Copper-transporting ATPase 1

NameCopper-transporting ATPase 1
Synonyms3.6.3.54 Copper pump 1 MC1 Menkes disease-associated protein MNK
Gene NameATP7A
OrganismHuman
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 residues1500
Molecular Weight163372.275
Theoretical pI6.18
GO Classification
Functions
    copper ion binding
copper ion transmembrane transporter activity
copper-dependent protein binding
superoxide dismutase copper chaperone activity
copper-exporting ATPase activity
ATP binding
Processes
    norepinephrine biosynthetic process
norepinephrine metabolic process
regulation of gene expression
negative regulation of neuron apoptotic process
serotonin metabolic process
central nervous system neuron development
positive regulation of oxidoreductase activity
positive regulation of catalytic activity
dendrite morphogenesis
response to iron(III) ion
ATP metabolic process
positive regulation of metalloenzyme activity
dopamine metabolic process
removal of superoxide radicals
blood vessel remodeling
negative regulation of metalloenzyme activity
transmembrane transport
detoxification of copper ion
locomotory behavior
cellular copper ion homeostasis
peptidyl-lysine modification
cartilage development
elastin biosynthetic process
release of cytochrome c from mitochondria
copper ion export
lactation
cerebellar Purkinje cell differentiation
epinephrine metabolic process
blood vessel development
neuron projection morphogenesis
copper ion import
copper ion transport
skin development
plasma membrane copper ion transport
collagen fibril organization
pyramidal neuron development
elastic fiber assembly
lung alveolus development
tyrosine metabolic process
regulation of oxidative phosphorylation
extracellular matrix organization
mitochondrion organization
catecholamine metabolic process
hair follicle morphogenesis
pigmentation
ion transmembrane transport
tryptophan metabolic process
in utero embryonic development
response to reactive oxygen species
T-helper cell differentiation
response to zinc ion
Components
    cytosol
perinuclear region of cytoplasm
endoplasmic reticulum
late endosome
plasma membrane
integral component of plasma membrane
trans-Golgi network transport vesicle
secretory granule
neuron projection
brush border membrane
trans-Golgi network
Golgi apparatus
membrane
neuronal cell body
basolateral plasma membrane
General FunctionSuperoxide dismutase copper chaperone activity
Specific FunctionMay 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.
Transmembrane Regions654-675 715-734 742-762 782-802 937-959 990-1011 1357-1374 1386-1405
GenBank Protein ID179253
UniProtKB IDQ04656
UniProtKB Entry NameATP7A_HUMAN
Cellular LocationGolgi 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
GenBank Gene IDL06133
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:869
Chromosome LocationX
LocusNone
References
  1. 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.[15981243 ]
  2. 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.[17108763 ]
  3. 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.[8490659 ]
  4. 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.[7607665 ]
  5. 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.[9693104 ]
  6. 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.[10079814 ]
  7. 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.[15772651 ]
  8. 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.[7490081 ]
  9. 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.[8490646 ]
  10. 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.[8490647 ]
  11. 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.[11214319 ]
  12. 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.[9467005 ]
  13. 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.[10970802 ]
  14. 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.[9147644 ]
  15. 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.[10484781 ]
  16. 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.[16051599 ]
  17. 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.[19690332 ]
  18. 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.[20068231 ]
  19. 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.[24275569 ]
  20. 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.[9437429 ]
  21. Tumer Z, Moller LB, Horn N: Mutation spectrum of ATP7A, the gene defective in Menkes disease. Adv Exp Med Biol. 1999;448:83-95.[10079817 ]
  22. 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.[7977350 ]
  23. 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.[8981948 ]
  24. 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.[9246006 ]
  25. 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.[10401004 ]
  26. 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.[10319589 ]
  27. 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.[11431706 ]
  28. 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.[11241493 ]
  29. 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.[11350187 ]
  30. 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.[22992316 ]
  31. 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.[20170900 ]

Related FRC

FRCD ID Name Exact Mass Structure




F04874



Aflatoxin B1


312.277




F03371



Copper


63.546