374:
351:
3627:
3612:
3762:
248:
273:
3747:
3582:
3567:
3687:
3672:
3732:
3552:
3717:
3702:
3642:
3657:
380:
279:
3597:
29:
1908:
distributed to cells in the body. Copper accumulates in some tissues, such as the small intestine and kidneys, while the brain and other tissues have unusually low levels. The decreased supply of copper can reduce the activity of numerous copper-containing enzymes that are necessary for the structure and function of bone, skin, hair, blood vessels, and the nervous system. Copper is also critical for the propagation of
1649:
1904:(OHS), the milder form of Menkes disease. Many of these mutations delete part of the gene and are predicted to produce a shortened ATP7A protein that is unable to transport Cu(I). Other mutations insert additional DNA base pairs or use the wrong base pairs, which leads to ATP7A proteins that do not function properly.
1748:
of the intermediate finishes the catalytic cycle. Within each cycle, ATP7A interconverts between at least two different conformations, E1 and E2. In the E1 state, Cu(I) is tightly bound to the binding sites on the cytoplasmic side; in the E2 state, the affinity of ATP7A for Cu(I) decreases and Cu(I)
1907:
The altered proteins that result from ATP7A mutations impair the absorption of copper from food, fail to supply copper to certain enzymes, or get stuck in the cell membrane, unable to shuttle back and forth from the Golgi. As a result of the disrupted activity of the ATP7A protein, copper is poorly
1693:
The six Cu(I)-binding sites at the N-terminal bind one Cu(I) each. This binding site is not specific for Cu(I) and can bind various transition metal ions. Cd(II), Au(III) and Hg(II) bind to the binding site more tightly than does Zn(II), whereas Mn(II) and Ni(II) have lower affinities relative to
1719:
Of the six copper(I)-binding sites, two are considered enough for the function of Cu(I) transport. The reason why there are six binding sites remains not fully understood. However, some scientists have proposed that the other four sites may serve as a Cu(I) concentration detector.
1613:
at band Xq21.1. The encoded ATP7A protein has 1,500 amino acids. At least 12 disease-causing mutations in this gene have been discovered. Mutations/additions/deletions of this gene often cause copper deficiency, which leads to progressive neurodegeneration and death in children.
55:
1711:(C) residues in each Cu(I)-binding site are coordinated to Cu(I) with a S-Cu(I)-S angle between 120 and 180° and a Cu-S distance of 2.16 Å. Experimental results from a homologous protein ATP7B suggests that reducing reagents are involved, and upon Cu(I) binding the
1785:) that are critical for the structures and functions of brain, bone, skin, hair, connective tissue, and the nervous system. If Cu(I) levels in the cell environment are elevated, however, ATP7A moves to the cell membrane and eliminates excess Cu(I) from the cell.
1757:
ATP7A is important for regulating copper Cu(I) in mammals. This protein is found in most tissues, but it is not expressed in the liver. In the small intestine, the ATP7A protein helps control the absorption of Cu(I) from food. After Cu(I) ions are absorbed into
1572:
and is expressed in the intestine and all tissues except liver. In the intestine, ATP7A regulates Cu(I) absorption in the human body by transporting Cu(I) from the small intestine into the blood. In other tissues, ATP7A shuttles between the
1715:
between the cysteine residues is broken as cysteine starts to bind to Cu(I), leading to a series of conformational changes at the N-terminal of the protein, and possibly activating the Cu(I)-transporting activity of other cytosolic loops.
1698:
mechanism is observed. When the Cu(I) concentration is low, Cu(I) has a lower affinity for ATP7A compared to Zn(II); as the Cu(I) concentration increases, a dramatic increasing affinity of Cu(I) for the protein is observed.
3626:
2995:
Kaler SG, Gallo LK, Proud VK, Percy AK, Mark Y, Segal NA, Goldstein DS, Holmes CS, Gahl WA (1995). "Occipital horn syndrome and a mild Menkes phenotype associated with splice site mutations at the MNK locus".
3611:
3106:
Mercer JF, Livingston J, Hall B, Paynter JA, Begy C, Chandrasekharappa S, Lockhart P, Grimes A, Bhave M, Siemieniak D (1993). "Isolation of a partial candidate gene for Menkes disease by positional cloning".
3761:
3068:
Chelly J, Tümer Z, Tønnesen T, Petterson A, Ishikawa-Brush Y, Tommerup N, Horn N, Monaco AP (1993). "Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein".
1912:
proteins, and mice with mutations in Atp7a have a delayed onset of prion disease. A comprehensive resource of clinically annotated genetic variants in ATP7A gene has been made available confirming to the
3746:
1577:
and the cell membrane to maintain proper Cu(I) concentrations (since there is no free Cu(I) in the cell, Cu(I) ions are all tightly bound) in the cell and provides certain enzymes with Cu(I) (e.g.
2639:
Greenough M, Pase L, Voskoboinik I, Petris MJ, O'Brien AW, Camakaris J (2004). "Signals regulating trafficking of Menkes (MNK; ATP7A) copper-translocating P-type ATPase in polarized MDCK cells".
3581:
3181:
Levinson B, Conant R, Schnur R, Das S, Packman S, Gitschier J (1997). "A repeated element in the regulatory region of the MNK gene and its deletion in a patient with occipital horn syndrome".
3566:
3686:
3671:
3731:
3551:
1769:
In other organs and tissues, the ATP7A protein has a dual role and shuttles between two locations within the cell. The protein normally resides in a cell structure called the
3802:
1881:(GRX1) has is also essential for ATP7A function. It promotes Cu(I) binding for subsequent transport by catalyzing the reduction of disulfide bridges. It may also catalyze de-
1740:(D) residue within the enzyme. The first step is ATP binding to the ATP-binding domain and Cu(I) binding to the transmembrane region. Then ATP7A is phosphorylated at the key
3144:
Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J (1993). "Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase".
3716:
3701:
1914:
387:
286:
3641:
3257:"Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking"
3421:
Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ (1998). "Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase".
3476:
GeneReviews/NCBI/NIH/UW entry on ATP7A-Related Copper
Transport Disorders Includes: Menkes Disease, Occipital Horn Syndrome, ATP7A-Related Distal Motor Neuropathy
3656:
2828:
Voskoboinik I, Camakaris J (2003). "Menkes copper-translocating P-type ATPase (ATP7A): biochemical and cell biology properties, and role in Menkes disease".
2719:
Voskoboinik I, Camakaris J (2002). "Menkes copper-translocating P-type ATPase (ATP7A): biochemical and cell biology properties, and role in Menkes disease".
2966:
Tümer Z, Vural B, Tønnesen T, Chelly J, Monaco AP, Horn N (1995). "Characterization of the exon structure of the Menkes disease gene using vectorette PCR".
5340:
1274:
1255:
1877:(ATOX1) is required to maintain Cu(I) copper homeostasis in the cell. It can bind and transport cytosolic Cu(I) to ATP7A in the trans-Golgi-network.
209:
4495:
5525:
3795:
4025:
3531:
2773:
2354:
2057:
2022:
5105:
3994:
2309:
Crisponi G, Nurchi VM, Fanni D, Gerosa C, Nemolato S, Faa G (April 2010). "Copper-related diseases: From chemistry to molecular pathology".
5746:
2004:
3596:
4719:
5101:
373:
3788:
3491:
1497:
1490:
2678:"Similar splice-site mutations of the ATP7A gene lead to different phenotypes: classical Menkes disease or occipital horn syndrome"
350:
4694:
1925:
A proton pump inhibitor, Omeprazole, has been shown to block ATP7A, in addition to its more established role of blocking ATP4A.
1660:
The TGEA motif lies in the loop on the cytosolic side between transmembrane segments 4 and 5 and is involved in energy transfer.
5680:
4585:
1991:
1970:
1773:, which modifies and transports newly produced enzymes and other proteins. Here, ATP7A supplies Cu(I) to certain enzymes (e.g.
5333:
4672:
4580:
3485:
2606:"The copper-transporting ATPases, menkes and wilson disease proteins, have distinct roles in adult and developing cerebellum"
1667:
Between transmembrane segments 6 and 7 is a large cytoplasmic loop, where three motifs are located: DKTG, SEHPL, and GDGXND.
3480:
1987:
3635:: Solution structure and backbone dynamics of the Cu(I) form of the second metal-binding domain of the Menkes protein ATP7A
3497:
2937:
Dierick HA, Ambrosini L, Spencer J, Glover TW, Mercer JF (1996). "Molecular structure of the Menkes disease gene (ATP7A)".
2756:
Harris ED, Reddy MC, Qian Y, Tiffany-Castiglioni E, Majumdar S, Nelson J (1999). "Multiple Forms of the Menkes Cu-ATPase".
272:
247:
52:
4602:
1774:
1578:
3620:: Solution structure and backbone dynamics of the apo-form of the second metal-binding domain of the Menkes protein ATP7A
2129:"Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases"
1966:
4650:
3967:
1689:
The GDGXND motif near transmembrane segment 7 is thought to contain mainly α-helices and serves as a structural support.
189:
3380:"A C2055T transition in exon 8 of the ATP7A gene is associated with exon skipping in an occipital horn syndrome family"
4572:
3770:: Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein)
386:
285:
1644:
A large N-terminal cytosolic domain that contains six repeated Cu(I)-binding sites, each containing a GMTCXXC motif.
4703:
2865:
La
Fontaine S, Mercer JF (2007). "Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis".
