Variant position: 666 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1466 The length of the canonical sequence.
Location on the sequence:
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 TGGPPGENGKPGEPGPKGDA GAPGAPGGKGDAGAPGERGPP
Mouse TGGPPGENGKPGEPGPKGEV GAPGAPGGKGDSGAPGERGPP
Rat TSGPPGENGKPGEPGPKGEA GAPGVPGGKGDSGAPGERGPP
Bovine TSGPPGENGKPGEPGPKGEA GAPGIPGGKGDSGAPGERGPP
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
154 – 1221 Collagen alpha-1(III) chain
168 – 1196 Triple-helical region
650 – 650 4-hydroxyproline
656 – 656 4-hydroxyproline
659 – 659 4-hydroxyproline
661 – 661 4-hydroxyproline
668 – 668 4-hydroxyproline
671 – 671 4-hydroxyproline
680 – 680 4-hydroxyproline
686 – 686 4-hydroxyproline
A novel G499D substitution in the alpha 1(III) chain of type III collagen produces variable forms of Ehlers-Danlos syndrome type IV.
McGrory J.; Costa T.; Cole W.G.;
Hum. Mutat. 7:59-60(1996)
Cited for: VARIANT EDSVASC ASP-666;
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.