PrionDB: Extraction of mutation data from the literature

2005, PrionDB.

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

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation K109I was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation K109I in PRIO_MOUSE

Point mutation:	K109I
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_MOUSE (Prnp,Prn-p)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 109 in PRIO_MOUSE
Other point mutations / same protein	List of mutations in PRIO_MOUSE
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 110 in Mammalian prion proteins family Position 110 in Prion proteins (PRP, PRNP) family
Reference:	A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum. Stewart RS, Drisaldi B, Harris DA Mol Biol Cell 2001 Apr;12(4):881-9.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	True positive

Relevant sentences:

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) )

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