Variant position: 459 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 616 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 FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSAGD-DR
Mouse FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSAGD-D
Rat FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSAGD-D
Pig FIDEVDSLLRERREGEHDAS RRLKTEFLIEFDGVQSAGD-D
Bovine FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSAGD-D
Chicken FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSSGE-D
Xenopus laevis FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSGGD-D
Xenopus tropicalis FIDEVDSLLCERREGEHDAS RRLKTEFLIEFDGVQSGGD-D
Zebrafish FIDEIDSLLCERREGEHDAS RRLKTEFLIEFDGVQSGGD-E
Caenorhabditis elegans FIDEIDSILCERSEKDAEVS RRMKTEFLVQFDGATSSAD-D
Drosophila FIDEVDSLLSERSSSEHEAS RRLKTEFLVEFDGLPGNPDGD
Slime mold FIDEIDSLLTERSSNESEAS RRLKTEILVQFDGARTNGD-E
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
1 – 616 Spastin
78 – 616 Cytoplasmic
228 – 616 Sufficient for microtubule severing
442 – 442 E -> Q. Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules.
448 – 448 C -> AG. Abolishes ATPase activity.
448 – 448 C -> S. Does not affect ATPase activity.
451 – 451 R -> G. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.
457 – 457 A -> E. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing.
Two novel mutations in the spastin gene (SPG4) found by DHPLC mutation analysis.
Falco M.; Scuderi C.; Musumeci S.; Sturnio M.; Neri M.; Bigoni S.; Caniatti L.; Fichera M.;
Neuromuscul. Disord. 14:750-753(2004)
Cited for: VARIANTS SPG4 GLY-459 AND CYS-460;
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.