Sequence information
Variant position: 464 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:
DSLLCERREGEHDASRRLKT
E FLIEFDGVQSAGDDRVLVMG
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 DSLLCERREGEHDASRRLKTE FLIEFDGVQSAGD-DRVLVMG
Mouse DSLLCERREGEHDASRRLKTE FLIEFDGVQSAGD-DRVLVM
Rat DSLLCERREGEHDASRRLKTE FLIEFDGVQSAGD-DRVLVM
Pig DSLLRERREGEHDASRRLKTE FLIEFDGVQSAGD-DRVLVM
Bovine DSLLCERREGEHDASRRLKTE FLIEFDGVQSAGD-DRVLVM
Chicken DSLLCERREGEHDASRRLKTE FLIEFDGVQSSGE-DRILVM
Xenopus laevis DSLLCERREGEHDASRRLKTE FLIEFDGVQSGGD-DRVLVM
Xenopus tropicalis DSLLCERREGEHDASRRLKTE FLIEFDGVQSGGD-DRVLVM
Zebrafish DSLLCERREGEHDASRRLKTE FLIEFDGVQSGGD-ERVLVM
Caenorhabditis elegans DSILCERSEKDAEVSRRMKTE FLVQFDGATSSAD-DRILVI
Drosophila DSLLSERSSSEHEASRRLKTE FLVEFDGLPGNPDGDRIVVL
Slime mold DSLLTERSSNESEASRRLKTE ILVQFDGARTNGD-ERVLVM
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
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.
Mutagenesis
457 – 457
A -> E. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing.
Helix
458 – 472
Literature citations
Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic paraplegia.
McCorquodale D.S. III; Ozomaro U.; Huang J.; Montenegro G.; Kushman A.; Citrigno L.; Price J.; Speziani F.; Pericak-Vance M.A.; Zuchner S.;
Clin. Genet. 79:523-530(2011)
Cited for: VARIANTS SPG4 THR-97; ASP-201; SER-314; VAL-360; ALA-464; GLY-498 AND ILE-550;
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.