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UniProtKB/Swiss-Prot Q9UBP0: Variant p.Val423Leu

Spastin
Gene: SPAST
Variant information

Variant position:  423
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Unclassified
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Valine (V) to Leucine (L) at position 423 (V423L, p.Val423Leu).
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:  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:  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:  In a breast cancer sample; somatic mutation.
Any additional useful information about the variant.



Sequence information

Variant position:  423
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:   FFNISAASLTSKYVGEGEKL  V RALFAVARELQPSIIFIDEV
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                         FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEV

Mouse                         FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEV

Rat                           FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEV

Pig                           FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEV

Bovine                        FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEV

Chicken                       FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEV

Xenopus laevis                FFNISAASLTSKYVGEGEKLVRALFSVARELQPSIIFIDEV

Xenopus tropicalis            FFNISAASLTSKYVGEGEKLVRALFSVARELQPSIIFIDEV

Zebrafish                     FFNISAATLTSKYVGEGEKLVRALFAVARELQPSIIFIDEI

Caenorhabditis elegans        FFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEI

Drosophila                    FLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEV

Slime mold                    FFSISSSSLTSKYVGDGEKLVRALFAVATHFQPSIIFIDEI

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.

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.


Literature citations

The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Science 314:268-274(2006)
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-423;

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.