PrionDB: Extraction of mutation data from the literature

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This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in PRIO_HUMAN at position 148 were found are listed after the table.

Point mutations at position R148 in PRIO_HUMAN

ProteinPRIO_HUMAN (P04156)    Gene: PRNP    (other point mutations)Swiss-Prot
Cross-reference table
Family page
PositionR148
General numbering (PrionDB) -
DomainNot determined
Family alignments Mammalian prion proteins
Prion proteins (PRP, PRNP)
Other point mutations at the same position Position 148 in Mammalian prion proteins family
Position 148 in Prion proteins (PRP, PRNP) family
Reference #1Gambetti P, Kong Q, Zou W, Parchi P, Chen SG
Br Med Bull 2003;66:213-39.		Medline
Text sourceHTML full text
Point mutationR148H (True positive)
Reference #2Soldevila M, Andres AM, Blancher A, Calafell F, Ordonez M, Pumarola M, Oliva B, Aramburu J, Bertranpetit J
Neurosci Lett 2004 Jan 30;355(3):157-60.		Medline
Text sourceHTML full text
Point mutationR148H (True positive)

Relevant sentences

Reference #1 (Gambetti P et al.): R148H
  • R148H-129M is similar to sCJDMV2 in all aspects7 , 97

  • Pastore M , Castellani RJ , Chin S et al. CJD-associated with the novel R148H prion protein gene mutation

Reference #2 (Soldevila M et al.): R148H
  • We found two sequence variants: one is a synonymous polymorphism unique to the chimpanzee at codon 226 , TAC to TAT (Y) , with a TAC allele frequency of 80.6% ; the other is a non-synonymous change at codon 148 (R148H) that falls in the target epitope for some common commercial antibodies used for prion diagnostics , and is highly conserved across species

  • Although this variant (R148H) has not been found in any other species , a disease-associated mutation in the same region , codon 145 (Y145Stop) , has been detected in a human CJD patient [4 ]

  • The functional impact of the R148H on protein function would be limited , according to the accepted structural model [18 ]

  • Even though other factors (species characteristics , age , sex , other susceptibility alleles) may influence the outcome , it seems unlikely (because of the low impact on prion structure and failure to observe any symptomatology) that the R148H variant per se might induce a pathogenic form of the protein or cause CJD , even if it lies in a very conserved region

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F.Horn (priondbcmbi.ru.nl), 22-Aug-2005