Sequence information
Variant position: 692 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 770 The length of the canonical sequence.
Location on the sequence:
DAEFRHDSGYEVHHQKLVFF
A EDVGSNKGAIIGLMVGGVVI
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 DAEFRHD----------------SGYEVHHQKLVFFA EDVGSNKGAIIGLMVGGVVI
Chimpanzee DAEFRHD----------------SGYEVHHQKLVFFA EDVG
Mouse DAEFGHD----------------SGFEVRHQKLVFFA EDVG
Rat DAEFGHD----------------SGFEVRHQKLVFFA EDVG
Pig DAEFRHD----------------SGYEVHHQKLVFFA EDVG
Caenorhabditis elegans DIEPIIDEP--------------ASFY-RHDKLIQSP EVER
Drosophila AVAHQEAEPQVQHFMTHDLGHRESSFS-LRREFAQHA HAAK
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
18 – 770
Amyloid-beta precursor protein
Chain
672 – 770
C99
Chain
672 – 713
Amyloid-beta protein 42
Chain
672 – 711
Amyloid-beta protein 40
Chain
688 – 770
C83
Peptide
688 – 713
P3(42)
Peptide
688 – 711
P3(40)
Chain
691 – 770
C80
Topological domain
18 – 701
Extracellular
Binding site
677 – 677
Binding site
677 – 677
Binding site
681 – 681
Binding site
681 – 681
Binding site
684 – 684
Binding site
684 – 684
Binding site
685 – 685
Binding site
685 – 685
Site
704 – 704
Implicated in free radical propagation
Site
706 – 706
Susceptible to oxidation
Glycosylation
681 – 681
O-linked (HexNAc...) tyrosine; partial
Alternative sequence
306 – 770
Missing. In isoform APP305.
Mutagenesis
676 – 676
R -> G. 60-70% zinc-induced amyloid-beta protein 28 aggregation.
Mutagenesis
681 – 681
Y -> F. 60-70% zinc-induced amyloid-beta protein 28 aggregation.
Mutagenesis
684 – 684
H -> R. Only 23% zinc-induced amyloid-beta protein 28 aggregation.
Mutagenesis
695 – 695
V -> C. Causes formation of an artifactual disulfide bond with PSEN1.
Mutagenesis
704 – 704
G -> V. Reduced protein oxidation. No hippocampal neuron toxicity.
Mutagenesis
706 – 706
M -> L. Reduced lipid peroxidation inhibition.
Mutagenesis
706 – 706
M -> V. No free radical production. No hippocampal neuron toxicity.
Beta strand
692 – 694
Literature citations
Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene.
Hendriks L.; van Duijn C.M.; Cras P.; Cruts M.; Van Hul W.; van Harskamp F.; Warren A.; McInnis M.G.; Antonarakis S.E.; Martin J.J.; Hofman A.; Van Broeckhoven C.;
Nat. Genet. 1:218-221(1992)
Cited for: VARIANT AD1 GLY-692;
Presenile Alzheimer dementia characterized by amyloid angiopathy and large amyloid core type senile plaques in the APP 692Ala-->Gly mutation.
Cras P.; van Harskamp F.; Hendriks L.; Ceuterick C.; van Duijn C.M.; Stefanko S.Z.; Hofman A.; Kros J.M.; Van Broeckhoven C.; Martin J.J.;
Acta Neuropathol. 96:253-260(1998)
Cited for: VARIANT AD1 GLY-692; CHARACTERIZATION OF PHENOTYPE;
In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692-->Gly) Alzheimer's disease.
Walsh D.M.; Hartley D.M.; Condron M.M.; Selkoe D.J.; Teplow D.B.;
Biochem. J. 355:869-877(2001)
Cited for: CHARACTERIZATION OF VARIANT AD1 GLY-692;
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.