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
Functions
ATP binding / copper ion binding / copper ion transmembrane transporter activity / copper-dependent protein binding / copper-exporting ATPase activity / superoxide dismutase copper chaperone activity
Processes
ATP 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 process
Components
basolateral 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
ResourceLink
UniProtKB IDQ04656
UniProtKB Entry NameATP7A_HUMAN
GenBank Protein ID179253
GenBank Gene IDL06133
HGNC IDHGNC:869
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]
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  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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00515CisplatinapprovedunknownsubstrateDetails
DB00958CarboplatinapprovedunknownsubstrateDetails
DB00526Oxaliplatinapproved, investigationalunknownsubstrateDetails
DB09130Copperapproved, investigationalnosubstrateDetails