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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UBP0: Variant p.Leu426Val

Spastin
Gene: SPAST
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Variant information Variant position: help 426 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Leucine (L) to Valine (V) at position 426 (L426V, p.Leu426Val). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 426 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 616 The length of the canonical sequence.
Location on the sequence: help ISAASLTSKYVGEGEKLVRA L FAVARELQPSIIFIDEVDSL 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         ISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL

Mouse                         ISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL

Rat                           ISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL

Pig                           ISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL

Bovine                        ISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL

Chicken                       ISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL

Xenopus laevis                ISAASLTSKYVGEGEKLVRALFSVARELQPSIIFIDEVDSL

Xenopus tropicalis            ISAASLTSKYVGEGEKLVRALFSVARELQPSIIFIDEVDSL

Zebrafish                     ISAATLTSKYVGEGEKLVRALFAVARELQPSIIFIDEIDSL

Caenorhabditis elegans        ISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSI

Drosophila                    ISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSL

Slime mold                    ISSSSLTSKYVGDGEKLVRALFAVATHFQPSIIFIDEIDSL
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 616 Spastin
Topological domain 78 – 616 Cytoplasmic
Region 228 – 616 Sufficient for microtubule severing
Mutagenesis 415 – 415 Y -> A. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes 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.
Helix 425 – 432



Literature citations
Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics.
Errico A.; Ballabio A.; Rugarli E.I.;
Hum. Mol. Genet. 11:153-163(2002)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SPG4 ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499 AND VAL-556; Spectrum of SPG4 mutations in autosomal dominant spastic paraplegia.
Fonknechten N.; Mavel D.; Byrne P.; Davoine C.-S.; Cruaud C.; Bonsch D.; Samson D.; Coutinho P.; Hutchinson M.; McMonagle P.; Burgunder J.-M.; Tartaglione A.; Heinzlef O.; Feki I.; Deufel T.; Parfrey N.; Brice A.; Fontaine B.; Prud'homme J.-F.; Weissenbach J.; Duerr A.; Hazan J.;
Hum. Mol. Genet. 9:637-644(2000)
Cited for: VARIANTS SPG4 CYS-362; ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499; ASN-555 AND VAL-556; Spectrum of SPG4 mutations in a large collection of North American families with hereditary spastic paraplegia.
Meijer I.A.; Hand C.K.; Cossette P.; Figlewicz D.A.; Rouleau G.A.;
Arch. Neurol. 59:281-286(2002)
Cited for: VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562; Novel and recurrent spastin mutations in a large series of SPG4 Italian families.
Nanetti L.; Baratta S.; Panzeri M.; Tomasello C.; Lovati C.; Azzollini J.; Gellera C.; Di Bella D.; Taroni F.; Mariotti C.;
Neurosci. Lett. 528:42-45(2012)
Cited for: VARIANTS SPG4 THR-95; 112-GLU--VAL-616 DEL; 135-GLU--VAL-616 DEL; LEU-399; ARG-406; THR-409; VAL-426; 431-ARG--VAL-616 DEL; CYS-460; TRP-503; ARG-559 AND 562-ARG--VAL-616 DEL;
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.