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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15269: Variant p.Val144Asp

Serine palmitoyltransferase 1
Gene: SPTLC1
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Variant information Variant position: help 144 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 Valine (V) to Aspartate (D) at position 144 (V144D, p.Val144Asp). 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 medium size and hydrophobic (V) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 HSAN1A; reduced canonical activity towards serine; does not affect the interaction with SPTLC2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 144 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 473 The length of the canonical sequence.
Location on the sequence: help SLKKYGVGTCGPRGFYGTFD V HLDLEDRLAKFMKTEEAIIY 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                         SLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIY

Mouse                         SLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIY

Rat                           SLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIY

Bovine                        SLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIY

Caenorhabditis elegans        TIFKYGVGSCGPRGFYGTVDVHLDLEKELAKFMGCEEAVLY

Slime mold                    AIRKYGVGSCGPRGFYGTIDVHLDLEKKTASFMKTPEAVLY

Baker's yeast                 TIKNYGVGACGPAGFYGNQDVHYTLEYDLAQFFGTQGSVLY

Fission yeast                 TLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVY
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 – 473 Serine palmitoyltransferase 1
Topological domain 37 – 473 Cytoplasmic
Modified residue 164 – 164 Phosphotyrosine; by ABL
Alternative sequence 143 – 143 D -> E. In isoform 2.
Alternative sequence 144 – 473 Missing. In isoform 2.
Mutagenesis 138 – 138 F -> A. Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates.
Mutagenesis 164 – 164 Y -> F. Increased serine palmitoyltransferase activity and sphingolipid content.
Helix 143 – 155



Literature citations
Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I.
Dawkins J.L.; Hulme D.J.; Brahmbhatt S.B.; Auer-Grumbach M.; Nicholson G.A.;
Nat. Genet. 27:309-312(2001)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1); VARIANTS HSAN1A TRP-133; TYR-133 AND ASP-144; A systematic comparison of all mutations in hereditary sensory neuropathy type I (HSAN I) reveals that the G387A mutation is not disease associated.
Hornemann T.; Penno A.; Richard S.; Nicholson G.; van Dijk F.S.; Rotthier A.; Timmerman V.; von Eckardstein A.;
Neurogenetics 10:135-143(2009)
Cited for: CHARACTERIZATION OF VARIANTS HSAN1A TYR-133; TRP-133 AND ASP-144; CHARACTERIZATION OF VARIANT ALA-387; LACK OF ASSOCIATION OF VARIANT ALA-387 WITH HSAN1A; INTERACTION WITH SPTLC2; V144D Mutation of SPTLC1 Can Present with Both Painful and Painless Phenotypes in Hereditary Sensory and Autonomic Neuropathies Type I.
Ho K.W.D.; Jerath N.U.;
Case Rep. Genet. 2018:1898151-1898151(2018)
Cited for: VARIANT HSAN1A ASP-144;
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.