379:
278:
5326:
5308:
5068:
5063:
4631:
4172:
4070:
3895:
3891:
3868:
3841:
3828:
3815:
3524:
3755:: Solution structure of the apo form of the third metal-binding domain of ATP7A protein (Menkes Disease protein)
2251:"Cellular multitasking: the dual role of human Cu-ATPases in cofactor delivery and intracellular copper balance"
5716:
4186:
3881:
3846:
3819:
3469:
1319:
197:
1626:
with the N- and C-termini both oriented towards the cytosol (see picture). It is highly homologous to protein
5721:
4556:
4519:
3858:
1901:
1300:
3475:
3335:"Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network"
5583:
5353:
5161:
4286:
3926:
3590:: Solution Structure of the Cu(I) bound form of the first heavy metal binding motif of the Menkes protein
5698:
5489:
5453:
5370:
4416:
4324:
1623:
1569:
2040:
Tümer Z, Møller LB, Horn N (1999). "Mutation
Spectrum of ATP7A, the Gene Defective in Menkes Disease".
1900:
in the ATP7A gene. Researchers have identified different ATP7A mutations that cause Menkes disease and
5690:
5672:
5432:
5427:
5422:
4687:
3575:: Solution Structure of the Reduced Form of the First Heavy Metal Binding Motif of the Menkes Protein
3517:
2140:
1763:
1635:
261:
5196:
1663:
The CPC motif located in transmembrane segment 6 is common for all heavy metal transporting ATPases.
4621:
3503:
1938:
1882:
1833:
1469:
1448:
1414:
1393:
176:
3465:
5708:
4636:
4202:
3780:
3446:
3169:
3132:
3094:
3021:
2853:
2816:
2744:
2664:
2458:
2109:
221:
3695:: Solution structure of the Cu(I) form of the sixth soluble domain A69P mutant of Menkes protein
1473:
1444:
1418:
1389:
2676:
Møller LB, Tümer Z, Lund C, Petersen C, Cole T, Hanusch R, Seidel J, Jensen LR, Horn N (2000).
2527:"Disruption of copper homeostasis due to a mutation of Atp7a delays the onset of prion disease"
5654:
3876:
3680:: Solution structure of the apo form of the sixth soluble domain A69P mutant of Menkes protein
3438:
3409:
3366:
3321:
3286:
3243:
3198:
3161:
3124:
3086:
3056:
3013:
2983:
2954:
2925:
2882:
2845:
2808:
2779:
2769:
2736:
2707:
2656:
2627:
2558:
2507:
2450:
2401:
2350:
2280:
2222:
2166:
2101:
2063:
2053:
1745:
1648:
169:
45:
5295:
5290:
5275:
4963:
5570:
5361:
5259:
5253:
5248:
5226:
5216:
5206:
5173:
5055:
5050:
5040:
4821:
4761:
4266:
4212:
4194:
4060:
4050:
4004:
3430:
3399:
3391:
3356:
3346:
3311:
3276:
3268:
3233:
3223:
3190:
3153:
3116:
3078:
3046:
3005:
2975:
2946:
2915:
2907:
2874:
2837:
2800:
2761:
2728:
2697:
2689:
2648:
2617:
2548:
2538:
2497:
2489:
2440:
2432:
2391:
2383:
2318:
2270:
2262:
2212:
2204:
2156:
2148:
2093:
2045:
466:
397:
341:
296:
5237:
5077:
5072:
4079:
3212:"Biochemical characterization and intracellular localization of the Menkes disease protein"
2084:
Kodama H, Murata Y (Aug 1999). "Molecular genetics and pathophysiology of Menkes disease".
1744:(D) residue in the highly conserved DKTG motif, accompanied by Cu(I) release. A subsequent
217:
5662:
5608:
5444:
5185:
5011:
4707:
4680:
4613:
4502:
4316:
4016:
3836:
3740:: FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES
3560:: FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES
2525:
Siggs OM, Cruite JT, Du X, Rutschmann S, Masliah E, Beutler B, Oldstone MB (August 2012).
1843:
Delivers Cu(I) to placental cuproenzymes and transports Cu(I) into the foetal circulation
1829:
1809:
1770:
1733:
1676:
1574:
441:
3300:"Identification of point mutations in 41 unrelated patients affected with Menkes disease"
2445:
2420:
2144:
5390:
5109:
5093:
3936:
3404:
3379:
3361:
3334:
3316:
3299:
3272:
3051:
3034:
2920:
2895:
2702:
2677:
2553:
2526:
2502:
2477:
2396:
2371:
2275:
2250:
2217:
2192:
2161:
2128:
1893:
1712:
1594:
1565:
28:
3395:
3281:
3256:
2186:
2184:
2182:
2180:
1189:
1184:
1179:
1174:
1169:
1164:
1159:
1154:
1149:
1144:
1139:
1134:
1129:
1124:
1119:
1114:
1109:
1104:
1099:
1094:
1089:
1084:
1079:
1074:
1069:
1064:
1059:
1054:
1049:
1044:
1039:
1034:
1029:
1024:
1019:
1014:
1009:
1004:
999:
994:
989:
984:
979:
974:
969:
964:
959:
954:
949:
944:
939:
934:
929:
924:
919:
914:
909:
904:
899:
894:
889:
884:
879:
874:
869:
864:
859:
843:
838:
833:
828:
823:
818:
813:
808:
803:
798:
793:
788:
783:
778:
773:
768:
763:
758:
753:
748:
743:
738:
733:
717:
712:
707:
702:
697:
692:
687:
682:
677:
672:
667:
662:
657:
5740:
5588:
5537:
5189:
5001:
4480:
4090:
3238:
3211:
3098:
2979:
2097:
1813:
1782:
1741:
1737:
1729:
1695:
1672:
1586:
1561:
644:
3725:: Solution structure of the Cu(I) form of the sixth soluble domain of Menkes protein
3173:
3025:
2857:
2820:
2748:
2668:
2462:
2113:
1682:
The SEHPL motif only exists in heavy metal transporting P-type ATPases. Without the
5463:
4728:
4715:
4465:
4438:
4367:
4360:
4343:
4338:
4312:
3136:
2577:"ATP7Agen a comprehensive resource for clinically annotated variants in ATP7A Gene"
1885:
reaction of the C (cysteine) residues within the six Cu(I)-binding motifs GMTCXXC.
1610:
459:
238:
3710:: Solution structure of the apo form of the sixth soluble domain of Menkes protein
3450:
201:
2791:
Cox DW, Moore SD (2003). "Copper transporting P-type ATPases and human disease".
225:
5645:
5552:
5547:
5520:
5418:
5413:
4561:
3650:: Solution structure of the copper(I) form of the fifth domain of Menkes protein
2765:
2760:. Advances in Experimental Medicine and Biology. Vol. 448. pp. 39–51.
2079:
2077:
2049:
2044:. Advances in Experimental Medicine and Biology. Vol. 448. pp. 83–95.
2027:
National Center for
Biotechnology Information, U.S. National Library of Medicine
2009:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1837:
5318:
3255:
Petris MJ, Mercer JF, Culvenor JG, Lockhart P, Gleeson PA, Camakaris J (1997).
3035:"Diverse mutations in patients with Menkes disease often lead to exon skipping"
2652:
2152:
542:
5542:
5409:
5349:
4546:
4235:
2911:
2878:
2841:
2804:
2732:
2493:
2436:
2322:
2266:
2208:
1823:
1778:
1759:
1582:
358:
255:
205:
3228:
2193:"ATP7A-related copper transport diseases-emerging concepts and future trends"
5530:
4252:
3811:
3194:
2543:
2304:
2302:
2300:
2298:
2296:
2294:
1854:
Distributes Cu(I) in the various compartments of the central nervous system
1683:
1219:
602:
480:
425:
412:
324:
311:
213:
2950:
2929:
2886:
2849:
2812:
2783:
2740:
2711:
2660:
2631:
2622:
2605:
2562:
2511:
2454:
2405:
2284:
2226:
2170:
2105:
2067:
3665:: Solution structure of the apo form of the fifth domain of Menkes protein
3442:
3413:
3370:
3351:
3325:
3290:
3247:
3202:
3165:
3128:
3090:
3060:
3017:
2987:
2958:
1537:
1532:
5511:
5498:
5468:
5458:
5404:
5379:
5169:
4968:
4958:
4953:
4938:
4933:
4928:
4918:
4913:
4908:
4898:
4893:
4883:
4878:
4873:
4868:
4849:
4841:
4737:
1897:
1788:
The functions of ATP7A in some tissues of the human body are as follows:
1708:
1521:
1364:
1345:
2244:
2242:
2240:
2238:
2236:
5631:
5626:
5593:
5285:
5280:
4948:
4943:
4923:
4903:
4888:
4863:
4858:
4853:
4657:
4626:
4404:
4399:
4158:
4148:
4123:
4118:
3853:
3434:
3009:
2576:
2387:
1671:
The DKTG motif is essential for the proper function of the ATPase. The
1331:
1286:
1175:
positive regulation of vascular associated smooth muscle cell migration
3120:
3082:
3033:
Das S, Levinson B, Whitney S, Vulpe C, Packman S, Gitschier J (1994).
2896:"Biochemical basis of regulation of human copper-transporting ATPases"
2421:"Cellular copper distribution: a mechanistic systems biology approach"
146:
142:
138:
134:
130:
126:
122:
118:
114:
110:
106:
102:
98:
94:
90:
86:
82:
78:
74:
5269:
5264:
5243:
5221:
5211:
5148:
5143:
5138:
5133:
5128:
5123:
5118:
5113:
5085:
5045:
5035:
5030:
5025:
5020:
5015:
4985:
4975:
4811:
4791:
4786:
4781:
4776:
4756:
4746:
4711:
4534:
4176:
4153:
4143:
4113:
4108:
4103:
4098:
4055:
4045:
4040:
4035:
4030:
3999:
3987:
3982:
3977:
3972:
3960:
3955:
3950:
3899:
3378:
Ronce N, Moizard MP, Robb L, Toutain A, Villard L, Moraine C (1997).
