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Q04656

- ATP7A_HUMAN

UniProt

Q04656 - ATP7A_HUMAN

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Protein
Copper-transporting ATPase 1
Gene
ATP7A, MC1, MNK
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 intermediate By similarity
Metal bindingi1301 – 13011Magnesium By similarity
Metal bindingi1305 – 13051Magnesium By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 653653Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei654 – 67522Helical; Reviewed prediction
Add
BLAST
Topological domaini676 – 71439Extracellular Reviewed prediction
Add
BLAST
Transmembranei715 – 73420Helical; Reviewed prediction
Add
BLAST
Topological domaini735 – 7417Cytoplasmic Reviewed prediction
Transmembranei742 – 76221Helical; Reviewed prediction
Add
BLAST
Topological domaini763 – 78119Extracellular Reviewed prediction
Add
BLAST
Transmembranei782 – 80221Helical; Reviewed prediction
Add
BLAST
Topological domaini803 – 936134Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei937 – 95923Helical; Reviewed prediction
Add
BLAST
Topological domaini960 – 98930Extracellular Reviewed prediction
Add
BLAST
Transmembranei990 – 101122Helical; Reviewed prediction
Add
BLAST
Topological domaini1012 – 1356345Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1357 – 137418Helical; Reviewed prediction
Add
BLAST
Topological domaini1375 – 138511Extracellular Reviewed prediction
Add
BLAST
Transmembranei1386 – 140520Helical; Reviewed prediction
Add
BLAST
Topological domaini1406 – 150095Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. brush border membrane Source: Ensembl
  4. cytosol Source: UniProtKB-SubCell
  5. endoplasmic reticulum Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. late endosome Source: UniProtKB
  8. neuron projection Source: UniProtKB
  9. neuronal cell body 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 1
PRO_0000046311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei339 – 3391Phosphoserine1 Publication
Modified residuei357 – 3571Phosphoserine By similarity
Glycosylationi686 – 6861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi975 – 9751N-linked (GlcNAc...) Reviewed prediction
Modified residuei1212 – 12121Phosphothreonine By similarity
Modified residuei1466 – 14661Phosphoserine By 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

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.

Miscellaneous databases

EvolutionaryTraceiQ04656.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1486 – 150015PDZD11-binding
Add
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.

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

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.
VSP_000419
Alternative sequencei1 – 11M → MRKLSIRKRDNNLLKPSSAS SLGIAVSLGRPVLSRSSSGT VNLLEEVGLHIRDTAFSSTK LLEAISTVSAQVEELAVHNE CY in isoform 2.
VSP_000420
Alternative sequencei1 – 11M → MRKLSIRKRDNNLLKECNEE IK in isoform 6.
VSP_000421
Alternative sequencei42 – 1038997Missing in isoform 3.
VSP_000424Add
BLAST
Alternative sequencei53 – 8129DPKLQ…NPDPL → AHWFGFAALDGICSNGCFIC FCSTFFSSL in isoform 6.
VSP_000422Add
BLAST
Alternative sequencei82 – 14991418Missing in isoform 6.
VSP_000423Add
BLAST
Alternative sequencei725 – 80278Missing in isoform 5.
VSP_000425Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101V → A no nucleotide entry 1 Publication
Sequence conflicti36 – 361V → E in AAA16974. 1 Publication
Sequence conflicti336 – 3361E → V in AAA35580. 1 Publication
Sequence conflicti336 – 3361E → V in AAA96010. 1 Publication
Sequence conflicti446 – 4461D → G in CAB08162. 1 Publication
Sequence conflicti624 – 6241S → G in CAB08162. 1 Publication
Sequence conflicti725 – 7251F → V in CAB08162. 1 Publication
Sequence conflicti833 – 8331S → R in CAB08162. 1 Publication
Sequence conflicti1099 – 10991E → K no nucleotide entry 1 Publication
Sequence conflicti1171 – 11711N → S in CAB08162. 1 Publication
Sequence conflicti1178 – 11781Y → C no nucleotide entry 1 Publication
Sequence conflicti1178 – 11781Y → H in AAA35580. 1 Publication
Sequence conflicti1178 – 11781Y → H in CAB94714. 1 Publication
Sequence conflicti1178 – 11781Y → H in AAA96010. 1 Publication
Sequence conflicti1220 – 12201D → G in CAB08162. 1 Publication
Sequence conflicti1295 – 12951R → W no nucleotide entry 1 Publication
Sequence conflicti1313 – 13131N → D no nucleotide entry 1 Publication
Sequence conflicti1336 – 13361N → D in CAB08162. 1 Publication
Sequence conflicti1350 – 13501E → K in AAA35580. 1 Publication
Sequence conflicti1350 – 13501E → K in CAB94714. 1 Publication
Sequence conflicti1350 – 13501E → K in AAA96010. 1 Publication
Sequence conflicti1376 – 13761V → M in CAB08162. 1 Publication
Sequence conflicti1396 – 13961S → P no nucleotide entry 1 Publication
Sequence conflicti1409 – 14091L → R in CAB08160. 1 Publication
Sequence conflicti1455 – 14551R → W no nucleotide entry 1 Publication

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.

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

« 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: September 3, 2014
This is version 175 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

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