Variant position: 436 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 VGEGEKLVRALFAVARELQP SIIFIDEVDSLLCERREGEHD
Mouse VGEGEKLVRALFAVARELQP SIIFIDEVDSLLCERREGEHD
Rat VGEGEKLVRALFAVARELQP SIIFIDEVDSLLCERREGEHD
Pig VGEGEKLVRALFAVARELQP SIIFIDEVDSLLRERREGEHD
Bovine VGEGEKLVRALFAVARELQP SIIFIDEVDSLLCERREGEHD
Chicken VGEGEKLVRALFAVARELQP SIIFIDEVDSLLCERREGEHD
Xenopus laevis VGEGEKLVRALFSVARELQP SIIFIDEVDSLLCERREGEHD
Xenopus tropicalis VGEGEKLVRALFSVARELQP SIIFIDEVDSLLCERREGEHD
Zebrafish VGEGEKLVRALFAVARELQP SIIFIDEIDSLLCERREGEHD
Caenorhabditis elegans VGDSEKTIRGLFQIARNAQP SIIFIDEIDSILCERSEKDAE
Drosophila VGDGEKLVRALFAVARHMQP SIIFIDEVDSLLSERSSSEHE
Slime mold VGDGEKLVRALFAVATHFQP SIIFIDEIDSLLTERSSNESE
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.
435 – 442
Novel mutations in spastin gene and absence of correlation with age at onset of symptoms.
Hentati A.; Deng H.-X.; Zhai H.; Chen W.; Yang Y.; Hung W.-Y.; Azim A.C.; Bohlega S.; Tandan R.; Warner C.; Laing N.G.; Cambi F.; Mitsumoto H.; Roos R.P.; Boustany R.-M.N.; Ben-Hamida M.; Hentati F.; Siddique T.;
Cited for: VARIANTS SPG4 PHE-436 AND ASP-559;
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