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Gene Ontology Classifications
prion protein

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Prnp. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2012]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
  1. Dutta A et al. (2013) The effect of beta2-alpha2 loop mutation on amyloidogenic properties of the prion protein. FEBS Lett, 587:2918-23. (PubMed:23892077)
  2. Gaspersic J et al. (2010) Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. FEBS J, 277:2038-50. (PubMed:20345906)
  3. Hu W et al. (2010) Pharmacological prion protein silencing accelerates central nervous system autoimmune disease via T cell receptor signalling. Brain, 133:375-88. (PubMed:20145049)
  4. Kasai K et al. (2012) Novel assay with fluorescence-labelled PrP peptides for differentiating L-type atypical and classical BSEs, and scrapie. FEBS Lett, 586:325-9. (PubMed:22285492)
  5. Keshet GI et al. (1999) Scrapie-infected mice and PrP knockout mice share abnormal localization and activity of neuronal nitric oxide synthase. J Neurochem, 72:1224-31. (PubMed:10037495)
  6. Li A et al. (2005) Mammalian prion protein suppresses Bax-induced cell death in yeast. J Biol Chem, 280:17430-4. (PubMed:15753097)
  7. Lorenz H et al. (2002) Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J Biol Chem, 277:8508-16. (PubMed:11756421)
  8. Luo JC et al. (2012) Formation of amyloid fibrils from beta-amylase. FEBS Lett, 586:680-5. (PubMed:22449963)
  9. Lysek DA et al. (2004) Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy. Biochemistry, 43:10393-9. (PubMed:15301538)
  10. Mercer RC et al. (2013) The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6. J Biol Chem, 288:37241-55. (PubMed:24225951)
  11. Pauly PC et al. (1998) Copper stimulates endocytosis of the prion protein. J Biol Chem, 273:33107-10. (PubMed:9837873)
  12. Rachidi W et al. (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J Biol Chem, 278:9064-72. (PubMed:12500977)
  13. Rouvinski A et al. (2003) Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexes. Biochem Biophys Res Commun, 308:750-8. (PubMed:12927782)
  14. Senatore A et al. (2012) Mutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC alpha(2)delta-1 Subunit. Neuron, 74:300-13. (PubMed:22542184)
  15. Spielhaupter C et al. (2001) PrPC Directly Interacts with Proteins Involved in Signaling Pathways. J Biol Chem, 276:44604-12. (PubMed:11571277)
  16. Taylor DR et al. (2005) Assigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosis. J Cell Sci, 118:5141-53. (PubMed:16254249)

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Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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Mouse Genome Database (MGD), Gene Expression Database (GXD), Mouse Tumor Biology (MTB), Gene Ontology (GO), MouseCyc
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