Reviewed, UniProtKB/Swiss-Prot Q04656 (ATP7A_HUMAN)

Names and origin

Protein names

Recommended name:
    Copper-transporting ATPase 1
    EC=3.6.3.4
Alternative name(s):
    Copper pump 1
    Menkes disease-associated protein

Gene names

Name:	ATP7A
Synonyms:	MC1, MNK

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.
Catalytic activity	ATP + H2O + Cu2+(In) = ADP + phosphate + Cu2+(Out).
Subunit structure	Monomer.
Subcellular location	Golgi apparatus › trans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Cycles constitutively between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels. Ref.12 Ref.14 Ref.15 Isoform 3: Cytoplasm › cytosol Probable. Isoform 5: Endoplasmic reticulum. Ref.12 Ref.14 Ref.15
Tissue specificity	Found in most tissues except liver. Isoform 3 is widely expressed including in liver cell lines. Isoform 1 is expressed in fibroblasts, choriocarcinoma, colon carcinoma and neuroblastoma cell lines. Isoform 2 is expressed in fibroblasts, colon carcinoma and neuroblastoma cell lines.
Domain	The C-terminal di-leucine, 1487-Leu-Leu-1488, is an endocytic targeting signal which functions in retrieving recycling from the plasma membrane to the TGN. Mutation of the di-leucine signal results in the accumulation of the protein in the plasma membrane.
Involvement in disease	Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:309400]; also known as kinky hair disease. MNKD is 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. Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:304150]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included 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. Ref.20
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IB subfamily. Contains 6 HMA domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Transmembrane
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro T-helper cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB blood vessel remodeling Inferred from sequence or structural similarity. Source: UniProtKB cartilage development Inferred from sequence or structural similarity. Source: UniProtKB cellular copper ion homeostasis Inferred from mutant phenotype. Source: UniProtKB cerebellar Purkinje cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB collagen fibril organization Inferred from sequence or structural similarity. Source: UniProtKB copper ion export Inferred from sequence or structural similarity. Source: UniProtKB copper ion import Inferred from sequence or structural similarity. Source: UniProtKB detoxification of copper ion Inferred from sequence or structural similarity. Source: UniProtKB dopamine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB elastic fiber assembly Inferred from sequence or structural similarity. Source: UniProtKB elastin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB epinephrine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB hair follicle morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB lung alveolus development Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of metalloenzyme activity Inferred from sequence or structural similarity. Source: UniProtKB neuron projection morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB neuroprotection Inferred from sequence or structural similarity. Source: UniProtKB norepinephrine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-lysine modification Inferred from sequence or structural similarity. Source: UniProtKB pigmentation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of metalloenzyme activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of oxidoreductase activity Inferred from direct assay. Source: UniProtKB pyramidal neuron development Inferred from sequence or structural similarity. Source: UniProtKB regulation of oxidative phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB removal of superoxide radicals Inferred from sequence or structural similarity. Source: UniProtKB serotonin metabolic process Inferred from sequence or structural similarity. Source: UniProtKB skin development Inferred from sequence or structural similarity. Source: UniProtKB tryptophan metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	basolateral plasma membrane Inferred from direct assay. Source: UniProtKB cell soma Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell late endosome Inferred from direct assay. Source: UniProtKB neuron projection Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB trans-Golgi network Inferred from direct assay. Source: UniProtKB trans-Golgi network transport vesicle Inferred from mutant phenotype. Source: HGNC
Molecular function	ATP binding Traceable author statement. Source: HGNC copper-dependent protein binding Inferred from physical interaction. Source: UniProtKB copper-exporting ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase copper chaperone activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 4 (identifier: Q04656-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q04656-2)

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

Isoform 2 (identifier: Q04656-3)

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

Isoform 3 (identifier: Q04656-4)

Also known as: 2-16;

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

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

Isoform 5 (identifier: Q04656-5)

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

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

Isoform 6 (identifier: Q04656-6)

Also known as: NML45;

