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
VNITVKQHTVTTT-K--------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.