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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50897: Variant p.Arg122Trp

Palmitoyl-protein thioesterase 1
Gene: PPT1
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Variant information Variant position: help 122 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 Arginine (R) to Tryptophan (W) at position 122 (R122W, p.Arg122Trp). 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 large size and basic (R) to large size and aromatic (W) 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 CLN1; retained in the endoplasmic reticulum rather than reaching the lysosome. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 122 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 306 The length of the canonical sequence.
Location on the sequence: help DPKLQQGYNAMGFSQGGQFL R AVAQRCPSPPMINLISVGGQ 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                         DPKLQQG-----------------------------YNAMG---------------------------------FSQGG----QFLRAVAQRC-----PSPPMINL---------ISVGGQ

Mouse                         DPKLQQG-----------------------------YNAIG

Rat                           DPKLQHG-----------------------------YNAIG

Bovine                        DPKLQQG-----------------------------YNAMG

Caenorhabditis elegans        DPELKNG-----------------------------YNAIG

Drosophila                    DEHLAKG-----------------------------YHAIG

Baker's yeast                 EERFRKAIGGAENEAKISLCQTLNLSSFDANADLANYEGPK

Fission yeast                 RIRFQEAIHNTEPPSPLA---NINIEDMDIPSD---YDGVI
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 28 – 306 Palmitoyl-protein thioesterase 1
Active site 115 – 115
Disulfide bond 96 – 128
Alternative sequence 42 – 144 Missing. In isoform 2.
Helix 116 – 127



Literature citations
Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis.
Vesa J.; Hellsten E.; Verkruyse L.A.; Camp L.A.; Rapola J.; Santavuori P.; Hofmann S.L.; Peltonen L.;
Nature 376:584-587(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1); VARIANT CLN1 TRP-122; Novel interactions of CLN5 support molecular networking between neuronal ceroid lipofuscinosis proteins.
Lyly A.; von Schantz C.; Heine C.; Schmiedt M.L.; Sipilae T.; Jalanko A.; Kyttaelae A.;
BMC Cell Biol. 10:83-83(2009)
Cited for: CHARACTERIZATION OF VARIANTS CLN1 ARG-108 AND TRP-122; INTERACTION WITH CLN5; 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.