3157:
1638:
that form a channel and allow for Cu(I) to pass through the membrane;
1505:
1241:
2693:
5598:
5232:
5097:
4831:
4826:
4816:
4806:
4801:
4796:
4771:
4766:
4751:
4590:
4529:
4512:
4507:
4355:
4333:
4299:
4294:
4279:
4257:
4245:
4240:
4230:
4225:
4220:
3945:
1943:
1934:
1909:
1874:
1866:
1627:
3298:
Tümer Z, Lund C, Tolshave J, Vural B, Tønnesen T, Horn N (1997).
1568:
to transport Cu(I) across cell membranes. The ATP7A protein is a
1204:
1200:
5621:
5616:
5515:
5399:
5200:
4595:
4551:
4539:
4524:
4490:
4485:
4470:
4453:
4448:
4443:
4431:
4426:
4421:
4411:
4387:
4382:
4377:
4372:
4274:
1878:
1870:
193:
5322:
4676:
3784:
3513:
4645:
4641:
3509:
2347:
Biological inorganic chemistry : structure and reactivity
2604:
Barnes N, Tsivkovskii R, Tsivkovskaia N, Lutsenko S (2005).
1115:
cellular response to platelet-derived growth factor stimulus
2419:
Banci L, Bertini I, Cantini F, Ciofi-Baffoni S (Aug 2010).
1818:
Removes excess Cu(I) to maintain Cu(I) level in the kidney
1589:). The X-linked, inherited, lethal genetic disorder of the
1597:, a copper deficiency resulting in early childhood death.
180:, DSMAX, MK, MNK, SMAX3, ATPase copper transporting alpha
3481:
OMIM entries on ATP7A-Related Copper
Transport Disorders
3333:
Dierick HA, Adam AN, Escara-Wilke JF, Glover TW (1997).
2370:
Inesi G, Pilankatta R, Tadini-Buoninsegni F (Oct 2014).
678:
ATPase-coupled cation transmembrane transporter activity
449:
2372:"Biochemical characterization of P-type copper ATPases"
1652:
Proposed structure of copper-transporting protein ATP7A
1110:
negative regulation of iron ion transmembrane transport
2478:"The many "faces" of copper in medicine and treatment"
2249:
Lutsenko S, Gupta A, Burkhead JL, Zuzel V (Aug 2008).
614:
1917:
guidelines for interpretation of sequence variants.
1125:
positive regulation of epithelial cell proliferation
5707:
5689:
5671:
5653:
5644:
5607:
5569:
5488:
5481:
5443:
5389:
5378:
5369:
5360:
5000:
4984:
4840:
4736:
4727:
4611:
4570:
4310:
4184:
4171:
4136:
4088:
4069:
4015:
3935:
3914:
3907:
3890:
3867:
3827:
3210:Yamaguchi Y, Heiny ME, Suzuki M, Gitlin JD (1997).
1462:
1437:
1407:
1382:
3605:: Second Metal Binding Domain of the Menkes ATPase
2476:Hordyjewska A, Popiołek Ł, Kocot J (August 2014).
2345:Bertini I, Gray H, Stiefel E, Valentine J (2006).
1983:
1981:
1979:
1962:
1960:
1958:
1656:Many motifs in the ATP7A structure are conserved:
1915:American College of Medical Genetics and Genomics
1630:. ATP7A contains three major functional domains:
396:
295:
1762:, ATP7A is required to transfer them across the
2340:
2338:
2336:
2334:
2332:
1988:GRCm38: Ensembl release 89: ENSMUSG00000033792
950:positive regulation of oxidoreductase activity
693:superoxide dismutase copper chaperone activity
5334:
4688:
3796:
3525:
1728:ATP7A belongs to a transporter family called
1100:positive regulation of lamellipodium assembly
683:copper ion transmembrane transporter activity
8:
1686:(H) residue ATP7A may not function properly.
2349:. Sausalito, CA: University Science Books.
1967:GRCh38: Ensembl release 89: ENSG00000165240
1609:gene is located on the long (q) arm of the
1180:regulation of cytochrome-c oxidase activity
1170:positive regulation of response to wounding
713:P-type divalent copper transporter activity
5650:
5485:
5386:
5375:
5366:
5341:
5327:
5319:
4733:
4695:
4681:
4673:
4181:
3911:
3904:
3803:
3789:
3781:
3532:
3518:
3510:
1215:
640:
437:
336:
233:
63:
5084:3.A.3.1.4: H/K transporting, nongastric:
3468:at the U.S. National Library of Medicine
3403:
3360:
3350:
3315:
3280:
3237:
3227:
3050:
2919:
2894:Lutsenko S, LeShane ES, Shinde U (2007).
2701:
2621:
2552:
2542:
2501:
2444:
2395:
2274:
2216:
2160:
2127:Šimčíková D, Heneberg P (December 2019).
1694:Zn(II). In the case of Cu(I), a possible
1075:negative regulation of catalytic activity
1050:positive regulation of catalytic activity
990:central nervous system neuron development
1790:
1647:
1130:cellular response to amino acid stimulus
980:cerebellar Purkinje cell differentiation
5526:Iron-responsive element-binding protein
3547:
2255:Archives of Biochemistry and Biophysics
1954:
1749:is released on the extracellular side.
930:regulation of oxidative phosphorylation
1865:ATP7A has been shown to interact with
18:
734:trans-Golgi network transport vesicle
401:
362:
357:
300:
259:
254:
7:
2425:Cellular and Molecular Life Sciences
1040:plasma membrane copper ion transport
1564:which uses the energy arising from
3273:10.1002/j.1460-2075.1996.tb00997.x
2758:Copper Transport and Its Disorders
2042:Copper Transport and Its Disorders
1459:
1434:
1404:
1379:
1355:
1336:
1310:
1291:
1265:
1246:
619:
565:choroid plexus of fourth ventricle
537:
475:
454:
14:
4729:F-, V-, and A-type ATPase (3.A.2)
895:extracellular matrix organization
3760:
3745:
3730:
3715:
3700:
3685:
3670:
3655:
3640:
3625:
3610:
3595:
3580:
3565:
3550:
2098:10.1046/j.1442-200x.1999.01091.x
1140:cellular response to cadmium ion
1120:positive regulation of cell size
860:norepinephrine metabolic process
698:copper-dependent protein binding
385:
378:
372:
349:
284:
277:
271:
246:
27:
5681:Phosphoric acids and phosphates
4745:H transporting, mitochondrial:
1150:cellular response to copper ion
1145:cellular response to cobalt ion
1135:cellular response to antibiotic
1065:cellular copper ion homeostasis
1025:catecholamine metabolic process
885:neuron projection morphogenesis
784:perinuclear region of cytoplasm
2311:Coordination Chemistry Reviews
1875:Antioxidant 1 copper chaperone
1105:antimicrobial humoral response
1000:in utero embryonic development
870:removal of superoxide radicals
744:integral component of membrane
603:More reference expression data
1:
5414:Ferroportin (SLC11A3/SLC40A1)
3396:10.1016/S0002-9297(07)64297-9
1160:cellular response to lead ion
1155:cellular response to iron ion
1095:regulation of gene expression
1055:epinephrine metabolic process
910:T-helper cell differentiation
370:
269:
16:Protein-coding gene in humans
3216:Proc. Natl. Acad. Sci. U.S.A
2980:10.1016/0888-7543(95)80160-N
2531:Proc. Natl. Acad. Sci. U.S.A
1679:during the transport cycles.
1560:), is a copper-transporting
1165:cellular response to hypoxia
1060:elastin biosynthetic process
1020:peptidyl-lysine modification
920:tryptophan metabolic process
900:collagen fibril organization
890:pyramidal neuron development
875:detoxification of copper ion
553:Epithelium of choroid plexus
5747:Genes on human chromosome X
4573:Protein-synthesizing GTPase
2766:10.1007/978-1-4615-4859-1_4
2050:10.1007/978-1-4615-4859-1_7
1812:of the proximal and distal
1035:hair follicle morphogenesis
1005:ion transmembrane transport
960:serotonin metabolic process
829:phagocytic vesicle membrane
794:basolateral plasma membrane
5763:
5155:3.A.3.5: Cu transporting:
4704:Membrane transport protein
3502:gene details page in the
2653:10.1152/ajpcell.00179.2004
2153:10.1038/s41598-019-54976-4
975:mitochondrion organization
905:dopamine metabolic process
573:retinal pigment epithelium
5507:
5304:
4850:H transporting, lysosomal
4632:Guanylate-binding protein
3816:acid anhydride hydrolases
3545:
2912:10.1016/j.abb.2007.04.013
2879:10.1016/j.abb.2007.04.021
2641:Am J Physiol Cell Physiol
2494:10.1007/s10534-014-9736-5
2437:10.1007/s00018-010-0330-x
2323:10.1016/j.ccr.2009.12.018
2267:10.1016/j.abb.2008.05.005
2209:10.1038/nrneurol.2010.180
2197:Nature Reviews. Neurology
2023:"Mouse PubMed Reference:"
2005:"Human PubMed Reference:"
1536:
1531:
1527:
1520:
1504:
1498:Chr X: 105.07 – 105.17 Mb
1485:
1466:
1441:
1430:
1411:
1386:
1375:
1362:
1358:
1343:
1339:
1330:
1317:
1313:
1298:
1294:
1285:
1272:
1268:
1253:
1249:
1240:
1225:
1218:
1214:
1198:
1085:response to manganese ion
1010:lung alveolus development
865:response to iron(III) ion
643:
639:
627:
622:
613:
600:
549:
540:
487:
478:
448:
440:
436:
419:
406:
369:
348:
339:
335:
318:
305:
268:
245:
236:
232:
187:
184:
174:
167:
162:
71:
66:
49:
44:
39:
35:
26:
21:
5717:Calcium-sensing receptor
5464:Calreticulin/mobilferrin
4187:Heterotrimeric G protein
3882:Phosphoadenylylsulfatase
3470:Medical Subject Headings
3229:10.1073/pnas.93.24.14030
2086:Pediatrics International
1775:peptidyl-α-monooxygenase
1579:peptidyl-α-monooxygenase
970:blood vessel development
557:Rostral migratory stream
5722:Calcium-binding protein
3859:Thiamine-triphosphatase
2842:10.1023/A:1021250003104
2805:10.1023/A:1021293818125
2733:10.1023/A:1021250003104
2544:10.1073/pnas.1211499109
2376:The Biochemical Journal
1902:occipital horn syndrome
1491:Chr X: 77.91 – 78.05 Mb
1015:blood vessel remodeling
569:external carotid artery
561:internal carotid artery
2951:10.1006/geno.1995.1175
2900:Arch. Biochem. Biophys
2867:Arch. Biochem. Biophys
2623:10.1074/jbc.M413840200
1848:Central nervous system
1766:into the circulation.
