Sequence information
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:
VGEGEKLVRALFAVARELQP
S IIFIDEVDSLLCERREGEHD
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 VGEGEKLVRALFAVARELQPS IIFIDEVDSLLCERREGEHD
Mouse VGEGEKLVRALFAVARELQPS IIFIDEVDSLLCERREGEHD
Rat VGEGEKLVRALFAVARELQPS IIFIDEVDSLLCERREGEHD
Pig VGEGEKLVRALFAVARELQPS IIFIDEVDSLLRERREGEHD
Bovine VGEGEKLVRALFAVARELQPS IIFIDEVDSLLCERREGEHD
Chicken VGEGEKLVRALFAVARELQPS IIFIDEVDSLLCERREGEHD
Xenopus laevis VGEGEKLVRALFSVARELQPS IIFIDEVDSLLCERREGEHD
Xenopus tropicalis VGEGEKLVRALFSVARELQPS IIFIDEVDSLLCERREGEHD
Zebrafish VGEGEKLVRALFAVARELQPS IIFIDEIDSLLCERREGEHD
Caenorhabditis elegans VGDSEKTIRGLFQIARNAQPS IIFIDEIDSILCERSEKDAE
Drosophila VGDGEKLVRALFAVARHMQPS IIFIDEVDSLLSERSSSEHE
Slime mold VGDGEKLVRALFAVATHFQPS IIFIDEIDSLLTERSSNESE
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
Chain
1 – 616
Spastin
Topological domain
78 – 616
Cytoplasmic
Region
228 – 616
Sufficient for microtubule severing
Mutagenesis
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.
Mutagenesis
448 – 448
C -> AG. Abolishes ATPase activity.
Mutagenesis
448 – 448
C -> S. Does not affect ATPase activity.
Mutagenesis
451 – 451
R -> G. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.
Beta strand
433 – 441
Literature citations
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.;
Neurology 55:1388-1390(2000)
Cited for: VARIANTS SPG4 PHE-436 AND ASP-559;
Disclaimer:
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.