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

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1500

1500

Copper-transporting ATPase 1

PRO_0000046311

Regions

Topological domain

1 – 653

653

Cytoplasmic Potential

Transmembrane

654 – 675

22

Potential

Topological domain

676 – 714

39

Extracellular Potential

Transmembrane

715 – 734

20

Potential

Topological domain

735 – 741

7

Cytoplasmic Potential

Transmembrane

742 – 762

21

Potential

Topological domain

763 – 781

19

Extracellular Potential

Transmembrane

782 – 802

21

Potential

Topological domain

803 – 936

134

Cytoplasmic Potential

Transmembrane

937 – 959

23

Potential

Topological domain

960 – 989

30

Extracellular Potential

Transmembrane

990 – 1011

22

Potential

Topological domain

1012 – 1356

345

Cytoplasmic Potential

Transmembrane

1357 – 1374

18

Potential

Topological domain

1375 – 1385

11

Extracellular Potential

Transmembrane

1386 – 1405

20

Potential

Topological domain

1406 – 1500

95

Cytoplasmic Potential

Domain

9 – 75

67

HMA 1

Domain

172 – 238

67

HMA 2

Domain

278 – 344

67

HMA 3

Domain

378 – 444

67

HMA 4

Domain

489 – 555

67

HMA 5

Domain

565 – 631

67

HMA 6

Motif

1487 – 1488

2

Endocytosis signal

Compositional bias

355 – 362

8

Poly-Ser

Sites

Active site

1044

1

4-aspartylphosphate intermediate By similarity

Metal binding

1301

1

Magnesium By similarity

Metal binding

1305

1

Magnesium By similarity

Amino acid modifications

Modified residue

353

1

Phosphoserine By similarity

Modified residue

357

1

Phosphoserine By similarity

Glycosylation

686

1

N-linked (GlcNAc...) Potential

Glycosylation

975

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1

1

M → MRKLSIRKRDNNLLK in isoform 1.

VSP_000419

Alternative sequence

1

1

M → MRKLSIRKRDNNLLKPSSAS SLGIAVSLGRPVLSRSSSGT VNLLEEVGLHIRDTAFSSTK LLEAISTVSAQVEELAVHNE CY in isoform 2.

VSP_000420

Alternative sequence

1

1

M → MRKLSIRKRDNNLLKECNEE IK in isoform 6.

VSP_000421

Alternative sequence

42 – 1038

997

Missing in isoform 3.

VSP_000424

Alternative sequence

53 – 81

29

DPKLQ…NPDPL → AHWFGFAALDGICSNGCFIC FCSTFFSSL in isoform 6.

VSP_000422

Alternative sequence

82 – 1499

1418

Missing in isoform 6.

VSP_000423

Alternative sequence

725 – 802

78

Missing in isoform 5.

VSP_000425

Natural variant

629

1

A → P in MNKD. Ref.19

VAR_000699

Natural variant

637

1

S → L in OHS. Ref.20

VAR_009999

Natural variant

669

1

I → T: dbSNP rs2234935. Ref.1 Ref.3

VAR_016119

Natural variant

703

1

R → H: dbSNP rs2234936.

