Variant position: 426 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 ISAASLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEVDSL
Mouse ISAASLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEVDSL
Rat ISAASLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEVDSL
Pig ISAASLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEVDSL
Bovine ISAASLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEVDSL
Chicken ISAASLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEVDSL
Xenopus laevis ISAASLTSKYVGEGEKLVRA LFSVARELQPSIIFIDEVDSL
Xenopus tropicalis ISAASLTSKYVGEGEKLVRA LFSVARELQPSIIFIDEVDSL
Zebrafish ISAATLTSKYVGEGEKLVRA LFAVARELQPSIIFIDEIDSL
Caenorhabditis elegans ISASSLTSKWVGDSEKTIRG LFQIARNAQPSIIFIDEIDSI
Drosophila ISAASLTSKYVGDGEKLVRA LFAVARHMQPSIIFIDEVDSL
Slime mold ISSSSLTSKYVGDGEKLVRA LFAVATHFQPSIIFIDEIDSL
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
415 – 415 Y -> A. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes 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.
425 – 432
Unique spectrum of SPAST variants in Estonian HSP patients: presence of benign missense changes but lack of exonic rearrangements.
Braschinsky M.; Tamm R.; Beetz C.; Sachez-Ferrero E.; Raukas E.; Luus S.M.; Gross-Paju K.; Boillot C.; Canzian F.; Metspalu A.; Haldre S.;
BMC Neurol. 10:17-17(2010)
Cited for: VARIANTS LEU-44 AND GLY-229; VARIANTS SPG4 ILE-162; PHE-426 AND SER-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.