1732:, which catalyze auto-
1653:
1641:An ATP-binding domain;
1636:transmembrane segments
985:elastic fiber assembly
945:response to copper ion
824:apical plasma membrane
5699:Magnesium transporter
5490:Iron-binding proteins
5454:Duodenal cytochrome B
4614:Polymerization motors
4325:Rho family of GTPases
3195:10.1093/hmg/5.11.1737
2830:J. Bioenerg. Biomembr
2793:J. Bioenerg. Biomembr
2191:Kaler SG (Jan 2011).
1889:Clinical significance
1703:Conformational change
1651:
1624:transmembrane protein
1570:transmembrane protein
940:cartilage development
789:brush border membrane
779:endoplasmic reticulum
5691:Magnesium metabolism
5673:Phosphate metabolism
5423:Transferrin receptor
3496:genome location and
3466:ATP7A+protein,+human
1836:and foetal vascular
1764:basolateral membrane
1090:response to lead ion
1070:copper ion transport
925:response to zinc ion
364:X chromosome (mouse)
262:X chromosome (human)
67:List of PDB id codes
40:Available structures
5258:Class VI, type 11:
4622:dynamin superfamily
3504:UCSC Genome Browser
3352:10.1093/hmg/6.3.409
2721:J Bioenerg Biomembr
2581:clingen.igib.res.in
2145:2019NatSR...918577S
1834:syncytiotrophoblast
1736:of a key conserved
1724:Transport mechanism
1696:cooperative-binding
1030:metal ion transport
935:locomotory behavior
749:trans-Golgi network
718:cuprous ion binding
503:germinal epithelium
403:X D|X 47.36 cM
5709:Calcium metabolism
5242:Class V, type 10:
5231:Class II, type 9:
3435:10.1038/nsb0198-47
3010:10.1038/ng1094-195
2388:10.1042/BJ20140741
2133:Scientific Reports
1654:
1320:ENSMUSG00000033792
853:Biological process
774:neuronal cell body
727:Cellular component
673:hydrolase activity
663:copper ion binding
658:nucleotide binding
651:Molecular function
491:buccal mucosa cell
5734:
5733:
5730:
5729:
5655:Sodium metabolism
5640:
5639:
5571:Copper metabolism
5565:
5564:
5561:
5560:
5477:
5476:
5316:
5315:
5205:Class I, type 8:
5012:Na/K transporting
4996:
4995:
4670:
4669:
4666:
4665:
4167:
4166:
4132:
4131:
3877:Adenylylsulfatase
3778:
3777:
3423:Nat. Struct. Biol
3384:Am. J. Hum. Genet
3304:Am. J. Hum. Genet
3121:10.1038/ng0193-20
3083:10.1038/ng0193-14
3039:Am. J. Hum. Genet
2775:978-1-4613-7204-2
2356:978-1-891389-43-6
2059:978-1-4613-7204-2
1883:glutathionylation
1858:
1857:
1851:Various locations
1746:dephosphorylation
1713:disulfide bonding
1547:
1546:
1543:
1542:
1516:
1515:
1481:
1480:
1456:
1455:
1426:
1425:
1401:
1400:
1371:
1370:
1352:
1351:
1326:
1325:
1307:
1306:
1281:
1280:
1262:
1261:
1210:
1209:
1185:copper ion export
1080:liver development
880:copper ion import
834:cell leading edge
799:secretory granule
764:neuron projection
708:chaperone binding
668:metal ion binding
635:
634:
631:
630:
609:
608:
596:
595:
534:
533:
507:corpus epididymis
432:
431:
331:
330:
226:ATP7A - orthologs
158:
157:
154:
153:
50:Ortholog search:
5754:
5651:
5486:
5387:
5376:
5367:
5362:Transition metal
5354:Metal metabolism
5343:
5336:
5329:
5320:
5309:ATPase disorders
5180:Other/ungrouped:
4734:
4697:
4690:
4683:
4674:
4182:
3912:
3905:
3805:
3798:
3791:
3782:
3764:
3749:
3734:
3719:
3704:
3689:
3674:
3659:
3644:
3629:
3614:
3599:
3584:
3569:
3554:
3534:
3527:
3520:
3511:
3454:
3417:
3407:
3374:
3364:
3354:
3329:
3319:
3294:
3284:
3251:
3241:
3231:
3206:
3177:
3158:10.1038/ng0193-7
3140:
3102:
3064:
3054:
3029:
2991:
2962:
2933:
2923:
2890:
2861:
2824:
2787:
2752:
2715:
2705:
2672:
2635:
2625:
2591:
2590:
2588:
2587:
2573:
2567:
2566:
2556:
2546:
2522:
2516:
2515:
2505:
2473:
2467:
2466:
2448:
2416:
2410:
2409:
2399:
2367:
2361:
2360:
2342:
2327:
2326:
2317:(7–8): 876–889.
2306:
2289:
2288:
2278:
2246:
2231:
2230:
2220:
2188:
2175:
2174:
2164:
2124:
2118:
2117:
2081:
2072:
2071:
2037:
2031:
2030:
2019:
2013:
2012:
2001:
1995:
1985:
1974:
1964:
1939:Wilson's disease
1810:epithelial cells
1791:
1552:, also known as
1529:
1528:
1500:
1493:
1476:
1460:
1451:
1435:
1431:RefSeq (protein)
1421:
1405:
1396:
1380:
1356:
1337:
1311:
1292:
1266:
1247:
1216:
995:cation transport
915:skin development
641:
620:
605:
585:efferent ductule
545:
543:Top expressed in
538:
483:
481:Top expressed in
476:
455:
438:
428:
415:
404:
389:
382:
376:
365:
353:
337:
327:
314:
303:
288:
281:
275:
264:
250:
234:
228:
179:
172:
149:
64:
58:
37:
36:
31:
19:
5762:
5761:
5757:
5756:
5755:
5753:
5752:
5751:
5737:
5736:
5735:
5726:
5703:
5685:
5667:
5636:
5609:Zinc metabolism
5603:
5557:
5503:
5473:
5445:Iron(III) oxide
5439:
5381:
5371:Iron metabolism
5356:
5347:
5317:
5312:
5300:
5197:Mg transporting
5110:Ca transporting
4992:
4991:found in Archea
4980:
4836:
4723:
4701:
4671:
4662:
4607:
4566:
4317:Ras superfamily
4306:
4290:
4270:
4216:
4206:
4198:
4163:
4128:
4084:
4065:
4011:
3968:Plasma membrane
3931:
3886:
3863:
3837:Pyrophosphatase
3823:
3809:
3779:
3774:
3771:
3765:
3756:
3750:
3741:
3735:
3726:
3720:
3711:
3705:
3696:
3690:
3681:
3675:
3666:
3660:
3651:
3645:
3636:
3630:
3621:
3615:
3606:
3600:
3591:
3585:
3576:
3570:
3561:
3555:
3541:
3538:
3462:
3457:
3420:
3377:
3339:Hum. Mol. Genet
3332:
3297:
3267:(22): 6084–95.
3254:
3222:(24): 14030–5.
3209:
3189:(11): 1737–42.
3183:Hum. Mol. Genet
3180:
3143:
3105:
3067:
3032:
2994:
2965:
2936:
2893:
2864:
2827:
2790:
2776:
2755:
2718:
2675:
2647:(5): C1463–71.
2638:
2603:
2599:
2597:Further reading
2594:
2585:
2583:
2575:
2574:
2570:
2537:(34): 13733–8.
2524:
2523:
2519:
2475:
2474:
2470:
2431:(15): 2563–89.
