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_MOUSE at position 109 were found are listed after the table.

Point mutations at position K109 in PRIO_MOUSE

ProteinPRIO_MOUSE (P04925)    Gene: Prnp,Prn-p    (other point mutations)Swiss-Prot
Cross-reference table
Family page
PositionK109
General numbering (PrionDB) -
DomainNot determined
Family alignments Mammalian prion proteins
Prion proteins (PRP, PRNP)
Other point mutations at the same position Position 110 in Mammalian prion proteins family
Position 110 in Prion proteins (PRP, PRNP) family
Reference #1Stewart RS, Harris DA
J Biol Chem 2001 Jan 19;276(3):2212-20.		Medline
Text sourceHTML full text
Point mutationK109I (True positive)
Reference #2Stewart RS, Drisaldi B, Harris DA
Mol Biol Cell 2001 Apr;12(4):881-9.		Medline
Text sourceHTML full text
Point mutationK109I (True positive)
Reference #3Stewart RS, Harris DA
J Biol Chem 2003 Nov 14;278(46):45960-8. Epub 2003 Aug 21.		Medline
Text sourceHTML full text
Point mutationK109I (True positive)
Reference #4Stewart RS, Harris DA
J Biol Chem 2005 Apr 22;280(16):15855-64. Epub 2005 Jan 25.		Medline
Text sourceHTML full text
Point mutationK109I (True positive)

Relevant sentences

Reference #1 (Stewart RS et al.): K109I
  • The following mutations were introduced into the wild-type PrP cDNA using polymerase chain reaction as described previously (14 ): PG11 (six-octapeptide insertion) , PG14 (eight-octapeptide insertion) , K109I / H110I , 3AV (Ala --> Val at 112 , 114 , and 117) , A116V , D177N , V179I , F197S , E199K , and V209I

  • As positive controls , we analyzed PrP containing the 3AV and A116V mutations , as well as another artificial mutation in the central region (K109I / H110I , referred to as KH-II) that has been reported to increase the amount of transmembrane PrP (12 , 22 )

  • The previously studied mutations included one (A116V) whose human homologue (A117V) is associated with Gerstmann-Sträussler syndrome (38 , 39 ) , and three (N107I , K109I / H110I , and 3AV) that are artificial and have not been described in humans

Reference #2 (Stewart RS et al.): K109I
  • Mutations within or near the central , hydrophobic domain either enhance (3AV , N107I , K109I / H110I , A116V) or diminish (G122P) the efficacy of the internal signal-anchor sequence , thereby either increasing or decreasing the proportion of CtmPrP

  • In contrast to our study , a previous report concluded that CtmPrP transits beyond the ER , based on the endoglycosidase H-resistance of PrP from the brains of transgenic mice that express the 3AV or K109I / H110I mutations (Hegde et al. , 1998a(image) )

Reference #3 (Stewart RS et al.): K109I
  • Some mutations (e.g. A116V , K109I / H110I , and 3AV) increased the proportion of CtmPrP , whereas other mutations (e.g. G122P) decreased it

Reference #4 (Stewart RS et al.): K109I
  • Hegde et al. (7 ) have reported that PrP carrying either of two CtmPrP-favoring mutations (3AV or K109I / H110I) is endo H-resistant in brain lysates from transgenic mice

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