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 T188R 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 T188R in PRIO_HUMAN

Point mutation:	T188R
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_HUMAN (PRNP)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 188 in PRIO_HUMAN
Other point mutations / same protein	List of mutations in PRIO_HUMAN
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 188 in Mammalian prion proteins family Position 188 in Prion proteins (PRP, PRNP) family
Reference:	Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. Lorenz H, Windl O, Kretzschmar HA J Biol Chem 2002 Mar 8;277(10):8508-16.	Medline
Other point mutations / same article	List
Text source	HTML and PDF full texts
Validation status	True positive

Relevant sentences:

T188R

Two Creutzfeldt-Jakob disease-associated PrP mutants , PrP T188K and PrP T188R , revealed a secretory pathway to the cell membrane and PrP Sc-like properties , i.e. enhanced proteinase K resistance and detergent insolubility similar to other mutant PrPs associated with familial prion diseases
Among these PrP mutants , there were three , GFP-PrP Q159 Stop , GFP-PrP T187K , and GFP-PrP T187R (corresponding to human PrP Q160 Stop , T188K , T188R) , that have so far never been cellularly examined and which were assayed in this study most intensively
Biochemical as well as cellular data have been described for four of the seven disease-related PrP mutants , i.e. the three full-length PrP mutants PrP P102L , PrP D178N , PrP E200K (7 , 19 ) and the truncated molecule PrP Y145 Stop (20 ) but not for PrP Q160 Stop , PrP T188K , and PrP T188R (human PrPs)
Two newly described human pathogenic PrP mutants , PrP T188K and PrP T188R , are associated with familial forms of Creutzfeldt-Jakob disease (28 , 33 ) , albeit histopathological characterizations are missing up to now
GFP-PrP chimera with mouse PrPa Human PrP Phenotype P101L P102L GSS W144Stopb Y145Stop GSS Q159Stop Q160Stop EODc D177N D178N FFI T187K T188K CJD T187R T188R CJDd E199K E200K CJD a Mouse PrP contains methionine at position 128 , which corresponds to codon 129 in human PrP , a polymorphic site encoding either methionine or valine
d The T188R / 129V haplotype is linked to CJD
No disease-linked phenotype has been described for T188R / 129M

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