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UniProtKB/Swiss-Prot Q9UG56: Variant p.Cys300Tyr

Phosphatidylserine decarboxylase proenzyme, mitochondrial
Gene: PISD
Variant information

Variant position:  300
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 Cysteine (C) to Tyrosine (Y) at position 300 (C300Y, p.Cys300Tyr).
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 (C) to large size and aromatic (Y)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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 LIBF; loss of autocatalytic processing; probably decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; patient-derived fibroblasts show fragmented mitochondrial morphology around the nucleus; decreased cell viability with increased CASP3 and CASP7 activation.
Any additional useful information about the variant.



Sequence information

Variant position:  300
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  409
The length of the canonical sequence.

Location on the sequence:   FPGSLMSVNPGMARWIKELF  C HNERVVLTGDWKHGFFSLTA
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                         FPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTA

Mouse                         FPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTA

Rat                           FPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTA

Bovine                        FPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTA

Caenorhabditis elegans        VPGLLLSVRPTLLSHVPHLFCLNERVVLNGSWRHGFFSMSA

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 53 – 409 Phosphatidylserine decarboxylase proenzyme, mitochondrial
Chain 53 – 377 Phosphatidylserine decarboxylase beta chain
Topological domain 83 – 409 Mitochondrial intermembrane


Literature citations

The homozygous variant c.797G>A/p.(Cys266Tyr) in PISD is associated with a Spondyloepimetaphyseal dysplasia with large epiphyses and disturbed mitochondrial function.
Girisha K.M.; von Elsner L.; Neethukrishna K.; Muranjan M.; Shukla A.; Bhavani G.S.; Nishimura G.; Kutsche K.; Mortier G.;
Hum. Mutat. 40:299-309(2019)
Cited for: INVOLVEMENT IN LIBF; VARIANT LIBF TYR-300; CHARACTERIZATION OF VARIANT LIBF TYR-300; FUNCTION;

PISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes.
Zhao T.; Goedhart C.M.; Sam P.N.; Sabouny R.; Lingrell S.; Cornish A.J.; Lamont R.E.; Bernier F.P.; Sinasac D.; Parboosingh J.S.; Vance J.E.; Claypool S.M.; Innes A.M.; Shutt T.E.;
Life. Sci Alliance 2:0-0(2019)
Cited for: VARIANT LIBF GLN-277; CHARACTERIZATION OF VARIANTS LIBF GLN-277 AND TYR-300; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; SUBCELLULAR LOCATION; PROTEOLYTIC CLEAVAGE; MUTAGENESIS OF SER-378;

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.