2418:
2417:
2413:
2369:
2368:
2364:
2357:
2344:
2343:
2330:
2308:
2307:
2292:
2248:
2247:
2234:
2190:
2189:
2178:
2126:
2125:
2121:
2083:
2082:
2075:
2060:
2039:
2038:
2034:
2021:
2020:
2016:
2003:
2002:
1998:
1986:
1977:
1965:
1956:
1952:
1931:
1923:
1891:
1863:
1830:cytotrophoblast
1771:Golgi apparatus
1755:
1734:phosphorylation
1726:
1705:
1675:(D) residue is
1620:
1603:
1575:Golgi apparatus
1554:Menkes' protein
1538:View/Edit Mouse
1533:View/Edit Human
1496:
1489:
1486:Location (UCSC)
1472:
1468:
1447:
1443:
1417:
1413:
1392:
1388:
1301:ENSG00000165240
1194:
848:
804:plasma membrane
754:Golgi apparatus
722:
703:protein binding
601:
592:
587:
583:
579:
575:
571:
567:
563:
559:
555:
541:
530:
525:
523:visceral pleura
521:
519:parietal pleura
517:
515:Achilles tendon
513:
509:
505:
501:
497:
495:trabecular bone
493:
479:
423:
410:
402:
392:
391:
390:
383:
363:
340:Gene location (
322:
309:
301:
291:
290:
289:
282:
260:
237:Gene location (
188:
175:
168:
73:
51:
17:
12:
11:
5:
5760:
5758:
5750:
5749:
5739:
5738:
5732:
5731:
5728:
5727:
5725:
5724:
5719:
5713:
5711:
5705:
5704:
5702:
5701:
5695:
5693:
5687:
5686:
5684:
5683:
5677:
5675:
5669:
5668:
5666:
5665:
5659:
5657:
5648:
5642:
5641:
5638:
5637:
5635:
5634:
5629:
5624:
5619:
5613:
5611:
5605:
5604:
5602:
5601:
5596:
5591:
5586:
5581:
5575:
5573:
5567:
5566:
5563:
5562:
5559:
5558:
5556:
5555:
5550:
5545:
5540:
5535:
5534:
5533:
5523:
5518:
5508:
5505:
5504:
5502:
5501:
5495:
5493:
5483:
5479:
5478:
5475:
5474:
5472:
5471:
5466:
5461:
5456:
5450:
5448:
5441:
5440:
5438:
5437:
5436:
5435:
5430:
5416:
5407:
5402:
5400:DMT1 (SLC11A2)
5396:
5394:
5391:Iron(II) oxide
5384:
5373:
5364:
5358:
5357:
5348:
5346:
5345:
5338:
5331:
5323:
5314:
5313:
5305:
5302:
5301:
5299:
5298:
5293:
5288:
5283:
5278:
5272:
5267:
5262:
5256:
5251:
5246:
5240:
5235:
5229:
5224:
5219:
5214:
5209:
5203:
5193:
5192:
5182:
5181:
5177:
5176:
5165:
5164:
5159:
5152:
5151:
5146:
5141:
5136:
5131:
5126:
5121:
5116:
5089:
5088:
5081:
5080:
5075:
5069:H/K exchanging
5066:
5059:
5058:
5053:
5048:
5043:
5038:
5033:
5028:
5023:
5018:
5007:
5005:
4998:
4997:
4994:
4993:
4990:
4988:
4982:
4981:
4979:
4978:
4972:
4971:
4966:
4961:
4956:
4951:
4946:
4941:
4936:
4931:
4926:
4921:
4916:
4911:
4906:
4901:
4896:
4891:
4886:
4881:
4876:
4871:
4866:
4861:
4856:
4846:
4844:
4838:
4837:
4835:
4834:
4829:
4824:
4819:
4814:
4809:
4804:
4799:
4794:
4789:
4784:
4779:
4774:
4769:
4764:
4759:
4754:
4749:
4742:
4740:
4731:
4725:
4724:
4702:
4700:
4699:
4692:
4685:
4677:
4668:
4667:
4664:
4663:
4661:
4660:
4655:
4654:
4653:
4648:
4639:
4634:
4629:
4618:
4616:
4609:
4608:
4606:
4605:
4600:
4599:
4598:
4593:
4588:
4577:
4575:
4568:
4567:
4565:
4564:
4559:
4554:
4549:
4544:
4543:
4542:
4537:
4532:
4527:
4517:
4516:
4515:
4510:
4500:
4499:
4498:
4493:
4488:
4476:
4475:
4474:
4473:
4468:
4458:
4457:
4456:
4451:
4446:
4436:
4435:
4434:
4429:
4424:
4414:
4409:
4408:
4407:
4402:
4392:
4391:
4390:
4385:
4380:
4375:
4365:
4364:
4363:
4358:
4348:
4347:
4346:
4341:
4336:
4321:
4319:
4308:
4307:
4305:
4304:
4303:
4302:
4297:
4288:
4284:
4283:
4282:
4277:
4268:
4264:
4263:
4262:
4261:
4260:
4250:
4249:
4248:
4243:
4233:
4228:
4223:
4214:
4210:
4209:
4208:
4204:
4196:
4191:
4189:
4179:
4169:
4168:
4165:
4164:
4162:
4161:
4156:
4151:
4146:
4140:
4138:
4134:
4133:
4130:
4129:
4127:
4126:
4121:
4116:
4111:
4106:
4101:
4095:
4093:
4086:
4085:
4083:
4082:
4076:
4074:
4067:
4066:
4064:
4063:
4058:
4053:
4048:
4043:
4038:
4033:
4028:
4022:
4020:
4013:
4012:
4010:
4009:
4008:
4007:
4002:
3992:
3991:
3990:
3985:
3980:
3975:
3965:
3964:
3963:
3958:
3953:
3942:
3940:
3933:
3932:
3930:
3929:
3924:
3918:
3916:
3915:Cu++ (3.6.3.4)
3909:
3902:
3888:
3887:
3885:
3884:
3879:
3873:
3871:
3865:
3864:
3862:
3861:
3856:
3851:
3850:
3849:
3844:
3833:
3831:
3825:
3824:
3810:
3808:
3807:
3800:
3793:
3785:
3776:
3775:
3773:
3772:
3766:
3759:
3757:
3751:
3744:
3742:
3736:
3729:
3727:
3721:
3714:
3712:
3706:
3699:
3697:
3691:
3684:
3682:
3676:
3669:
3667:
3661:
3654:
3652:
3646:
3639:
3637:
3631:
3624:
3622:
3616:
3609:
3607:
3601:
3594:
3592:
3586:
3579:
3577:
3571:
3564:
3562:
3556:
3549:
3546:
3543:
3542:
3539:
3537:
3536:
3529:
3522:
3514:
3508:
3507:
3488:
3483:
3478:
3473:
3461:
3460:External links
3458:
3456:
3455:
3418:
3375:
3330:
3295:
3252:
3207:
3178:
3141:
3103:
3065:
3030:
3004:(2): 195–202.
2992:
2963:
2934:
2891:
2862:
2825:
2788:
2774:
2753:
2716:
2694:10.1086/302857
2688:(4): 1211–20.
2682:Am J Hum Genet
2673:
2636:
2616:(10): 9640–5.
