 1020 1030 1040 1050
PCSLGLATPT AVMVGTGVGA QNGILIKGGE PLEMAHKVKV VVFDKTGTIT
1060 1070 1080 1090 1100
HGTPVVNQVK VLTESNRISH HKILAIVGTA ESNSEHPLGT AITKYCKQEL
1110 1120 1130 1140 1150
DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN NIKNASLVQI
1160 1170 1180 1190 1200
DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN
1210 1220 1230 1240 1250
DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV
1260 1270 1280 1290 1300
VLMTGDNSKT ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG
1310 1320 1330 1340 1350
DGINDSPALA MANVGIAIGT GTDVAIEAAD VVLIRNDLLD VVASIDLSRE
1360 1370 1380 1390 1400
TVKRIRINFV FALIYNLVGI PIAAGVFMPI GLVLQPWMGS AAMAASSVSV
1410 1420 1430 1440 1450
VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI DDTSRNSPKL
1460 1470 1480 1490 1500
GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL
Length:1,500
Mass (Da):163,374
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:
EMBLi
GenBanki
DDBJi
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]
CCDS75997.1. [Q04656-5]
PIRiS36149.
RefSeqiNP_000043.4. NM_000052.6.
NP_001269153.1. NM_001282224.1.
UniGeneiHs.496414.
Hs.733232.

Genome annotation databases

EnsembliENST00000341514; ENSP00000345728; ENSG00000165240.
ENST00000343533; ENSP00000343026; ENSG00000165240.
ENST00000350425; ENSP00000343678; ENSG00000165240.
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:
EMBLi
GenBanki
DDBJi
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 ]
CCDS75997.1. [Q04656-5 ]
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:
PDBei
RCSB PDBi
PDBji
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, 713-1413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107020. 9 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 .
ENST00000343533 ; ENSP00000343026 ; ENSG00000165240 .
ENST00000350425 ; ENSP00000343678 ; ENSG00000165240 .
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.
InParanoidi Q04656.
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.
ExpressionAtlasi Q04656. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 178 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