VAR_016120

Natural variant

706

1

L → R in MNKD. Ref.25

VAR_023261

Natural variant

727

1

G → R in MNKD. Ref.19

VAR_000700

Natural variant

767

1

V → L: dbSNP rs2227291. Ref.18

VAR_010000

Natural variant

844

1

R → H in MNKD. Ref.26

VAR_023262

Natural variant

853

1

G → R in MNKD. Ref.26

VAR_023263

Natural variant

860

1

G → V in MNKD. Ref.26

VAR_023264

Natural variant

873

1

L → R in MNKD. Ref.22

VAR_010001

Natural variant

876

1

G → E in MNKD. Ref.26

VAR_010002

Natural variant

876

1

G → R in MNKD. Ref.26

VAR_023265

Natural variant

924

1

Q → R in MNKD. Ref.26

VAR_023266

Natural variant

1000

1

C → R in MNKD. Ref.26

VAR_010003

Natural variant

1006

1

L → P in MNKD. Ref.19

VAR_000701

Natural variant

1007

1

A → V in MNKD. Ref.26

VAR_023267

Natural variant

1015

1

G → D in MNKD. Ref.26

VAR_023268

Natural variant

1019

1

G → D in MNKD. Ref.19

VAR_000702

Natural variant

1044

1

D → G in MNKD. Ref.26

VAR_023269

Natural variant

1100

1

L → P in MNKD. Ref.26

VAR_023270

Natural variant

1118

1

G → D in MNKD. Ref.25

VAR_023271

Natural variant

1255

1

G → R in MNKD. Ref.25

VAR_023272

Natural variant

1282

1

K → E in MNKD. Ref.26

VAR_023273

Natural variant

1300

1

G → E in MNKD. Ref.26

VAR_010004

Natural variant

1302

1

G → R in MNKD. Ref.18

VAR_010005

Natural variant

1302

1

G → V in MNKD. Ref.26

VAR_010006

Natural variant

1304

1

N → K in MNKD. Ref.26

VAR_023274

Natural variant

1305

1

D → A in MNKD. Ref.26

VAR_010007

Natural variant

1315

1

G → R in MNKD. Ref.26

VAR_023275

Natural variant

1325

1

A → V in MNKD. Ref.26

VAR_023276

Natural variant

1344

1

S → R in MNKD. Ref.24

VAR_023277

Natural variant

1345

1

I → F in MNKD. Ref.24

VAR_023278

Natural variant

1362

1

A → V in MNKD. Ref.21

VAR_010008

Natural variant

1369

1

G → R in MNKD. Ref.26

VAR_023279

Natural variant

1397

1

S → F in MNKD. Ref.26

VAR_023280

Natural variant

1464

1

I → V: dbSNP rs2234938.

VAR_016121

Experimental info

Mutagenesis

1487 – 1488

2

LL → AA: Loss of relocalization to the trans-Golgi. Ref.15

Sequence conflict

10

1

V → A Ref.4

Sequence conflict

36

1

V → E in AAA16974. Ref.10

Sequence conflict

336

1

E → V in AAA35580. Ref.1

Sequence conflict

336

1

E → V in AAA96010. Ref.8

Sequence conflict

446

1

D → G in CAB08162. Ref.6

Sequence conflict

624

1

S → G in CAB08162. Ref.6

Sequence conflict

725

1

F → V in CAB08162. Ref.6

Sequence conflict

833

1

S → R in CAB08162. Ref.6

Sequence conflict

1099

1

E → K Ref.4

Sequence conflict

1171

1

N → S in CAB08162. Ref.6

Sequence conflict

1178

1

Y → C Ref.4

Sequence conflict

1178

1

Y → H in AAA35580. Ref.1

Sequence conflict

1178

1

Y → H in CAB94714. Ref.3

Sequence conflict

1178

1

Y → H in AAA96010. Ref.8

Sequence conflict

1220

1

D → G in CAB08162. Ref.6

Sequence conflict

1295

1

R → W Ref.4

Sequence conflict

1313

1

N → D Ref.4

Sequence conflict

1336

1

N → D in CAB08162. Ref.6

Sequence conflict

1350

1

E → K in AAA35580. Ref.1

Sequence conflict

1350

1

E → K in CAB94714. Ref.3

Sequence conflict

1350

1

E → K in AAA96010. Ref.8

Sequence conflict

1376

1

V → M in CAB08162. Ref.6

Sequence conflict

1396

1

S → P Ref.4

Sequence conflict

1409

1

L → R in CAB08160. Ref.6

Sequence conflict

1455

1

R → W Ref.4

Secondary structure

1

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1500

Helix Strand Turn

Details...

