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Symbol PRNP contributors: mct/shn - updated : 26-12-2013
HGNC name prion protein
HGNC id 9449
Type ubiquitous
   expressed in (based on citations)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
blood / hematopoieticerythroid    
Endocrinepancreas   highly
Nervousbrain   highly Homo sapiens
Reproductivefemale systemovary   
 male systemprostate   
Urinarykidney   highly
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Nervouscentral  highly Homo sapiens
SystemCellPubmedSpeciesStageRna symbol
Lymphoid/Immunedendritic cell
cell lineage
cell lines
  • N terminal signal peptide of 22 AA
  • four sequential copies of the five tandem octapeptide repeats highly instable
  • two hydrophobic segments
  • two possible sites for N glycosylation
  • five tandem octapeptide repeats highly instable
  • an active domain requiring certain regions such as the Cu-binding octameric repeat region and the hydrophobic core
  • C terminal hydrophobic region TM2 functioning as second signal sequence
  • secondary structure alpha helical conformation with a single disulfide bond linking CYS residues at 179 and 214 position
    conjugated GlycoP , Other
    interspecies ortholog to Prnp, Mus musculus
    ortholog to Prnp, Rattus norvegicus
    ortholog to prnp, Danio rerio
    ortholog to PRNP, Pan troglodytes
    intraspecies homolog to PRNP
  • prion family
  • CATEGORY regulatory , signaling neurotransmitter
    SUBCELLULAR LOCALIZATION     plasma membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
  • glycosylphosphatidylinositol-anchored cell-surface protein
  • PrPC mutants, PrP145stop and PrP160stop were detected in the nucleus when expressed in neuroblastoma cells ,
  • basic FUNCTION
  • may be a signal transduction protein
  • potent anti-apoptotic protein against BAX-mediated cell-death
  • Cu-binding protein and normal function requires Cu-binding
  • playing a role in the formation of long-term memory
  • having a neuroprotective activity against apoptosis
  • playing a role in copper homeostasis
  • essential for myelin maintenance ,
  • a mediator of Amyloid beta toxicity
  • interaction between the middle region of PRNP and lipids is essential for the formation of its conformation, and role of alteration of this interaction in the pathogenesis of prion disease
  • enhancing of the phagocytotic activity in PRNP-deficient macrophage cells
  • involved in T lymphocytes response to oxidative stress, and having a protective function in thymocytes against oxidative stress
  • anchored PRNP is an essential component for the rapid neural spread and CNS neuroinvasion of prion infection
  • CELLULAR PROCESS cell life, antiapoptosis
    signaling neurotransmission
    neuronal transmission
    a component
  • DNA molecules
  • RNA
  • RNA molecules ,
  • small molecule metal binding,
  • Cu2+
  • unilamellar vesicles containing phosphatidylserine
  • phosphatidylglycerol and phosphatidylserine
  • Hemin (iron protoporphyrin IX)
  • protein
  • heat shock protein 60, Hsp60
  • casein kinase 2, CK2
  • plasminogen
  • neuronal phosphoprotein synapsin Ib, Grb2, and Pint1
  • stress-inducible protein 1, STI1
  • heparin
  • tubulin
  • heterogeneous nuclear ribonucleoprotein A2/B1 and aldolase C
  • lipoprotein receptor-related protein 1, LRP1
  • clusterin
  • Abeta42 oligomers
  • ADAM23
  • STIP1 (PMID :
  • kinesin and dynein
  • Hsp70
  • thiamine
  • KCTD1 is a molecular interaction partners of the cellular prion protein (PRNP)
  • ADAM8 can perform alpha-cleavage of PRNP and PRNP can regulate ADAM8 expression
  • amyloid-beta precursor protein
  • FOXO3 negatively regulates PRNP expression by binding to the PRNP promoter, which is negatively regulated by insulin-like growth factor 1 (IGF1)
  • interacts with BECN1 to recruit the PIK3C3 complex into lipid rafts and thus activates autophagy in response to Abeta42, defining a novel role of PRNP in the regulation of autophagy
  • AMFR is critical for unglycosylated PRNP ubiquitylation and degradation
  • cell & other
    activated by ATOX1, a transcription factor that upregulates prion protein expression
    Other endoproteolytic alpha-cleavage of cellular prion protein (PRNP) regulates PRNP toxicity and functions
    corresponding disease(s) CJD , GSSS , IDTF , HDL1 , EOD
    related resource Prion Protein/CJD database
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    by misfolded prion protein in sudden infant death syndrome (SIDS)
    constitutional     --over  
    in ischemic brain damage
    tumoral     --over  
    in gastric cancer tissues (ectopic expression of PRNP could promote tumorigenesis, proliferation, and G1/S transition in gastric cancer cells)
    constitutional     --other  
    altered expression levels may play an important role in susceptibility to infection
    tumoral     --over  
    may constitute a prognostic marker for colorectal cancerrecurrence
  • for Creutzfeldt-Jakob disease
  • to fatal familial insomnia
  • to Alzheimer disease-like tau disease
  • Variant & Polymorphism SNP
  • strong susceptibility factor for PRNP disease (sporadic CJD)
  • SNP M129V increasing the risk of Creutzfeldt-Jakob disease
  • SNP M129M or M129V increasing the long-term memory, and associated to a fatal familial insomnia
  • rare PRNP mutation (Q160X) that resulted in the production of truncated PRNP, associated to Alzheimer disease-like tau disease
  • Candidate gene
    Therapy target
    target for anticancer therapy
  • mice expressing DeltaPrP or Dpl suffer from widespread leukoencephalopathy
  • mouse expressing the PrP(DeltaCD), a PrP variant lacking 40 central residues, displays a rapidly progressive, lethal phenotype with extensive central and peripheral myelin degeneration
  • ablation of the prion protein PrP(C) triggers a chronic demyelinating polyneuropathy in four independently targeted mouse strains
  • absence of PrPC in a transgenic Alzheimer mouse rescues deficits in spatial learning and memory
  • Knockdown PRNP homolog in the zebrafish leads to a dose-dependent phenotype characterized by systemic morphological defects, reduced cell adhesion and CNS cell death