Copper-transporting ATPase 1

Details

Name
Copper-transporting ATPase 1
Synonyms
  • 7.2.2.8
  • Copper pump 1
  • MC1
  • Menkes disease-associated protein
  • MNK
Gene Name
ATP7A
UniProtKB Entry
Q04656Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0057030|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
GTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLVGIPIAAGVFMPI
GLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYESYELPARSQIGQKSPSEISVHVGI
DDTSRNSPKLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL
Number of residues
1500
Molecular Weight
163371.335
Theoretical pI
6.18
GO Classification
Functions
ATP hydrolysis activity / cuprous ion binding / P-type divalent copper transporter activity / P-type monovalent copper transporter activity / protein-folding chaperone binding / small GTPase binding
Processes
cellular response to amino acid stimulus / cellular response to antibiotic / cellular response to cadmium ion / cellular response to cobalt ion / cellular response to copper ion / cellular response to hypoxia / cellular response to iron ion / cellular response to lead ion / cellular response to platelet-derived growth factor stimulus / copper ion homeostasis / female pregnancy / intracellular copper ion homeostasis / liver development / negative regulation of iron ion transmembrane transport / positive regulation of cell size / positive regulation of epithelial cell proliferation / positive regulation of lamellipodium assembly / positive regulation of melanin biosynthetic process / positive regulation of response to wounding / positive regulation of tyrosinase activity / positive regulation of vascular associated smooth muscle cell migration / response to manganese ion
Components
apical plasma membrane / axon / cell leading edge / dendrite / early endosome membrane / melanosome membrane / microvillus / perikaryon / phagocytic vesicle membrane / postsynaptic density / trans-Golgi network membrane
General Function
ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity)
Specific Function
ATP binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
654-675 715-734 742-762 782-802 937-959 990-1011 1357-1374 1386-1405
Cellular Location
Golgi apparatus, trans-Golgi network membrane
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
Xq21.1
External Identifiers
ResourceLink
UniProtKB IDQ04656
UniProtKB Entry NameATP7A_HUMAN
GenBank Protein ID179253
GenBank Gene IDL06133
GeneCard IDATP7A
HGNC IDHGNC:869
PDB ID(s)1AW0, 1KVI, 1KVJ, 1Q8L, 1S6O, 1S6U, 1Y3J, 1Y3K, 1YJR, 1YJT, 1YJU, 1YJV, 2AW0, 2G9O, 2GA7, 2K1R, 2KIJ, 2KMV, 2KMX, 3CJK, 5T7L, 7LU8
KEGG IDhsa:538
NCBI Gene ID538
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. 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]
  24. 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]
  25. 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]
  26. 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]
  27. 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]
  28. 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]
  29. 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]
  30. 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]
  31. 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]

Associated Data

Bio-Entities
Bio-EntityType
Copper-transporting ATPase 1 (Humans)protein
primary
Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
CisplatinapprovedunknowntransportersubstrateDetails
CarboplatinapprovedunknowntransportersubstrateDetails
Oxaliplatinapproved, investigationalnotransportersubstrateDetails
Copperapproved, investigationalnotransportersubstrateDetails