UniProtKB/Swiss-Prot P04156 : Variant p.Glu200Lys
Major prion protein
Gene: PRNP
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Variant information
Variant position:
200
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
LP/P [Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]
The variants are classified into three categories: LP/P, LB/B and US.LP/P: likely pathogenic or pathogenic. LB/B: likely benign or benign. US: uncertain significance
Residue change:
From Glutamate (E) to Lysine (K) at position 200 (E200K, p.Glu200Lys).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:
Change from medium size and acidic (E) to large size and basic (K)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another: Lowest score: -4 (low probability of substitution).Highest score: 11 (high probability of substitution). More information can be found on the following page
Variant description:
In CJD.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
200
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:
253
The length of the canonical sequence.
Location on the sequence:
VNITIKQHTVTTTTKGENFT
E TDVKMMERVVEQMCITQYER
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:
The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VNITIKQHTVTTTTK--------GENFTE TDV--KMMERVVEQMCITQYER
Gorilla VNITIKQHTVTTTTK--------GENFTE TDV--KMMERVV
VNITVKQHTV-TTTK--------GENFTE TDI--KMMERVV
Rhesus macaque VNITIKQHTVTTTTK--------GENFTE TDV--KMMERVV
Chimpanzee VNITIKQHTVTTTTK--------GENFTE TDV--KMMERVV
Mouse VNITIKQHTVTTTTK--------GENFTE TDV--KMMERVV
Rat VNITIKQHTVTTTTK--------GENFTE TDV--KMMERVV
Pig VNITVKQHTVTTTTK--------GENFTE TDV--KMIERVV
Bovine VNITVKEHTVTTTTK--------GENFTE TDI--KMMERVV
Rabbit VNITVKQHTVTTTTK--------GENFTE TDI--KIMERVV
Goat VNITVKQHTVTTTTK--------GENFTE TDI--KIMERVV
Sheep VNITVKQHTVTTTTK--------GENFTE TDI--KIMERVV
Cat VNITVKQHTVTTTTK--------GENFTE TDM--KIMERVV
Chicken FNITVTEYSIGPAAKKNTSEAVAAANQTE VEMENKVVTKVI
Sequence annotation in neighborhood:
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
23 – 230
Major prion protein
Region
23 – 230
Interaction with GRB2, ERI3 and SYN1
Glycosylation
181 – 181
N-linked (GlcNAc...) asparagine
Glycosylation
197 – 197
N-linked (GlcNAc...) asparagine
Disulfide bond
179 – 214
Beta strand
196 – 202
Literature citations
Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases.
Zhang Y.; Swietnicki W.; Zagorski M.G.; Surewicz W.K.; Soennichsen F.D.;
J. Biol. Chem. 275:33650-33654(2000)
Cited for: STRUCTURE BY NMR OF 90-231 OF MUTANT LYS-200;
Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia.
Goldfarb L.; Mitrova E.; Brown P.; Toh B.K.; Gajdusek D.C.;
Lancet 336:514-515(1990)
Cited for: VARIANT CJD LYS-200;
Japanese family with Creutzfeldt-Jakob disease with codon 200 point mutation of the prion protein gene.
Inoue I.; Kitamoto T.; Doh-Ura K.; Shii H.; Goto I.; Tateishi J.;
Neurology 44:299-301(1994)
Cited for: VARIANT CJD LYS-200;
Mutation in codon 200 and polymorphism in codon 129 of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease.
Gabizon R.; Rosenman H.; Meiner Z.; Kahana I.; Kahana E.; Shugart Y.; Ott J.; Prusiner S.B.;
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 343:385-390(1994)
Cited for: VARIANT CJD LYS-200;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.