2600:
2598:
2595:
2593:
2592:
2568:
2517:
2468:
2411:
2362:
2355:
2328:
2290:
2232:
2176:
2119:
2073:
2058:
2032:
2014:
1996:
1975:
1953:
1951:
1948:
1947:
1946:
1941:
1930:
1927:
1922:
1919:
1894:Menkes disease
1890:
1887:
1879:Glutaredoxin-1
1862:
1859:
1856:
1855:
1852:
1849:
1845:
1844:
1841:
1826:
1820:
1819:
1816:
1806:
1802:
1801:
1798:
1795:
1754:
1751:
1730:P-type ATPases
1725:
1722:
1704:
1701:
1691:
1690:
1687:
1680:
1677:phosphorylated
1665:
1664:
1661:
1646:
1645:
1642:
1639:
1619:
1616:
1602:
1599:
1595:Menkes disease
1566:ATP hydrolysis
1545:
1544:
1541:
1540:
1535:
1525:
1524:
1518:
1517:
1514:
1513:
1511:
1509:
1502:
1501:
1494:
1487:
1483:
1482:
1479:
1478:
1464:
1463:
1457:
1454:
1453:
1439:
1438:
1432:
1428:
1427:
1424:
1423:
1409:
1408:
1402:
1399:
1398:
1384:
1383:
1377:
1373:
1372:
1369:
1368:
1360:
1359:
1353:
1350:
1349:
1341:
1340:
1334:
1328:
1327:
1324:
1323:
1315:
1314:
1308:
1305:
1304:
1296:
1295:
1289:
1283:
1282:
1279:
1278:
1270:
1269:
1263:
1260:
1259:
1251:
1250:
1244:
1238:
1237:
1232:
1227:
1223:
1222:
1212:
1211:
1208:
1207:
1196:
1195:
1193:
1192:
1187:
1182:
1177:
1172:
1167:
1162:
1157:
1152:
1147:
1142:
1137:
1132:
1127:
1122:
1117:
1112:
1107:
1102:
1097:
1092:
1087:
1082:
1077:
1072:
1067:
1062:
1057:
1052:
1047:
1042:
1037:
1032:
1027:
1022:
1017:
1012:
1007:
1002:
997:
992:
987:
982:
977:
972:
967:
962:
957:
952:
947:
942:
937:
932:
927:
922:
917:
912:
907:
902:
897:
892:
887:
882:
877:
872:
867:
862:
856:
854:
850:
849:
847:
846:
841:
836:
831:
826:
821:
816:
811:
806:
801:
796:
791:
786:
781:
776:
771:
766:
761:
756:
751:
746:
741:
736:
730:
728:
724:
723:
721:
720:
715:
710:
705:
700:
695:
690:
685:
680:
675:
670:
665:
660:
654:
652:
648:
647:
637:
636:
633:
632:
629:
628:
625:
624:
617:
611:
610:
607:
606:
598:
597:
594:
593:
591:
590:
586:
582:
581:left lung lobe
578:
574:
570:
566:
562:
558:
554:
550:
547:
546:
535:
532:
531:
529:
528:
524:
520:
516:
512:
508:
504:
500:
496:
492:
488:
485:
484:
472:
471:
463:
452:
446:
445:
442:RNA expression
434:
433:
430:
429:
421:
417:
416:
408:
405:
400:
394:
393:
384:
377:
371:
367:
366:
361:
355:
354:
346:
345:
333:
332:
329:
328:
320:
316:
315:
307:
304:
299:
293:
292:
283:
276:
270:
266:
265:
258:
252:
251:
243:
242:
230:
229:
186:
182:
181:
173:
165:
164:
160:
159:
156:
155:
152:
151:
69:
68:
60:
59:
48:
42:
41:
33:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
5759:
5748:
5745:
5744:
5742:
5723:
5720:
5718:
5715:
5714:
5712:
5710:
5706:
5700:
5697:
5696:
5694:
5692:
5688:
5682:
5679:
5678:
5676:
5674:
5670:
5664:
5661:
5660:
5658:
5656:
5652:
5649:
5647:
5643:
5633:
5630:
5628:
5625:
5623:
5620:
5618:
5615:
5614:
5612:
5610:
5606:
5600:
5597:
5595:
5592:
5590:
5589:Ceruloplasmin
5587:
5585:
5582:
5580:
5577:
5576:
5574:
5572:
5568:
5554:
5551:
5549:
5546:
5544:
5541:
5539:
5538:Ceruloplasmin
5536:
5532:
5529:
5528:
5527:
5524:
5522:
5519:
5517:
5513:
5510:
5509:
5506:
5500:
5497:
5496:
5494:
5491:
5487:
5484:
5480:
5470:
5467:
5465:
5462:
5460:
5457:
5455:
5452:
5451:
5449:
5446:
5442:
5434:
5431:
5429:
5426:
5425:
5424:
5420:
5417:
5415:
5411:
5408:
5406:
5403:
5401:
5398:
5397:
5395:
5392:
5388:
5385:
5383:
5380:Absorption in
5377:
5374:
5372:
5368:
5365:
5363:
5359:
5355:
5351:
5344:
5339:
5337:
5332:
5330:
5325:
5324:
5321:
5311:
5310:
5303:
5297:
5294:
5292:
5289:
5287:
5284:
5282:
5279:
5277:
5273:
5271:
5268:
5266:
5263:
5261:
5257:
5255:
5252:
5250:
5247:
5245:
5241:
5239:
5236:
5234:
5230:
5228:
5225:
5223:
5220:
5218:
5215:
5213:
5210:
5208:
5204:
5202:
5198:
5195:
5194:
5191:
5187:
5184:
5183:
5179:
5178:
5175:
5171:
5167:
5166:
5163:
5160:
5158:
5154:
5153:
5150:
5147:
5145:
5142:
5140:
5137:
5135:
5132:
5130:
5127:
5125:
5122:
5120:
5117:
5115:
5111:
5107:
5103:
5099:
5095:
5091:
5090:
5087:
5083:
5082:
5079:
5076:
5074:
5070:
5067:
5065:
5061:
5060:
5057:
5054:
5052:
5049:
5047:
5044:
5042:
5039:
5037:
5034:
5032:
5029:
5027:
5024:
5022:
5019:
5017:
5013:
5009:
5008:
5006:
5003:
5002:P-type ATPase
4999:
4989:
4987:
4983:
4977:
4974:
4973:
4970:
4967:
4965:
4962:
4960:
4957:
4955:
4952:
4950:
4947:
4945:
4942:
4940:
4937:
4935:
4932:
4930:
4927:
4925:
4922:
4920:
4917:
4915:
4912:
4910:
4907:
4905:
4902:
4900:
4897:
4895:
4892:
4890:
4887:
4885:
4882:
4880:
4877:
4875:
4872:
4870:
4867:
4865:
4862:
4860:
4857:
4855:
4851:
4848:
4847:
4845:
4843:
4839:
4833:
4830:
4828:
4825:
4823:
4820:
4818:
4815:
4813:
4810:
4808:
4805:
4803:
4800:
4798:
4795:
4793:
4790:
4788:
4785:
4783:
4780:
4778:
4775:
4773:
4770:
4768:
4765:
4763:
4760:
4758:
4755:
4753:
4750:
4748:
4744:
4743:
4741:
4739:
4735:
4732:
4730:
4726:
4721:
4717:
4713:
4709:
4705:
4698:
4693:
4691:
4686:
4684:
4679:
4678:
4675:
4659:
4656:
4652:
4649:
4647:
4643:
4640:
4638:
4635:
4633:
4630:
4628:
4625:
4624:
4623:
4620:
4619:
4617:
4615:
4610:
4604:
4601:
4597:
4594:
4592:
4589:
4587:
4584:
4583:
4582:
4579:
4578:
4576:
4574:
4569:
4563:
4560:
4558:
4555:
4553:
4550:
4548:
4545:
4541:
4538:
4536:
4533:
4531:
4528:
4526:
4523:
4522:
4521:
4518:
4514:
4511:
4509:
4506:
4505:
4504:
4501:
4497:
4494:
4492:
4489:
4487:
4484:
4483:
4482:
4478:
4477:
4472:
4469:
4467:
4464:
4463:
4462:
4459:
4455:
4452:
4450:
4447:
4445:
4442:
4441:
4440:
4437:
4433:
4430:
4428:
4425:
4423:
4420:
4419:
4418:
4415:
4413:
4410:
4406:
4403:
4401:
4398:
4397:
4396:
4393:
4389:
4386:
4384:
4381:
4379:
4376:
4374:
4371:
4370:
4369:
4366:
4362:
4359:
4357:
4354:
4353:
4352:
4349:
4345:
4342:
4340:
4337:
4335:
4332:
4331:
4330:
4326:
4323:
4322:
4320:
4318:
4314:
4309:
4301:
4298:
4296:
4293:
4292:
4291:
4285:
4281:
4278:
4276:
4273:
4272:
4271:
4265:
4259:
4256:
4255:
4254:
4251:
4247:
4244:
4242:
4239:
4238:
4237:
4234:
4232:
4229:
4227:
4224:
4222:
4219:
4218:
4217:
4211:
4207:
4201:
4200:
4199:
4193:
4192:
4190:
4188:
4183:
4180:
4178:
4174:
4170:
4160:
4157:
4155:
4152:
4150:
4147:
4145:
4142:
4141:
4139:
4135:
4125:
4122:
4120:
4117:
4115:
4112:
4110:
4107:
4105:
4102:
4100:
4097:
4096:
4094:
4092:
4091:P-type ATPase
4087:
4081:
4078:
4077:
4075:
4072:
4068:
4062:
4059:
4057:
4054:
4052:
4049:
4047:
4044:
4042:
4039:
4037:
4034:
4032:
4029:
4027:
4024:
4023:
4021:
4018:
4014:
4006:
4003:
4001:
3998:
3997:
3996:
3993:
3989:
3986:
3984:
3981:
3979:
3976:
3974:
3971:
3970:
3969:
3966:
3962:
3959:
3957:
3954:
3952:
3949:
3948:
3947:
3944:
3943:
3941:
3938:
3934:
3928:
3925:
3923:
3920:
3919:
3917:
3913:
3910:
3906:
3903:
3901:
3897:
3893:
3889:
3883:
3880:
3878:
3875:
3874:
3872:
3870:
3866:
3860:
3857:
3855:
3852:
3848:
3845:
3843:
3840:
3839:
3838:
3835:
3834:
3832:
3830:
3826:
3821:
3817:
3813:
3806:
3801:
3799:
3794:
3792:
3787:
3786:
3783:
3769:
3763:
3758:
3754:
3748:
3743:
3739:
3733:
3728:
3724:
3718:
3713:
3709:
3703:
3698:
3694:
3688:
3683:
3679:
3673:
3668:
3664:
3658:
3653:
3649:
3643:
3638:
3634:
3628:
3623:
3619:
3613:
3608:
3604:
3598:
3593:
3589:
3583:
3578:
3574:
3568:
3563:
3559:
3553:
3548:
3544:
3535:
3530:
3528:
3523:
3521:
3516:
3515:
3512:
3505:
3501:
3500:
3495:
3494:
3489:
3487:
3484:
3482:
3479:
3477:
3474:
3471:
3467:
3464:
3463:
3459:
3452:
3448:
3444:
3440:
3436:
3432:
3428:
3424:
3419:
3415:
3411:
3406:
3401:
3397:
3393:
3389:
3385:
3381:
3376:
3372:
3368:
3363:
3358:
3353:
3348:
3345:(3): 409–16.
3344:
3340:
3336:
3331:
3327:
3323:
3318:
3313:
3309:
3305:
3301:
3296:
3292:
3288:
3283:
3278:
3274:
3270:
3266:
3262:
3258:
3253:
3249:
3245:
3240:
3235:
3230:
3225:
3221:
3217:
3213:
3208:
3204:
3200:
3196:
3192:
3188:
3184:
3179:
3175:
3171:
3167:
3163:
3159:
3155:
3151:
3147:
3142:
3138:
3134:
3130:
3126:
3122:
3118:
3114:
3110:
3104:
3100:
3096:
3092:
3088:
3084:
3080:
3076:
3072:
3066:
3062:
3058:
3053:
3048:
3044:
3040:
3036:
3031:
3027:
3023:
3019:
3015:
3011:
3007:
3003:
2999:
2993:
2989:
2985:
2981:
2977:
2974:(3): 437–42.
