Target Gene Table
VIS IDVirusEnsembl IDGene TypeTarget GeneOncogeneTumor Suppressor GeneNCBI IDUniprot ID
TVIS30083502HIVENSG00000171867.18protein_codingPRNPNoNo5621F7VJQ1
P04156
Q53YK7
TVIS30052962HIVENSG00000171867.18protein_codingPRNPNoNo5621F7VJQ1
P04156
Q53YK7
TVIS30052963HIVENSG00000171867.18protein_codingPRNPNoNo5621F7VJQ1
P04156
Q53YK7
TCGA Plot Options
Drug Information
GenePRNP
DrugBank IDDB09130
Drug NameCopper
Target IDBE0008989
UniProt IDF7VJQ1
Regulation Type
PubMed IDs16824036; 16831968; 16990274; 17257012; 19236027; 19697239; 22791135
CitationsWells MA, Jackson GS, Jones S, Hosszu LL, Craven CJ, Clarke AR, Collinge J, Waltho JP: A reassessment of copper(II) binding in the full-length prion protein. Biochem J. 2006 Nov 1;399(3):435-44.@@Merle U, Stremmel W, Gessner R: Influence of homozygosity for methionine at codon 129 of the human prion gene on the onset of neurological and hepatic symptoms in Wilson disease. Arch Neurol. 2006 Jul;63(7):982-5.@@Shiraishi N, Utsunomiya H, Nishikimi M: Combination of NADPH and copper ions generates proteinase K-resistant aggregates from recombinant prion protein. J Biol Chem. 2006 Nov 17;281(46):34880-7. Epub 2006 Sep 21.@@Shearer J, Soh P: The copper(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox-active at physiological pH. Inorg Chem. 2007 Feb 5;46(3):710-9.@@Valensin G, Molteni E, Valensin D, Taraszkiewicz M, Kozlowski H: Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein. J Phys Chem B. 2009 Mar 19;113(11):3277-9. doi: 10.1021/jp901030a.@@Pushie MJ, Vogel HJ: A potential mechanism for Cu2+ reduction, beta-cleavage, and beta-sheet initiation within the N-terminal domain of the prion protein: insights from density functional theory and molecular dynamics calculations. J Toxicol Environ Health A. 2009;72(17-18):1040-59. doi: 10.1080/15287390903084389.@@Remelli M, Valensin D, Toso L, Gralka E, Guerrini R, Marzola E, Kozlowski H: Thermodynamic and spectroscopic investigation on the role of Met residues in Cu(II) binding to the non-octarepeat site of the human prion protein. Metallomics. 2012 Aug;4(8):794-806. doi: 10.1039/c2mt20060k. Epub 2012 Jul 13.
GroupsApproved; Investigational
Direct ClassificationHomogeneous transition metal compounds
SMILES[Cu]
Pathways
PharmGKBPA449114
ChEMBL