Turn

4 – 6

3

Beta strand

8 – 14

7

Turn

20 – 22

3

Helix

23 – 32

10

Beta strand

33 – 35

3

Beta strand

39 – 41

3

Helix

43 – 45

3

Beta strand

46 – 52

7

Turn

54 – 56

3

Helix

59 – 69

11

Beta strand

73 – 75

3

Beta strand

165 – 169

5

Beta strand

171 – 177

7

Turn

180 – 182

3

Helix

187 – 194

8

Beta strand

199 – 204

6

Turn

207 – 209

3

Beta strand

210 – 215

6

Helix

222 – 231

10

Turn

242 – 244

3

Beta strand

277 – 285

9

Helix

288 – 299

12

Beta strand

305 – 311

7

Turn

312 – 315

4

Beta strand

316 – 321

6

Helix

329 – 336

8

Turn

340 – 342

3

Beta strand

344 – 346

3

Beta strand

377 – 384

8

Helix

388 – 400

13

Beta strand

408 – 411

4

Turn

412 – 415

4

Beta strand

416 – 421

6

Turn

423 – 425

3

Helix

428 – 438

11

Beta strand

441 – 446

6

Beta strand

488 – 495

8

Helix

497 – 499

3

Helix

502 – 510

9

Beta strand

513 – 518

6

Turn

523 – 526

4

Beta strand

527 – 532

6

Turn

534 – 536

3

Helix

539 – 549

11

Beta strand

553 – 557

5

Beta strand

565 – 571

7

Helix

578 – 587

10

Beta strand

592 – 598

7

Helix

599 – 601

3

Beta strand

603 – 608

6

Turn

610 – 612

3

Helix

615 – 626

12

Beta strand

627 – 631

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: CF8FF9EA061D463B	FASTA	1,500	163,374
	10 20 30 40 50 60 MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK 70 80 90 100 110 120 TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP 130 140 150 160 170 180 QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM 190 200 210 220 230 240 TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK 250 260 270 280 290 300 QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS 310 320 330 340 350 360 ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS 370 380 390 400 410 420 SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE 430 440 450 460 470 480 YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD 490 500 510 520 530 540 KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP 550 560 570 580 590 600 MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA 610 620 630 640 650 660 TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF 670 680 690 700 710 720 CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC 730 740 750 760 770 780 VPVQFFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITF 790 800 810 820 830 840 FDTPPMLFVF IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE 850 860 870 880 890 900 LVQRGDIIKV VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL 910 920 930 940 950 960 LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI ATLLVWIVIG 970 980 990 1000 1010 1020 FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA 1030 1040 1050 1060 1070 1080 QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLTESNRISH HKILAIVGTA 1090 1100 1110 1120 1130 1140 ESNSEHPLGT AITKYCKQEL DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN 1150 1160 1170 1180 1190 1200 NIKNASLVQI DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN 1210 1220 1230 1240 1250 1260 DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV VLMTGDNSKT 1270 1280 1290 1300 1310 1320 ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT 1330 1340 1350 1360 1370 1380 GTDVAIEAAD VVLIRNDLLD VVASIDLSRE TVKRIRINFV FALIYNLVGI PIAAGVFMPI 1390 1400 1410 1420 1430 1440 GLVLQPWMGS AAMAASSVSV VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI 1450 1460 1470 1480 1490 1500 DDTSRNSPKL GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL
	Isoform 1. Checksum: B4FFD7472742EB62	FASTA	1,514	165,110
	10 20 30 40 50 60 MRKLSIRKRD NNLLKDPSMG VNSVTISVEG MTCNSCVWTI EQQIGKVNGV HHIKVSLEEK 70 80 90 100 110 120 NATIIYDPKL QTPKTLQEAI DDMGFDAVIH NPDPLPVLTD TLFLTVTASL TLPWDHIQST 130 140 150 160 170 180 LLKTKGVTDI KIYPQKRTVA VTIIPSIVNA NQIKELVPEL SLDTGTLEKK SGACEDHSMA 190 200 210 220 230 240 QAGEVVLKMK VEGMTCHSCT STIEGKIGKL QGVQRIKVSL DNQEATIVYQ PHLISVEEMK 250 260 270 280 290 300 KQIEAMGFPA FVKKQPKYLK LGAIDVERLK NTPVKSSEGS QQRSPSYTND STATFIIDGM 310 320 330 340 350 360 HCKSCVSNIE STLSALQYVS SIVVSLENRS AIVKYNASSV TPESLRKAIE AVSPGLYRVS 370 380 390 400 410 420 ITSEVESTSN SPSSSSLQKI PLNVVSQPLT QETVINIDGM TCNSCVQSIE GVISKKPGVK 430 440 450 460 470 480 SIRVSLANSN GTVEYDPLLT SPETLRGAIE DMGFDATLSD TNEPLVVIAQ PSSEMPLLTS 490 500 510 520 530 540 TNEFYTKGMT PVQDKEEGKN SSKCYIQVTG MTCASCVANI ERNLRREEGI YSILVALMAG 550 560 570 580 590 600 KAEVRYNPAV IQPPMIAEFI RELGFGATVI ENADEGDGVL ELVVRGMTCA SCVHKIESSL 610 620 630 640 650 660 TKHRGILYCS VALATNKAHI KYDPEIIGPR DIIHTIESLG FEASLVKKDR SASHLDHKRE 670 680 690 700 710 720 IRQWRRSFLV SLFFCIPVMG LMIYMMVMDH HFATLHHNQN MSKEEMINLH SSMFLERQIL 730 740 750 760 770 780 PGLSVMNLLS FLLCVPVQFF GGWYFYIQAY KALKHKTANM DVLIVLATTI AFAYSLIILL 790 800 810 820 830 840 VAMYERAKVN PITFFDTPPM LFVFIALGRW LEHIAKGKTS EALAKLISLQ ATEATIVTLD 850 860 870 880 890 900 SDNILLSEEQ VDVELVQRGD IIKVVPGGKF PVDGRVIEGH SMVDESLITG EAMPVAKKPG 910 920 930 940 950 960 STVIAGSINQ NGSLLICATH VGADTTLSQI VKLVEEAQTS KAPIQQFADK LSGYFVPFIV 970 980 990 1000 1010 1020 FVSIATLLVW IVIGFLNFEI VETYFPGYNR SISRTETIIR FAFQASITVL CIACPCSLGL 1030 1040 1050 1060 1070 1080 ATPTAVMVGT GVGAQNGILI KGGEPLEMAH KVKVVVFDKT GTITHGTPVV NQVKVLTESN 1090 1100 1110 1120 1130 1140 RISHHKILAI VGTAESNSEH PLGTAITKYC KQELDTETLG TCIDFQVVPG CGISCKVTNI 1150 1160 1170 1180 1190 1200 EGLLHKNNWN IEDNNIKNAS LVQIDASNEQ SSTSSSMIID AQISNALNAQ QYKVLIGNRE 1210 1220 1230 1240 1250 1260 WMIRNGLVIN NDVNDFMTEH ERKGRTAVLV AVDDELCGLI AIADTVKPEA ELAIHILKSM 1270 1280 1290 1300 1310 1320 GLEVVLMTGD NSKTARSIAS QVGITKVFAE VLPSHKVAKV KQLQEEGKRV AMVGDGINDS 1330 1340 1350 1360 1370 1380 PALAMANVGI AIGTGTDVAI EAADVVLIRN DLLDVVASID LSRETVKRIR INFVFALIYN 1390 1400 1410 1420 1430 1440 LVGIPIAAGV FMPIGLVLQP WMGSAAMAAS SVSVVLSSLF LKLYRKPTYE SYELPARSQI 1450 1460 1470 1480 1490 1500 GQKSPSEISV HVGIDDTSRN SPKLGLLDRI VNYSRASINS LLSDKRSLNS VVTSEPDKHS 1510 LLVGDFREDD DTAL