2973:
2969:
2964:
2960:
2956:
2952:
2948:
2944:
2940:
2935:
2931:
2927:
2922:
2917:
2913:
2909:
2906:(2): 134–48.
2905:
2901:
2897:
2892:
2888:
2884:
2880:
2876:
2873:(2): 149–67.
2872:
2868:
2863:
2859:
2855:
2851:
2847:
2843:
2839:
2836:(5): 363–71.
2835:
2831:
2826:
2822:
2818:
2814:
2810:
2806:
2802:
2798:
2794:
2789:
2785:
2781:
2777:
2771:
2767:
2763:
2759:
2754:
2750:
2746:
2742:
2738:
2734:
2730:
2727:(5): 363–71.
2726:
2722:
2717:
2713:
2709:
2704:
2699:
2695:
2691:
2687:
2683:
2679:
2674:
2670:
2666:
2662:
2658:
2654:
2650:
2646:
2642:
2637:
2633:
2629:
2624:
2619:
2615:
2611:
2607:
2602:
2601:
2596:
2582:
2578:
2572:
2569:
2564:
2560:
2555:
2550:
2545:
2540:
2536:
2532:
2528:
2521:
2518:
2513:
2509:
2504:
2499:
2495:
2491:
2488:(4): 611–21.
2487:
2483:
2479:
2472:
2469:
2464:
2460:
2456:
2452:
2447:
2442:
2438:
2434:
2430:
2426:
2422:
2415:
2412:
2407:
2403:
2398:
2393:
2389:
2385:
2382:(2): 167–76.
2381:
2377:
2373:
2366:
2363:
2358:
2352:
2348:
2341:
2339:
2337:
2335:
2333:
2329:
2324:
2320:
2316:
2312:
2305:
2303:
2301:
2299:
2297:
2295:
2291:
2286:
2282:
2277:
2272:
2268:
2264:
2260:
2256:
2252:
2245:
2243:
2241:
2239:
2237:
2233:
2228:
2224:
2219:
2214:
2210:
2206:
2202:
2198:
2194:
2187:
2185:
2183:
2181:
2177:
2172:
2168:
2163:
2158:
2154:
2150:
2146:
2142:
2138:
2134:
2130:
2123:
2120:
2115:
2111:
2107:
2103:
2099:
2095:
2091:
2087:
2080:
2078:
2074:
2069:
2065:
2061:
2055:
2051:
2047:
2043:
2036:
2033:
2028:
2024:
2018:
2015:
2010:
2006:
2000:
1997:
1993:
1989:
1984:
1982:
1980:
1976:
1972:
1968:
1963:
1961:
1959:
1955:
1949:
1945:
1942:
1940:
1936:
1933:
1932:
1928:
1926:
1920:
1918:
1916:
1911:
1905:
1903:
1899:
1896:is caused by
1895:
1888:
1886:
1884:
1880:
1876:
1872:
1868:
1860:
1853:
1850:
1847:
1846:
1842:
1839:
1835:
1831:
1827:
1825:
1822:
1821:
1817:
1815:
1814:renal tubules
1811:
1808:Expressed in
1807:
1804:
1803:
1799:
1796:
1793:
1792:
1789:
1786:
1784:
1783:lysyl oxidase
1780:
1776:
1772:
1767:
1765:
1761:
1752:
1750:
1747:
1743:
1742:aspartic acid
1739:
1738:aspartic acid
1735:
1731:
1723:
1721:
1717:
1714:
1710:
1702:
1700:
1697:
1688:
1685:
1681:
1678:
1674:
1673:aspartic acid
1670:
1669:
1668:
1662:
1659:
1658:
1657:
1650:
1643:
1640:
1637:
1633:
1632:
1631:
1629:
1625:
1617:
1615:
1612:
1608:
1600:
1598:
1596:
1592:
1588:
1587:lysyl oxidase
1584:
1580:
1576:
1571:
1567:
1563:
1562:P-type ATPase
1559:
1555:
1551:
1539:
1534:
1530:
1526:
1523:
1519:
1512:
1510:
1507:
1503:
1499:
1495:
1492:
1488:
1484:
1477:
1475:
1471:
1465:
1461:
1458:
1452:
1450:
1446:
1440:
1436:
1433:
1429:
1422:
1420:
1416:
1410:
1406:
1403:
1397:
1395:
1391:
1385:
1381:
1378:
1376:RefSeq (mRNA)
1374:
1367:
1366:
1361:
1357:
1354:
1348:
1347:
1342:
1338:
1335:
1333:
1329:
1322:
1321:
1316:
1312:
1309:
1303:
1302:
1297:
1293:
1290:
1288:
1284:
1277:
1276:
1271:
1267:
1264:
1258:
1257:
1252:
1248:
1245:
1243:
1239:
1236:
1233:
1231:
1228:
1224:
1221:
1217:
1213:
1206:
1202:
1197:
1191:
1188:
1186:
1183:
1181:
1178:
1176:
1173:
1171:
1168:
1166:
1163:
1161:
1158:
1156:
1153:
1151:
1148:
1146:
1143:
1141:
1138:
1136:
1133:
1131:
1128:
1126:
1123:
1121:
1118:
1116:
1113:
1111:
1108:
1106:
1103:
1101:
1098:
1096:
1093:
1091:
1088:
1086:
1083:
1081:
1078:
1076:
1073:
1071:
1068:
1066:
1063:
1061:
1058:
1056:
1053:
1051:
1048:
1046:
1043:
1041:
1038:
1036:
1033:
1031:
1028:
1026:
1023:
1021:
1018:
1016:
1013:
1011:
1008:
1006:
1003:
1001:
998:
996:
993:
991:
988:
986:
983:
981:
978:
976:
973:
971:
968:
966:
965:ion transport
963:
961:
958:
956:
953:
951:
948:
946:
943:
941:
938:
936:
933:
931:
928:
926:
923:
921:
918:
916:
913:
911:
908:
906:
903:
901:
898:
896:
893:
891:
888:
886:
883:
881:
878:
876:
873:
871:
868:
866:
863:
861:
858:
857:
855:
852:
851:
845:
844:membrane raft
842:
840:
837:
835:
832:
830:
827:
825:
822:
820:
817:
815:
814:late endosome
812:
810:
807:
805:
802:
800:
797:
795:
792:
790:
787:
785:
782:
780:
777:
775:
772:
770:
767:
765:
762:
760:
757:
755:
752:
750:
747:
745:
742:
740:
737:
735:
732:
731:
729:
726:
725:
719:
716:
714:
711:
709:
706:
704:
701:
699:
696:
694:
691:
689:
686:
684:
681:
679:
676:
674:
671:
669:
666:
664:
661:
659:
656:
655:
653:
650:
649:
646:
645:Gene ontology
642:
638:
626:
621:
618:
616:
612:
604:
599:
588:
584:
580:
576:
572:
568:
564:
560:
556:
552:
551:
548:
544:
539:
536:
526:
522:
518:
514:
510:
506:
502:
499:skin of thigh
498:
494:
490:
489:
486:
482:
477:
474:
473:
470:
468:
464:
462:
461:
457:
456:
453:
451:
447:
443:
439:
435:
427:
422:
418:
414:
409:
399:
395:
388:
381:
375:
368:
360:
356:
352:
347:
343:
338:
334:
326:
321:
317:
313:
308:
298:
294:
287:
280:
274:
267:
263:
257:
253:
249:
244:
240:
235:
231:
227:
223:
219:
215:
211:
207:
203:
199:
195:
191:
183:
178:
171:
166:
161:
150:
148:
144:
140:
136:
132:
128:
124:
120:
116:
112:
108:
104:
100:
96:
92:
88:
84:
80:
76:
70:
65:
62:
61:
57:
54:
47:
43:
38:
34:
30:
25:
20:
5578:
5306:
5156:
4716:ATP synthase
4460:
4394:
4350:
4328:
4313:Small GTPase
3927:Wilson/ATP7B
3922:Menkes/ATP7A
3921:
3767:
3752:
3737:
3722:
3707:
3692:
3677:
3662:
3647:
3632:
3617:
3602:
3587:
3572:
3557:
3498:
3492:
3429:(1): 47–54.
3426:
3422:
3390:(1): 233–8.
3387:
3383:
3342:
3338:
3310:(1): 63–71.
3307:
3303:
3264:
3260:
3219:
3215:
3186:
3182:
3149:
3145:
3112:
3108:
3074:
3070:
3045:(5): 883–9.
3042:
3038:
3001:
2997:
2971:
2967:
2945:(3): 462–9.
2942:
2938:
2903:
2899:
2870:
2866:
2833:
2829:
2799:(5): 333–8.
2796:
2792:
2757:
2724:
2720:
2685:
2681:
2644:
2640:
2613:
2609:
2584:. Retrieved
2580:
2571:
2534:
2530:
2520:
2485:
2481:
2471:
2428:
2424:
2414:
2379:
2375:
2365:
2346:
2314:
2310:
2261:(1): 22–32.
2258:
2254:
2203:(1): 15–29.
2200:
2196:
2139:(1): 18577.
2136:
2132:
2122:
2092:(4): 430–5.
