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 C214A 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 C214A in PRIO_HUMAN

Point mutation:	C214A
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 214 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 214 in Mammalian prion proteins family Position 214 in Prion proteins (PRP, PRNP) family
Reference:	Prion protein glycosylation is sensitive to redox change. Capellari S, Zaidi SI, Urig CB, Perry G, Smith MA, Petersen RB J Biol Chem 1999 Dec 3;274(49):34846-50.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	True positive

Relevant sentences:

C214A

The constructs used in this study employed alanine replacement of cysteine at residue 179 alone (C179A (-Cys1)) , residue 214 alone (C214A (-Cys2)) , or residues 179 and 214 together (C179A / C214A (-Cys1+2)) (Fig. 2 A)
H , diglycosylated with highly modified glycans ; I , intermediate ; U , unglycosylated ; H imm , diglycosylated with immature glycans ; C , control cell line ; -Cys1 , C179A ; -Cys2 , C214A ; -Cys1+2 , C179A / C214A
The same result was obtained when we digested the C214A and C179A / C214A mutants (data not shown)
In contrast , the double mutant (C179A / C214A) demonstrated a stable interaction principally with grp94 (Fig. 4 B)
However , a significant fraction of C179A / C214A reached the cell surface or was secreted
As demonstrated above , the C179A / C214A mutant reached the cell surface

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