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 21, 2013.)

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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]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Prnp
  • participates in the following biological processes:
    • response to oxidative stress ^[5]
  • performs the following molecular functions:
    • copper ion binding ^[5]
  • is located in the following cellular components:
    • endoplasmic reticulum ^[3]
    • Golgi apparatus ^[3]
    • membrane raft ^[6]
    • plasma membrane ^[4]
• The gene product of Prnp has been shown to bind to the gene products of Eri3, Grb2. ^[7]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Prnp
  • participates in the following biological processes:
    • negative regulation of activated T cell proliferation ^[1]
    • negative regulation of calcineurin-NFAT signaling cascade ^[1]
    • negative regulation of interferon-gamma production ^[1]
    • negative regulation of interleukin-17 production ^[1]
    • negative regulation of interleukin-2 production ^[1]
    • negative regulation of protein phosphorylation ^[1]
    • negative regulation of sequence-specific DNA binding transcription factor activity ^[1]
    • negative regulation of T cell receptor signaling pathway ^[1]
• Researchers have inferred, based on genetic interactions, that the gene product of Prnp
  • participates in the following biological processes:
    • negative regulation of apoptotic process based on interactions with Bax ^[2]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Prnp:
  • participates in the following biological processes:
    • learning or memory
    • negative regulation of apoptotic process
    • response to cadmium ion
    • response to copper ion
  • performs the following molecular functions:
    • ATP-dependent protein binding
    • chaperone binding
    • copper ion binding
    • identical protein binding
    • microtubule binding
    • tubulin binding
  • is located in the following cellular components:
    • cytoplasm
    • intracellular membrane-bounded organelle
    • membrane
    • nucleolus
    • nucleus
    • plasma membrane

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Summary text based on GO annotations supported by structural data

• Prnp encodes a protein or proteins that contain the following InterPro domains: Major prion protein N-terminal domain, Prion protein, Prion/Doppel protein, beta-ribbon domain, indicating that the gene product:
  • participates in the following biological processes:
    • protein homooligomerization

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Prnp indicates that it:
  • performs the following molecular functions:
    • metal ion binding
  • is located in the following cellular components:
    • anchored to membrane

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References

1. 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)
2. Li A et al. (2005) Mammalian prion protein suppresses Bax-induced cell death in yeast. J Biol Chem, 280:17430-4. (PubMed:15753097)
3. 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)
4. Pauly PC et al. (1998) Copper stimulates endocytosis of the prion protein. J Biol Chem, 273:33107-10. (PubMed:9837873)
5. 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)
6. 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)
7. Spielhaupter C et al. (2001) PrPC Directly Interacts with Proteins Involved in Signaling Pathways. J Biol Chem, 276:44604-12. (PubMed:11571277)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

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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