	Isoform 2. Checksum: FDE210402FD79C4B	FASTA	1,581	172,078
	10 20 30 40 50 60 MRKLSIRKRD NNLLKPSSAS SLGIAVSLGR PVLSRSSSGT VNLLEEVGLH IRDTAFSSTK 70 80 90 100 110 120 LLEAISTVSA QVEELAVHNE CYDPSMGVNS VTISVEGMTC NSCVWTIEQQ IGKVNGVHHI 130 140 150 160 170 180 KVSLEEKNAT IIYDPKLQTP KTLQEAIDDM GFDAVIHNPD PLPVLTDTLF LTVTASLTLP 190 200 210 220 230 240 WDHIQSTLLK TKGVTDIKIY PQKRTVAVTI IPSIVNANQI KELVPELSLD TGTLEKKSGA 250 260 270 280 290 300 CEDHSMAQAG EVVLKMKVEG MTCHSCTSTI EGKIGKLQGV QRIKVSLDNQ EATIVYQPHL 310 320 330 340 350 360 ISVEEMKKQI EAMGFPAFVK KQPKYLKLGA IDVERLKNTP VKSSEGSQQR SPSYTNDSTA 370 380 390 400 410 420 TFIIDGMHCK SCVSNIESTL SALQYVSSIV VSLENRSAIV KYNASSVTPE SLRKAIEAVS 430 440 450 460 470 480 PGLYRVSITS EVESTSNSPS SSSLQKIPLN VVSQPLTQET VINIDGMTCN SCVQSIEGVI 490 500 510 520 530 540 SKKPGVKSIR VSLANSNGTV EYDPLLTSPE TLRGAIEDMG FDATLSDTNE PLVVIAQPSS 550 560 570 580 590 600 EMPLLTSTNE FYTKGMTPVQ DKEEGKNSSK CYIQVTGMTC ASCVANIERN LRREEGIYSI 610 620 630 640 650 660 LVALMAGKAE VRYNPAVIQP PMIAEFIREL GFGATVIENA DEGDGVLELV VRGMTCASCV 670 680 690 700 710 720 HKIESSLTKH RGILYCSVAL ATNKAHIKYD PEIIGPRDII HTIESLGFEA SLVKKDRSAS 730 740 750 760 770 780 HLDHKREIRQ WRRSFLVSLF FCIPVMGLMI YMMVMDHHFA TLHHNQNMSK EEMINLHSSM 790 800 810 820 830 840 FLERQILPGL SVMNLLSFLL CVPVQFFGGW YFYIQAYKAL KHKTANMDVL IVLATTIAFA 850 860 870 880 890 900 YSLIILLVAM YERAKVNPIT FFDTPPMLFV FIALGRWLEH IAKGKTSEAL AKLISLQATE 910 920 930 940 950 960 ATIVTLDSDN ILLSEEQVDV ELVQRGDIIK VVPGGKFPVD GRVIEGHSMV DESLITGEAM 970 980 990 1000 1010 1020 PVAKKPGSTV IAGSINQNGS LLICATHVGA DTTLSQIVKL VEEAQTSKAP IQQFADKLSG 1030 1040 1050 1060 1070 1080 YFVPFIVFVS IATLLVWIVI GFLNFEIVET YFPGYNRSIS RTETIIRFAF QASITVLCIA 1090 1100 1110 1120 1130 1140 CPCSLGLATP TAVMVGTGVG AQNGILIKGG EPLEMAHKVK VVVFDKTGTI THGTPVVNQV 1150 1160 1170 1180 1190 1200 KVLTESNRIS HHKILAIVGT AESNSEHPLG TAITKYCKQE LDTETLGTCI DFQVVPGCGI 1210 1220 1230 1240 1250 1260 SCKVTNIEGL LHKNNWNIED NNIKNASLVQ IDASNEQSST SSSMIIDAQI SNALNAQQYK 1270 1280 1290 1300 1310 1320 VLIGNREWMI RNGLVINNDV NDFMTEHERK GRTAVLVAVD DELCGLIAIA DTVKPEAELA 1330 1340 1350 1360 1370 1380 IHILKSMGLE VVLMTGDNSK TARSIASQVG ITKVFAEVLP SHKVAKVKQL QEEGKRVAMV 1390 1400 1410 1420 1430 1440 GDGINDSPAL AMANVGIAIG TGTDVAIEAA DVVLIRNDLL DVVASIDLSR ETVKRIRINF 1450 1460 1470 1480 1490 1500 VFALIYNLVG IPIAAGVFMP IGLVLQPWMG SAAMAASSVS VVLSSLFLKL YRKPTYESYE 1510 1520 1530 1540 1550 1560 LPARSQIGQK SPSEISVHVG IDDTSRNSPK LGLLDRIVNY SRASINSLLS DKRSLNSVVT 1570 1580 SEPDKHSLLV GDFREDDDTA L
	Isoform 3 (2-16). Checksum: B81B1F9FFB00B832	FASTA	503	54,318
