Variant position: 441 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 KLVRALFAVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Mouse KLVRALFAVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Rat KLVRALFAVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Pig KLVRALFAVARELQPSIIFI DEVDSLLRERREGEHDASRRL
Bovine KLVRALFAVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Chicken KLVRALFAVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Xenopus laevis KLVRALFSVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Xenopus tropicalis KLVRALFSVARELQPSIIFI DEVDSLLCERREGEHDASRRL
Zebrafish KLVRALFAVARELQPSIIFI DEIDSLLCERREGEHDASRRL
Caenorhabditis elegans KTIRGLFQIARNAQPSIIFI DEIDSILCERSEKDAEVSRRM
Drosophila KLVRALFAVARHMQPSIIFI DEVDSLLSERSSSEHEASRRL
Slime mold KLVRALFAVATHFQPSIIFI DEIDSLLTERSSNESEASRRL
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.
435 – 442
Hereditary spastic paraplegia caused by mutations in the SPG4 gene.
Buerger J.; Fonknechten N.; Hoeltzenbein M.; Neumann L.; Bratanoff E.; Hazan J.; Reis A.;
Eur. J. Hum. Genet. 8:771-776(2000)
Cited for: VARIANT SPG4 GLY-441;
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