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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q12756: Variant p.Ala255Val

Kinesin-like protein KIF1A
Gene: KIF1A
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Variant information Variant position: help 255 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 Alanine (A) to Valine (V) at position 255 (A255V, p.Ala255Val). 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 Change from small size and hydrophobic (A) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 SPG30; reduces accumulation in distal regions of the neurites; no effect on microtubule motility. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 255 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1690 The length of the canonical sequence.
Location on the sequence: help NITTEKVSKISLVDLAGSER A DSTGAKGTRLKEGANINKSL 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                         NITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSL

Mouse                         NITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSL

Rat                           NITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSL

Drosophila                    NLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSL

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 – 1690 Kinesin-like protein KIF1A
Domain 5 – 354 Kinesin motor



Literature citations
Exome sequencing and disease-network analysis of a single family implicate a mutation in KIF1A in hereditary spastic paraparesis.
Erlich Y.; Edvardson S.; Hodges E.; Zenvirt S.; Thekkat P.; Shaag A.; Dor T.; Hannon G.J.; Elpeleg O.;
Genome Res. 21:658-664(2011)
Cited for: VARIANT SPG30 VAL-255; KIF1A missense mutations in SPG30, an autosomal recessive spastic paraplegia: distinct phenotypes according to the nature of the mutations.
Klebe S.; Lossos A.; Azzedine H.; Mundwiller E.; Sheffer R.; Gaussen M.; Marelli C.; Nawara M.; Carpentier W.; Meyer V.; Rastetter A.; Martin E.; Bouteiller D.; Orlando L.; Gyapay G.; El-Hachimi K.H.; Zimmerman B.; Gamliel M.; Misk A.; Lerer I.; Brice A.; Durr A.; Stevanin G.;
Eur. J. Hum. Genet. 20:645-649(2012)
Cited for: VARIANTS SPG30 VAL-255 AND GLY-350; De novo mutations in KIF1A cause progressive encephalopathy and brain atrophy.
Esmaeeli Nieh S.; Madou M.R.; Sirajuddin M.; Fregeau B.; McKnight D.; Lexa K.; Strober J.; Spaeth C.; Hallinan B.E.; Smaoui N.; Pappas J.G.; Burrow T.A.; McDonald M.T.; Latibashvili M.; Leshinsky-Silver E.; Lev D.; Blumkin L.; Vale R.D.; Barkovich A.J.; Sherr E.H.;
Ann. Clin. Transl. Neurol. 2:623-635(2015)
Cited for: VARIANTS MET-46; ASN-136; ILE-187; MET-205; ILE-220; ASP-233; VAL-336 AND HIS-355; VARIANTS NESCAVS MET-99; CYS-216; HIS-216; LYS-253 AND TRP-316; CHARACTERIZATION OF VARIANTS NESCAVS MET-99; CYS-216 AND LYS-253; CHARACTERIZATION OF VARIANT SPG30 VAL-255; CHARACTERIZATION OF VARIANT ILE-220; De novo mutations in the motor domain of KIF1A cause cognitive impairment, spastic paraparesis, axonal neuropathy, and cerebellar atrophy.
Lee J.R.; Srour M.; Kim D.; Hamdan F.F.; Lim S.H.; Brunel-Guitton C.; Decarie J.C.; Rossignol E.; Mitchell G.A.; Schreiber A.; Moran R.; Van Haren K.; Richardson R.; Nicolai J.; Oberndorff K.M.; Wagner J.D.; Boycott K.M.; Rahikkala E.; Junna N.; Tyynismaa H.; Cuppen I.; Verbeek N.E.; Stumpel C.T.; Willemsen M.A.; de Munnik S.A.; Rouleau G.A.; Kim E.; Kamsteeg E.J.; Kleefstra T.; Michaud J.L.;
Hum. Mutat. 36:69-78(2015)
Cited for: VARIANTS NESCAVS LEU-58; MET-99; ASP-102; PHE-144; CYS-167; PRO-202; ARG-215; PRO-216; GLN-249; LYS-253 AND TRP-316; CHARACTERIZATION OF VARIANTS NESCAVS MET-99; PRO-202; ARG-215; PRO-216 AND LYS-253; CHARACTERIZATION OF VARIANTS SPG30 VAL-255 AND GLY-350; SUBCELLULAR LOCATION;
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.