Copper-transporting ATPase 1
Details
- Name
- Copper-transporting ATPase 1
- Synonyms
- 3.6.3.54
- Copper pump 1
- MC1
- Menkes disease-associated protein
- MNK
- Gene Name
- ATP7A
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0007046|Copper-transporting ATPase 1 MDPSMGVNSVTISVEGMTCNSCVWTIEQQIGKVNGVHHIKVSLEEKNATIIYDPKLQTPK TLQEAIDDMGFDAVIHNPDPLPVLTDTLFLTVTASLTLPWDHIQSTLLKTKGVTDIKIYP QKRTVAVTIIPSIVNANQIKELVPELSLDTGTLEKKSGACEDHSMAQAGEVVLKMKVEGM TCHSCTSTIEGKIGKLQGVQRIKVSLDNQEATIVYQPHLISVEEMKKQIEAMGFPAFVKK QPKYLKLGAIDVERLKNTPVKSSEGSQQRSPSYTNDSTATFIIDGMHCKSCVSNIESTLS ALQYVSSIVVSLENRSAIVKYNASSVTPESLRKAIEAVSPGLYRVSITSEVESTSNSPSS SSLQKIPLNVVSQPLTQETVINIDGMTCNSCVQSIEGVISKKPGVKSIRVSLANSNGTVE YDPLLTSPETLRGAIEDMGFDATLSDTNEPLVVIAQPSSEMPLLTSTNEFYTKGMTPVQD KEEGKNSSKCYIQVTGMTCASCVANIERNLRREEGIYSILVALMAGKAEVRYNPAVIQPP MIAEFIRELGFGATVIENADEGDGVLELVVRGMTCASCVHKIESSLTKHRGILYCSVALA TNKAHIKYDPEIIGPRDIIHTIESLGFEASLVKKDRSASHLDHKREIRQWRRSFLVSLFF CIPVMGLMIYMMVMDHHFATLHHNQNMSKEEMINLHSSMFLERQILPGLSVMNLLSFLLC VPVQFFGGWYFYIQAYKALKHKTANMDVLIVLATTIAFAYSLIILLVAMYERAKVNPITF FDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLDSDNILLSEEQVDVE LVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSL LICATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVFVSIATLLVWIVIG FLNFEIVETYFPGYNRSISRTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGA QNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLTESNRISHHKILAIVGTA ESNSEHPLGTAITKYCKQELDTETLGTCIDFQVVPGCGISCKVTNIEGLLHKNNWNIEDN NIKNASLVQIDASNEQSSTSSSMIIDAQISNALNAQQYKVLIGNREWMIRNGLVINNDVN DFMTEHERKGRTAVLVAVDDELCGLIAIADTVKPEAELAIHILKSMGLEVVLMTGDNSKT ARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMANVGIAIGT GTDVAIEAADVVLIRNDLLDVVASIDLSRETVKRIRINFVFALIYNLVGIPIAAGVFMPI GLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYESYELPARSQIGQKSPSEISVHVGI DDTSRNSPKLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL
- Number of residues
- 1500
- Molecular Weight
- 163372.275
- Theoretical pI
- 6.18
- GO Classification
- FunctionsATP binding / copper ion binding / copper ion transmembrane transporter activity / copper-dependent protein binding / copper-exporting ATPase activity / superoxide dismutase copper chaperone activityProcessesATP metabolic process / blood vessel development / blood vessel remodeling / cartilage development / catecholamine metabolic process / cellular copper ion homeostasis / central nervous system neuron development / cerebellar Purkinje cell differentiation / collagen fibril organization / copper ion export / copper ion import / copper ion transport / dendrite morphogenesis / detoxification of copper ion / dopamine metabolic process / elastic fiber assembly / elastin biosynthetic process / epinephrine metabolic process / extracellular matrix organization / hair follicle morphogenesis / in utero embryonic development / ion transmembrane transport / lactation / locomotory behavior / lung alveolus development / mitochondrion organization / negative regulation of metalloenzyme activity / negative regulation of neuron apoptotic process / neuron projection morphogenesis / norepinephrine biosynthetic process / norepinephrine metabolic process / peptidyl-lysine modification / pigmentation / plasma membrane copper ion transport / positive regulation of catalytic activity / positive regulation of metalloenzyme activity / positive regulation of oxidoreductase activity / pyramidal neuron development / regulation of gene expression / regulation of oxidative phosphorylation / release of cytochrome c from mitochondria / removal of superoxide radicals / response to iron(III) ion / response to reactive oxygen species / response to zinc ion / serotonin metabolic process / skin development / T-helper cell differentiation / transmembrane transport / tryptophan metabolic process / tyrosine metabolic processComponentsbasolateral plasma membrane / brush border membrane / cytosol / endoplasmic reticulum / Golgi apparatus / integral component of plasma membrane / late endosome / membrane / neuron projection / neuronal cell body / perinuclear region of cytoplasm / plasma membrane / secretory granule / trans-Golgi network / trans-Golgi network transport vesicle
- General Function
- Superoxide dismutase copper chaperone activity
- Specific 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.