	10 20 30 40 50 60 MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VKVVVFDKTG TITHGTPVVN 70 80 90 100 110 120 QVKVLTESNR ISHHKILAIV GTAESNSEHP LGTAITKYCK QELDTETLGT CIDFQVVPGC 130 140 150 160 170 180 GISCKVTNIE GLLHKNNWNI EDNNIKNASL VQIDASNEQS STSSSMIIDA QISNALNAQQ 190 200 210 220 230 240 YKVLIGNREW MIRNGLVINN DVNDFMTEHE RKGRTAVLVA VDDELCGLIA IADTVKPEAE 250 260 270 280 290 300 LAIHILKSMG LEVVLMTGDN SKTARSIASQ VGITKVFAEV LPSHKVAKVK QLQEEGKRVA 310 320 330 340 350 360 MVGDGINDSP ALAMANVGIA IGTGTDVAIE AADVVLIRND LLDVVASIDL SRETVKRIRI 370 380 390 400 410 420 NFVFALIYNL VGIPIAAGVF MPIGLVLQPW MGSAAMAASS VSVVLSSLFL KLYRKPTYES 430 440 450 460 470 480 YELPARSQIG QKSPSEISVH VGIDDTSRNS PKLGLLDRIV NYSRASINSL LSDKRSLNSV 490 500 VTSEPDKHSL LVGDFREDDD TAL
	Isoform 5. Checksum: EEB740B5F6841813	FASTA	1,422	154,357
	10 20 30 40 50 60 MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK 70 80 90 100 110 120 TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP 130 140 150 160 170 180 QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM 190 200 210 220 230 240 TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK 250 260 270 280 290 300 QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS 310 320 330 340 350 360 ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS 370 380 390 400 410 420 SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE 430 440 450 460 470 480 YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD 490 500 510 520 530 540 KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP 550 560 570 580 590 600 MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA 610 620 630 640 650 660 TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF 670 680 690 700 710 720 CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC 730 740 750 760 770 780 VPVQGKTSEA LAKLISLQAT EATIVTLDSD NILLSEEQVD VELVQRGDII KVVPGGKFPV 790 800 810 820 830 840 DGRVIEGHSM VDESLITGEA MPVAKKPGST VIAGSINQNG SLLICATHVG ADTTLSQIVK 850 860 870 880 890 900 LVEEAQTSKA PIQQFADKLS GYFVPFIVFV SIATLLVWIV IGFLNFEIVE TYFPGYNRSI 910 920 930 940 950 960 SRTETIIRFA FQASITVLCI ACPCSLGLAT PTAVMVGTGV GAQNGILIKG GEPLEMAHKV 970 980 990 1000 1010 1020 KVVVFDKTGT ITHGTPVVNQ VKVLTESNRI SHHKILAIVG TAESNSEHPL GTAITKYCKQ 1030 1040 1050 1060 1070 1080 ELDTETLGTC IDFQVVPGCG ISCKVTNIEG LLHKNNWNIE DNNIKNASLV QIDASNEQSS 1090 1100 1110 1120 1130 1140 TSSSMIIDAQ ISNALNAQQY KVLIGNREWM IRNGLVINND VNDFMTEHER KGRTAVLVAV 1150 1160 1170 1180 1190 1200 DDELCGLIAI ADTVKPEAEL AIHILKSMGL EVVLMTGDNS KTARSIASQV GITKVFAEVL 1210 1220 1230 1240 1250 1260 PSHKVAKVKQ LQEEGKRVAM VGDGINDSPA LAMANVGIAI GTGTDVAIEA ADVVLIRNDL 1270 1280 1290 1300 1310 1320 LDVVASIDLS RETVKRIRIN FVFALIYNLV GIPIAAGVFM PIGLVLQPWM GSAAMAASSV 1330 1340 1350 1360 1370 1380 SVVLSSLFLK LYRKPTYESY ELPARSQIGQ KSPSEISVHV GIDDTSRNSP KLGLLDRIVN 1390 1400 1410 1420 YSRASINSLL SDKRSLNSVV TSEPDKHSLL VGDFREDDDT AL
	Isoform 6 (NML45). Checksum: 1F3873EFB0EA6CC2	FASTA	103	11,522
	10 20 30 40 50 60 MRKLSIRKRD NNLLKECNEE IKDPSMGVNS VTISVEGMTC NSCVWTIEQQ IGKVNGVHHI 70 80 90 100 KVSLEEKNAT IIYAHWFGFA ALDGICSNGC FICFCSTFFS SLL

