Variant position: 450 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 ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Mouse ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Rat ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Pig ARELQPSIIFIDEVDSLLRE RREGEHDASRRLKTEFLIEFD
Bovine ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Chicken ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Xenopus laevis ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Xenopus tropicalis ARELQPSIIFIDEVDSLLCE RREGEHDASRRLKTEFLIEFD
Zebrafish ARELQPSIIFIDEIDSLLCE RREGEHDASRRLKTEFLIEFD
Caenorhabditis elegans ARNAQPSIIFIDEIDSILCE RSEKDAEVSRRMKTEFLVQFD
Drosophila ARHMQPSIIFIDEVDSLLSE RSSSEHEASRRLKTEFLVEFD
Slime mold ATHFQPSIIFIDEIDSLLTE RSSNESEASRRLKTEILVQFD
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.
Detection of novel mutations and review of published data suggests that hereditary spastic paraplegia caused by spastin (SPAST) mutations is found more often in males.
Proukakis C.; Moore D.; Labrum R.; Wood N.W.; Houlden H.;
J. Neurol. Sci. 306:62-65(2011)
Cited for: VARIANTS SPG4 MET-364; LEU-368; GLU-377 AND SER-450;
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