- Pfam Domain Function
- Transmembrane Regions
- 654-675 715-734 742-762 782-802 937-959 990-1011 1357-1374 1386-1405
- Cellular Location
- Golgi apparatus
- Gene sequence
>lcl|BSEQ0021693|Copper-transporting ATPase 1 (ATP7A) ATGGATCCAAGTATGGGTGTGAATTCTGTTACCATTTCTGTTGAGGGTATGACTTGCAAT TCCTGTGTTTGGACCATTGAGCAGCAGATTGGAAAAGTGAATGGTGTGCATCACATTAAG GTATCACTGGAAGAAAAAAATGCAACTATTATTTATGACCCTAAACTACAGACTCCAAAG ACCCTACAGGAAGCTATTGATGACATGGGCTTTGATGCTGTTATCCATAATCCTGACCCT CTCCCTGTTTTAACTGACACCTTGTTTCTGACTGTTACGGCGTCACTGACTTTGCCATGG GACCATATCCAAAGCACATTGCTGAAGACCAAGGGTGTGACAGACATTAAAATTTACCCT CAGAAAAGAACTGTAGCAGTGACAATAATCCCTTCTATAGTGAATGCCAATCAGATAAAA GAGCTGGTTCCAGAACTCAGTTTAGATACTGGGACACTGGAGAAAAAGTCAGGAGCTTGT GAAGATCATAGTATGGCTCAAGCTGGTGAAGTCGTGCTGAAGATGAAAGTGGAAGGGATG ACCTGCCATTCATGTACTAGCACTATTGAAGGAAAAATTGGGAAACTGCAAGGTGTTCAG CGAATTAAAGTCTCCCTGGACAATCAAGAAGCTACTATTGTTTATCAACCTCATCTTATC TCAGTAGAGGAAATGAAAAAGCAGATTGAAGCTATGGGCTTTCCAGCATTTGTCAAAAAG CAGCCCAAGTACCTCAAATTGGGAGCTATTGATGTAGAACGTCTAAAGAACACACCAGTT AAATCCTCAGAAGGGTCACAGCAAAGGAGTCCATCATATACCAATGATTCAACAGCCACT TTCATCATTGATGGCATGCATTGTAAATCATGTGTGTCAAATATTGAAAGTACTTTATCT GCACTCCAATATGTAAGCAGCATAGTAGTTTCTTTAGAGAATAGGTCTGCCATTGTGAAG TATAATGCAAGCTCAGTCACTCCAGAATCCCTGAGAAAAGCAATAGAGGCTGTATCACCG GGGCTATATAGAGTTAGTATCACAAGTGAAGTTGAGAGTACCTCAAACTCTCCCTCCAGC TCATCTCTTCAGAAGATTCCTTTGAATGTAGTTAGCCAGCCTCTGACACAAGAAACTGTG ATAAACATTGATGGCATGACTTGTAATTCCTGTGTGCAGTCTATTGAGGGTGTCATATCA AAAAAGCCAGGTGTAAAATCCATACGAGTCTCCCTTGCAAATAGCAATGGGACTGTTGAG TATGATCCTCTACTAACCTCTCCAGAAACGTTGAGAGGAGCAATAGAAGACATGGGATTT GATGCTACCTTGTCAGACACGAATGAGCCGTTGGTAGTAATAGCTCAGCCTTCATCGGAA ATGCCGCTTTTGACTTCAACTAATGAATTTTATACTAAAGGGATGACACCAGTTCAAGAC AAGGAGGAAGGAAAGAATTCATCTAAGTGTTACATACAGGTCACTGGCATGACTTGCGCT TCCTGTGTAGCAAACATTGAACGGAATTTAAGGCGGGAAGAAGGAATATATTCTATACTT GTGGCCCTGATGGCTGGCAAGGCAGAAGTAAGGTATAATCCTGCTGTTATACAACCCCCA ATGATAGCAGAGTTCATCCGAGAACTTGGATTTGGAGCCACTGTGATAGAAAATGCTGAT GAAGGAGATGGTGTTTTGGAACTTGTTGTGAGGGGAATGACGTGTGCCTCCTGCGTACAT AAAATAGAGTCTAGTCTCACAAAACACAGAGGGATCCTATACTGCTCCGTGGCCCTGGCA ACCAACAAAGCACATATTAAATATGACCCAGAAATTATTGGTCCTAGAGATATTATCCAT ACAATTGAAAGCTTAGGTTTTGAAGCTTCTTTGGTCAAGAAGGATCGGTCAGCAAGTCAC TTAGATCATAAACGAGAAATAAGACAATGGAGACGGTCTTTTCTTGTGAGTCTGTTTTTC TGTATTCCTGTAATGGGGCTGATGATATATATGATGGTTATGGACCACCACTTTGCAACT CTTCACCATAATCAAAACATGAGTAAAGAAGAAATGATCAACCTTCATTCTTCTATGTTC CTGGAGCGCCAGATTCTTCCAGGATTGTCTGTTATGAATTTGCTGTCCTTTTTATTGTGT GTACCTGTACAGTTTTTCGGAGGCTGGTACTTCTACATTCAGGCTTATAAAGCACTGAAG CATAAGACAGCAAATATGGACGTACTGATTGTGCTGGCAACCACCATTGCATTTGCCTAC TCTTTGATTATTCTTCTAGTTGCAATGTATGAGAGAGCCAAAGTGAACCCTATTACTTTC TTTGACACACCCCCTATGCTGTTTGTGTTTATTGCACTAGGCCGATGGCTGGAACATATA