References

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[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: 7607665] [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: 9693104] [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: 10079814] [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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"Molecular structure of the Menkes disease gene (ATP7A)." Dierick H.A., Ambrosini L., Spencer J., Glover T.W., Mercer J.F.B. Genomics 28:462-469(1995) [PubMed: 7490081] [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: 8490646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-626 (ISOFORM 4). Tissue: Kidney.
[10]	"Isolation of a partial candidate gene for Menkes disease by positional cloning." Mercer J.F.B., Livingston J., Hall B., Paynter J.A., Begy C., Chandrasekharappa S., Lockhart P., Grimes A., Bhave M., Siemieniak D., Glover T.W. Nat. Genet. 3:20-25(1993) [PubMed: 8490647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-529 (ISOFORM 4). Tissue: Endothelial cell.
[11]	"Molecular phylogenetics and the origins of placental mammals." Murphy W.J., Eizirik E., Johnson W.E., Zhang Y.-P., Ryder O.A., O'Brien S.J. Nature 409:614-618(2001) [PubMed: 11214319] [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: 9467005] [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: 10970802] [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: 9147644] [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: 10484781] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEUCINE RESIDUES.
[16]	"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: 9437429] [Abstract] Cited for: STRUCTURE BY NMR OF 375-446.
[17]	"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: 10079817] [Abstract] Cited for: REVIEW, VARIANTS MNKD.
[18]	"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: 7977350] [Abstract] Cited for: VARIANT LEU-767, VARIANT MNKD ARG-1302.
[19]	"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: 8981948] [Abstract] Cited for: VARIANTS MNKD PRO-629; ARG-727; PRO-1006 AND ASP-1019.
[20]	"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: 9246006] [Abstract] Cited for: VARIANT OHS LEU-637.
[21]	"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: 10401004] [Abstract] Cited for: VARIANT MNKD VAL-1362.
[22]	"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: 10319589] [Abstract] Cited for: VARIANT MNKD ARG-873.
[23]	"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: 11431706] [Abstract] Cited for: INVOLVEMENT IN OCCIPITAL HORN SYNDROME.
[24]	"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: 11241493] [Abstract] Cited for: VARIANTS MNKD ARG-1344 AND PHE-1345.
[25]	"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: 11350187] [Abstract] Cited for: VARIANTS MNKD ARG-706; ASP-1118 AND ARG-1255.
[26]	"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: 15981243] [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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Protein Spotlight

Heavy metal - Issue 79 of February 2007

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00028610.
IPI00215614.
IPI00215615.
IPI00215616.
IPI00215617.
IPI00215619.

PIR

S36149.

RefSeq

NP_000043.3.

UniGene

Hs.496414

3D structure databases

PDBPDBe

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	[»]
3CJK	X-ray	1.80	B	7-77	[»]

DisProt

DP00282.

ModBase

Search...

Protein-protein interaction databases

STRING

Q04656.

Protein family/group databases

TCDB

3.A.3.5.6. P-type ATPase (P-ATPase) superfamily.

PTM databases

PhosphoSite

Q04656.

Proteomic databases

PRIDE

Q04656.

Genome annotation databases

Ensembl

ENST00000341514; ENSP00000345728; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000343533; ENSP00000343026; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000343912; ENSP00000342775; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000350425; ENSP00000343678; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000355691; ENSP00000355170; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000395563; ENSP00000378930; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000400858; ENSP00000383655; ENSG00000165240; Homo sapiens. [Genome view]
ENST00000400860; ENSP00000383657; ENSG00000165240; Homo sapiens. [Genome view]

GeneID

538.

KEGG

hsa:538.

UCSC

uc004ecx.2. human.

Organism-specific databases

CTD

538.

GeneCards

GC0XP077052.
GC0XP077053.

H-InvDB

HIX0016888.
HIX0031404.
HIX0059642.

HGNC

HGNC:869. ATP7A.

HPA

HPA012887.

MIM

300011. gene.
304150. phenotype.
309400. phenotype.

Orphanet

209. Cutis laxa.
90346. Cutis laxa, X-linked.
565. Menkes syndrome.
198. Occipital horn syndrome.

PharmGKB

PA72.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q04656.

Gene expression databases

ArrayExpress

Q04656.

Bgee

Q04656.

CleanEx

HS_ATP7A.

Genevestigator

Q04656.

GermOnline

ENSG00000165240. Homo sapiens.

Family and domain databases

InterPro

IPR001877. ATPase1_Cu-transp.
IPR008250. ATPase_P-typ_ATPase-assoc-reg.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR006122. Cu_ion_bd.
IPR005834. Dehalogen-like_hydro.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe_transpt.
[Graphical view]

PANTHER

PTHR11939. ATPase_P. 1 hit.

Pfam

PF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.
PR00942. CUATPASEI.

TIGRFAMs

TIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. Cu_ion_bd. 2 hits.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 6 hits.
PS50846. HMA_2. 6 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

ATP7A_HUMAN

Accession

Primary (citable) accession number: Q04656
Secondary accession number(s): B1AT72 , O00227, O00745, Q9BYY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 10, 2009
Last modified:	November 3, 2009
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.