Sequence information
Variant position: 678 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:
LTNIKTEEISEVKMDAEFRH
D SGYEVHHQKLVFFAEDVGSN
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 LTNIK-------------TEEISEVKMDAEFRHD ----------------SGYEVHHQKLVFFAEDVGSN
Chimpanzee LTNIK-------------TEEISEVKMDAEFRHD -------
Mouse LTNIK-------------TEEISEVKMDAEFGHD -------
Rat LTNIK-------------TEEISEVKMDAEFGHD -------
Pig LTNIK-------------TEEISEVKMDAEFRHD -------
Caenorhabditis elegans STSSE--------SDEDEDKNIKELRVDIEPIID EP-----
Drosophila VSSTKVQTVLPTVDDDAVQRAVEDVAAAVAHQEA EPQVQHF
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
18 – 687
Soluble APP-alpha
Chain
672 – 770
C99
Chain
672 – 713
Amyloid-beta protein 42
Chain
672 – 711
Amyloid-beta protein 40
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
678 – 679
Cleavage; by ACE
Glycosylation
659 – 659
O-linked (HexNAc...) threonine; partial
Glycosylation
663 – 663
O-linked (GalNAc...) threonine; partial
Glycosylation
667 – 667
O-linked (GalNAc...) serine; partial
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.
Turn
677 – 679
Literature citations
Novel amyloid precursor protein gene missense mutation (D678N) in probable familial Alzheimer's disease.
Wakutani Y.; Watanabe K.; Adachi Y.; Wada-Isoe K.; Urakami K.; Ninomiya H.; Saido T.C.; Hashimoto T.; Iwatsubo T.; Nakashima K.;
J. Neurol. Neurosurg. Psych. 75:1039-1042(2004)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 672-723; VARIANT AD1 ASN-678;
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.