GCAAAGGGCAAAACATCAGAGGCTCTTGCAAAGTTAATTTCACTACAAGCTACAGAAGCA ACTATTGTAACTCTTGATTCTGATAATATCCTCCTCAGTGAAGAACAAGTGGATGTGGAA CTTGTACAACGTGGAGATATCATTAAAGTAGTTCCAGGAGGCAAATTTCCAGTGGATGGT CGTGTTATTGAAGGACATTCTATGGTAGATGAGTCCCTCATCACAGGGGAGGCAATGCCT GTGGCTAAGAAACCTGGCAGCACAGTGATTGCTGGTTCCATTAACCAGAACGGGTCACTG CTTATCTGCGCAACACATGTTGGAGCAGACACAACCCTTTCTCAAATTGTCAAACTTGTG GAAGAGGCACAAACATCAAAGGCTCCTATCCAGCAGTTTGCAGACAAACTCAGTGGCTAT TTTGTTCCTTTTATTGTTTTTGTTTCCATTGCCACCCTCTTGGTATGGATTGTAATTGGA TTTCTGAATTTTGAAATTGTGGAAACCTACTTTCCTGGCTACAATAGAAGTATCTCCCGA ACAGAAACGATAATACGATTTGCTTTCCAAGCCTCTATCACAGTTCTGTGTATTGCATGT CCCTGTTCACTGGGACTGGCCACTCCAACTGCTGTGATGGTGGGTACAGGAGTAGGTGCT CAAAATGGCATACTAATAAAAGGTGGAGAGCCATTGGAGATGGCTCATAAGGTAAAGGTA GTGGTATTTGATAAGACTGGAACCATTACTCACGGAACCCCAGTGGTGAATCAAGTAAAG GTTCTAACTGAAAGTAACAGAATATCACACCATAAAATCTTGGCCATTGTGGGAACTGCT GAAAGTAACAGTGAACACCCTCTAGGAACAGCCATAACCAAATATTGCAAACAGGAGCTG GACACTGAAACCTTGGGTACCTGCATAGATTTCCAGGTTGTGCCAGGCTGTGGTATTAGC TGTAAAGTCACCAATATTGAAGGCTTGCTACATAAGAATAACTGGAATATAGAGGACAAT AATATTAAAAATGCATCCCTGGTTCAAATTGATGCCAGTAATGAACAGTCATCAACTTCG TCTTCCATGATTATTGATGCCCAGATCTCAAATGCTCTTAATGCTCAGCAGTATAAAGTC CTCATTGGTAACCGGGAGTGGATGATTAGAAATGGTCTTGTCATTAATAACGATGTAAAT GATTTCATGACTGAACATGAGAGAAAAGGTCGGACTGCTGTATTAGTAGCAGTTGATGAT GAGCTGTGTGGCTTGATAGCCATTGCAGACACAGTGAAGCCTGAAGCAGAACTGGCTATC CATATTCTGAAATCTATGGGCTTAGAAGTAGTTCTGATGACTGGAGACAACAGTAAAACA GCTAGATCTATTGCTTCTCAGGTTGGCATTACTAAGGTGTTTGCTGAAGTTCTACCTTCT CACAAGGTTGCTAAAGTGAAGCAACTTCAAGAGGAGGGGAAACGGGTAGCAATGGTGGGA GATGGAATCAATGACTCCCCAGCTCTGGCAATGGCTAATGTGGGAATTGCTATTGGCACA GGCACAGATGTAGCCATTGAAGCAGCTGATGTGGTTTTGATAAGGAATGATCTTCTGGAT GTAGTGGCAAGTATTGACTTATCAAGAAAGACAGTCAAGAGGATTCGGATAAATTTTGTC TTTGCTCTAATTTATAATCTGGTTGGAATTCCCATAGCTGCTGGAGTTTTTATGCCCATT GGTTTGGTTTTGCAGCCCTGGATGGGATCTGCAGCAATGGCTGCTTCATCTGTTTCTGTA GTACTTTCTTCTCTCTTCCTTAAACTTTACAGGAAACCAACTTACGAGAGTTATGAACTG CCTGCCCGGAGCCAGATAGGACAGAAGAGTCCTTCAGAAATCAGCGTTCATGTTGGAATA GATGATACCTCAAGGAATTCTCCTAAACTGGGTTTGCTGGACCGGATTGTTAATTATAGC AGAGCCTCTATAAACTCACTACTGTCTGATAAACGCTCCCTAAACAGTGTTGTTACCAGT GAACCTGACAAGCACTCACTCCTGGTGGGAGACTTCAGGGAAGATGATGACACTGCATTA TAA
- Chromosome Location
- X
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q04656 UniProtKB Entry Name ATP7A_HUMAN GenBank Protein ID 179253 GenBank Gene ID L06133 HGNC ID HGNC:869 - General References
- Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J: Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat Genet. 1993 Jan;3(1):7-13. [Article]
- Tumer Z, Vural B, Tonnesen T, Chelly J, Monaco AP, Horn N: Characterization of the exon structure of the Menkes disease gene using vectorette PCR. Genomics. 1995 Apr 10;26(3):437-42. [Article]
