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UniProtKB/Swiss-Prot Q9UBP0: Variant p.Gln347Lys

Spastin
Gene: SPAST
Variant information

Variant position:  347
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glutamine (Q) to Lysine (K) at position 347 (Q347K, p.Gln347Lys).
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:  Change from medium size and polar (Q) to large size and basic (K)
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 SPG4; promotes microtubule binding.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  347
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:   LIMNEIVDNGTAVKFDDIAG  Q DLAKQALQEIVILPSLRPEL
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                         LIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPEL

Mouse                         LIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPEL

Rat                           LIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPEL

Pig                           FIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPEL

Bovine                        LIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPEL

Chicken                       LILNEIVDSGPAVKFDDIAGQELAKQALQEIVILPSLRPEL

Xenopus laevis                LILNEIVDSGPSVKFADIAGQDLAKQALQEIVILPSIRPEL

Xenopus tropicalis            LILNEIVDSGPTVKFADIAGQDLAKQALQEIVILPSIRPEL

Zebrafish                     LILNEIVDSGSVVRFDDIAGQDLAKQALQEIVILPALRPEL

Caenorhabditis elegans        RLLDEVLDN-TGVRMDDVAGCHSAKAALEEAVILPALNPNL

Drosophila                    LILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPEL

Slime mold                    LIMNEIMDRKNPVKWDDVVGLDKVKQSLMESVILPNLRPDV

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


Literature citations

Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing.
Evans K.J.; Gomes E.R.; Reisenweber S.M.; Gundersen G.G.; Lauring B.P.;
J. Cell Biol. 168:599-606(2005)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; INTERACTION WITH MICROTUBULES; SUBCELLULAR LOCATION; MUTAGENESIS OF LYS-388 AND GLU-442; CHARACTERIZATION OF VARIANTS SPG4 LYS-344; LYS-347; LYS-386; ARG-388 AND CYS-499;

Spastin gene mutation in Japanese with hereditary spastic paraplegia.
Yabe I.; Sasaki H.; Tashiro K.; Matsuura T.; Takegami T.; Satoh T.;
J. Med. Genet. 39:E46-E46(2002)
Cited for: VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499;

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.