2089:
2085:
2041:
2035:
2026:
2017:
2008:
1999:
1924:
1906:
1892:
1864:
1861:Interactions
1787:
1768:
1756:
1727:
1718:
1706:
1692:
1666:
1655:
1621:
1611:X chromosome
1606:
1604:
1593:gene causes
1590:
1557:
1553:
1549:
1548:
1470:NP_001103227
1467:
1449:NP_001269153
1442:
1415:NM_001109757
1412:
1394:NM_001282224
1387:
1363:
1344:
1318:
1299:
1273:
1254:
1234:
1229:
955:pigmentation
577:vas deferens
465:
458:
424:105,168,532
411:105,070,882
185:External IDs
72:
5663:Na/K-ATPase
5646:Electrolyte
5553:Lactoferrin
5548:Hemosiderin
5521:Hemojuvelin
5419:Transferrin
5168:3.A.3.8.8:
5062:3.A.3.1.2:
5010:3.A.3.1.1:
4637:Mitofusin-1
4612:3.6.5.5-6:
4581:Prokaryotic
3540:PDB gallery
3152:(1): 7–13.
3115:(1): 20–5.
3077:(1): 14–9.
2610:J Biol Chem
1838:endothelial
1760:enterocytes
1622:ATP7A is a
819:microvillus
688:ATP binding
527:skin of hip
323:78,050,395
310:77,910,690
163:Identifiers
5410:Hephaestin
5350:Metabolism
4842:H (V-type)
4738:H (F-type)
4720:TC 3A2-3A3
4603:Eukaryotic
4236:Transducin
4073:(3.6.3.10)
3812:Hydrolases
3146:Nat. Genet
3109:Nat. Genet
3071:Nat. Genet
2998:Nat. Genet
2586:2020-07-06
1994:, May 2017
1973:, May 2017
1950:References
1921:Inhibition
1824:Parenchyma
1779:tyrosinase
1583:tyrosinase
839:perikaryon
469:(ortholog)
206:HomoloGene
5531:Aconitase
5307:see also
5274:type 13:
5092:3.A.3.2:
4708:ion pumps
4571:3.6.5.3:
4311:3.6.5.2:
4253:Gustducin
4185:3.6.5.1:
4019:(3.6.3.9)
3939:(3.6.3.8)
3842:Inorganic
3099:205341350
2482:Biometals
1898:mutations
1800:Function
1684:histidine
1618:Structure
1474:NP_033856
1445:NP_000043
1419:NM_009726
1390:NM_000052
1220:Orthologs
1190:transport
1045:lactation
739:cytoplasm
214:GeneCards
5741:Category
5512:Hepcidin
5499:Ferritin
5469:Ferritin
5459:Integrin
5405:Ferritin
5382:duodenum
5170:flippase
4986:A-ATPase
4969:ATP6V0E1
4959:ATP6V0D2
4954:ATP6V0D1
4939:ATP6V0A4
4934:ATP6V0A2
4929:ATP6V0A1
4919:ATP6V1G3
4914:ATP6V1G2
4909:ATP6V1G1
4899:ATP6V1E2
4894:ATP6V1E1
4884:ATP6V1C2
4879:ATP6V1C1
4874:ATP6V1B2
4869:ATP6V1B1
3847:Thiamine
3486:GeneCard
3174:24883244
3026:12122103
2968:Genomics
2939:Genomics
2930:17562324
2887:17531189
2858:23109512
2850:12539963
2821:21471699
2813:12539960
2784:10079814
2749:23109512
2741:12539963
2712:10739752
2669:40168524
2661:15269005
2632:15634671
2563:22869751
2512:24748564
2463:41967295
2455:20333435
2446:11115773
2406:25242165
2285:18534184
2227:21221114
2171:31819097
2114:19509148
2106:10453200
2068:10079817
1990:–
1969:–
1929:See also
1797:Location
1753:Function
1709:cysteine
1707:The two
1522:Wikidata
1199:Sources:
769:membrane
5632:SLC39A4
5627:SLC30A1
5594:SLC31A1
5296:ATP13A5
5291:ATP13A4
5286:ATP13A3
5281:ATP13A2
5276:ATP13A1
5004:(3.A.3)
4964:ATP6V0E
4949:ATP6V0C
4944:ATP6V0B
4924:ATP6V1H
4904:ATP6V1F
4889:ATP6V1D
4864:ATP6V1A
4859:ATP6AP2
4854:ATP6AP1
4712:ATPases
4658:Tubulin
4627:Dynamin
4479:other:
4159:Katanin
4149:Kinesin
4124:ATP13A3
4119:ATP13A2
3854:Apyrase
3443:9437429
3414:9246006
3405:1715861
3371:9147644
3362:7185191
3326:8981948
3317:1712537
3291:8947031
3248:8943055
3203:8923001
3166:8490659
3137:9148871
3129:8490647
3091:8490646
3061:7977350
3052:1918324
3018:7842019
2988:7607665
2959:7490081
2921:2025638
2703:1288188
2554:3427069
2503:4113679
2397:4179477
2276:2556376
2218:4214867
2162:6901466
2141:Bibcode
1992:Ensembl
1971:Ensembl
1828:In the
1332:UniProt
1287:Ensembl
1226:Species
1205:QuickGO
809:nucleus
759:cytosol
444:pattern
170:Aliases
5270:ATP11C
5265:ATP11B
5260:ATP11A
5254:ATP10D
5249:ATP10B
5244:ATP10A
5227:ATP8B4
5222:ATP8B3
5217:ATP8B2
5212:ATP8B1
5207:ATP8A1
5174:ATP8A2
5149:ATP2C1
5144:ATP2B4
5139:ATP2B3
5134:ATP2B2
5129:ATP2B1
5124:ATP2A3
5119:ATP2A2
5114:ATP2A1
5086:ATP12A
5056:ATP1G1
5051:ATP1B4
5046:ATP1B3
5041:ATP1B2
5036:ATP1B1
5031:ATP1A4
5026:ATP1A3
5021:ATP1A2
5016:ATP1A1
4976:TCIRG1
4822:ATP5L2
4812:ATP5J2
4792:ATP5G3
4787:ATP5G2
4782:ATP5G1
4777:ATP5F1
4762:ATP5C2
4757:ATP5C1
4747:ATP5A1
4535:ARL13B
4395:RhoBTB
4289:α12/13
4177:GTPase
4154:Myosin
4144:Dynein
4114:ATP12A
4109:ATP11B
4104:ATP10A
4099:ATP8B1
4089:Other
4061:ATP1B4
4056:ATP1B3
4051:ATP1B2
4046:ATP1B1
4041:ATP1A4
4036:ATP1A3
4031:ATP1A2
4026:ATP1A1
4017:Na+/K+
4005:ATP2C2
4000:ATP2C1
3988:ATP2B4
3983:ATP2B3
3978:ATP2B2
3973:ATP2B1
3961:ATP2A3
3956:ATP2A2
3951:ATP2A1
3900:ATPase
3490:Human
3472:(MeSH)
3451:172550
3449:
3441:
3412:
3402:
3369:
3359:
3324:
3314:
3289:
3282:452430
3279:
3261:EMBO J
3246:
3236:
3201:
3172:
3164:
3135:
3127:
3097:
3089:
3059:
3049:
3024:
3016:
2986:
2957:
2928:
2918:
2885:
2856:
2848:
2819:
2811:
2782:
2772:
2747:
2739:
2710:
2700:
2667:
2659:
2630:
2561:
2551:
2510:
2500:
2461:
2453:
2443:
2404:
2394:
2353:
2283:
2273:
2225:
2215:
2169:
2159:
2112:
2104:
2066:
2056:
1805:Kidney
1794:Tissue
1781:, and
1634:Eight
1585:, and
1508:search
1506:PubMed
1365:Q64430
1346:Q04656
1242:Entrez
615:BioGPS
302:Xq21.1
194:300011
5599:ATOX1
5584:ATP7B
5579:ATP7A
5482:Other
5238:ATP9B
5233:ATP9A
5162:ATP7B
5157:ATP7A
5098:SERCA
5078:ATP4B
5073:ATP4A
4832:ATP5S
4827:ATP5O
4817:ATP5L
4807:ATP5J
4802:ATP5I
4797:ATP5H
4772:ATP5E
4767:ATP5D
4752:ATP5B
4591:EF-Tu
4530:SAR1B
4513:RAB27
4508:RAB23
4461:RhoDF
4351:RhoUV
4334:CDC42
4329:Cdc42
4315:>
4300:GNA13
4295:GNA12
4280:GNA11
4269:αq/11
4258:GNAT3
4246:GNAT2
4241:GNAT1
4231:GNAI3
4226:GNAI2
4221:GNAI1
4173:3.6.5
4137:3.6.4
4080:ATP4A
4071:H+/K+
3946:SERCA
3908:3.6.3
3892:3.6.3
3869:3.6.2
3829:3.6.1
3499:ATP7A
3493:ATP7A
3447:S2CID
3239:19489
3170:S2CID
3133:S2CID
3095:S2CID
3022:S2CID
2854:S2CID
2817:S2CID
2745:S2CID
2665:S2CID
2459:S2CID
2110:S2CID
1944:ATOX1
1935:ATP7B
1910:prion
1867:ATOX1
1840:cells
1628:ATP7B
1607:ATP7A
1591:ATP7A
1550:ATP7A
1275:11977
1235:Mouse
1230:Human
1201:Amigo
511:tibia
467:Mouse
460:Human
407:Start
342:Mouse
306:Start
239:Human
218:ATP7A
202:99400
177:ATP7A
22:ATP7A
5622:TMC8
5617:TMC6
5516:HAMP
5433:TFR2
5428:TFR1
5201:ATP3
5186:Na/K
5108:) /
5106:SPCA
5102:PMCA
4651:OPA1
4644:and
4596:EF-G
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