- Reddy MC, Harris ED: Multiple transcripts coding for the menkes gene: evidence for alternative splicing of Menkes mRNA. Biochem J. 1998 Aug 15;334 ( Pt 1):71-7. [Article]
- Harris ED, Reddy MC, Qian Y, Tiffany-Castiglioni E, Majumdar S, Nelson J: Multiple forms of the Menkes Cu-ATPase. Adv Exp Med Biol. 1999;448:39-51. [Article]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, 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 KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [Article]
- Dierick HA, Ambrosini L, Spencer J, Glover TW, Mercer JF: Molecular structure of the Menkes disease gene (ATP7A). Genomics. 1995 Aug 10;28(3):462-9. [Article]
- Chelly J, Tumer Z, Tonnesen T, Petterson A, Ishikawa-Brush Y, Tommerup N, Horn N, Monaco AP: Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein. Nat Genet. 1993 Jan;3(1):14-9. [Article]
- Mercer JF, Livingston J, Hall B, Paynter JA, Begy C, Chandrasekharappa S, Lockhart P, Grimes A, Bhave M, Siemieniak D, et al.: Isolation of a partial candidate gene for Menkes disease by positional cloning. Nat Genet. 1993 Jan;3(1):20-5. [Article]
- Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [Article]
- Qi M, Byers PH: Constitutive skipping of alternatively spliced exon 10 in the ATP7A gene abolishes Golgi localization of the menkes protein and produces the occipital horn syndrome. Hum Mol Genet. 1998 Mar;7(3):465-9. [Article]
- Reddy MC, Majumdar S, Harris ED: Evidence for a Menkes-like protein with a nuclear targeting sequence. Biochem J. 2000 Sep 15;350 Pt 3:855-63. [Article]
- Dierick HA, Adam AN, Escara-Wilke JF, Glover TW: Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network. Hum Mol Genet. 1997 Mar;6(3):409-16. [Article]
- Petris MJ, Mercer JF: 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. Hum Mol Genet. 1999 Oct;8(11):2107-15. [Article]
- Stephenson SE, Dubach D, Lim CM, Mercer JF, La Fontaine S: A single PDZ domain protein interacts with the Menkes copper ATPase, ATP7A. A new protein implicated in copper homeostasis. J Biol Chem. 2005 Sep 30;280(39):33270-9. Epub 2005 Jul 28. [Article]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
- Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ: Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat Struct Biol. 1998 Jan;5(1):47-54. [Article]
- Tumer Z, Moller LB, Horn N: Mutation spectrum of ATP7A, the gene defective in Menkes disease. Adv Exp Med Biol. 1999;448:83-95. [Article]
- Das S, Levinson B, Whitney S, Vulpe C, Packman S, Gitschier J: Diverse mutations in patients with Menkes disease often lead to exon skipping. Am J Hum Genet. 1994 Nov;55(5):883-9. [Article]
- Tumer Z, Lund C, Tolshave J, Vural B, Tonnesen T, Horn N: Identification of point mutations in 41 unrelated patients affected with Menkes disease. Am J Hum Genet. 1997 Jan;60(1):63-71. [Article]
- Ronce N, Moizard MP, Robb L, Toutain A, Villard L, Moraine C: A C2055T transition in exon 8 of the ATP7A gene is associated with exon skipping in an occipital horn syndrome family. Am J Hum Genet. 1997 Jul;61(1):233-8. [Article]
- Ambrosini L, Mercer JF: Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease. Hum Mol Genet. 1999 Aug;8(8):1547-55. [Article]
- Ogawa A, Yamamoto S, Takayanagi M, Kogo T, Kanazawa M, Kohno Y: Identification of three novel mutations in the MNK gene in three unrelated Japanese patients with classical Menkes disease. J Hum Genet. 1999;44(3):206-9. [Article]
- Dagenais SL, Adam AN, Innis JW, Glover TW: A novel frameshift mutation in exon 23 of ATP7A (MNK) results in occipital horn syndrome and not in Menkes disease. Am J Hum Genet. 2001 Aug;69(2):420-7. Epub 2001 Jun 26. [Article]
- Gu YH, Kodama H, Murata Y, Mochizuki D, Yanagawa Y, Ushijima H, Shiba T, Lee CC: ATP7A gene mutations in 16 patients with Menkes disease and a patient with occipital horn syndrome. Am J Med Genet. 2001 Mar 15;99(3):217-22. [Article]
- Hahn S, Cho K, Ryu K, Kim J, Pai K, Kim M, Park H, Yoo O: Identification of four novel mutations in classical Menkes disease and successful prenatal DNA diagnosis. Mol Genet Metab. 2001 May;73(1):86-90. [Article]
- Moller LB, Bukrinsky JT, Molgaard A, Paulsen M, Lund C, Tumer Z, Larsen S, Horn N: Identification and analysis of 21 novel disease-causing amino acid substitutions in the conserved part of ATP7A. Hum Mutat. 2005 Aug;26(2):84-93. [Article]
- Tang J, Robertson S, Lem KE, Godwin SC, Kaler SG: Functional copper transport explains neurologic sparing in occipital horn syndrome. Genet Med. 2006 Nov;8(11):711-8. [Article]
- Kennerson ML, Nicholson GA, Kaler SG, Kowalski B, Mercer JF, Tang J, Llanos RM, Chu S, Takata RI, Speck-Martins CE, Baets J, Almeida-Souza L, Fischer D, Timmerman V, Taylor PE, Scherer SS, Ferguson TA, Bird TD, De Jonghe P, Feely SM, Shy ME, Garbern JY: Missense mutations in the copper transporter gene ATP7A cause X-linked distal hereditary motor neuropathy. Am J Hum Genet. 2010 Mar 12;86(3):343-52. doi: 10.1016/j.ajhg.2010.01.027. Epub 2010 Feb 18. [Article]
- Leon-Garcia G, Santana A, Villegas-Sepulveda N, Perez-Gonzalez C, Henrriquez-Esquiroz JM, de Leon-Garcia C, Wong C, Baeza I: The T1048I mutation in ATP7A gene causes an unusual Menkes disease presentation. BMC Pediatr. 2012 Sep 19;12:150. doi: 10.1186/1471-2431-12-150. [Article]