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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04156: Variant p.Phe198Ser

Major prion protein
Gene: PRNP
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Variant information Variant position: help 198 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 Phenylalanine (F) to Serine (S) at position 198 (F198S, p.Phe198Ser). 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 aromatic (F) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In GSD; atypical form with neurofibrillary tangles. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 198 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 253 The length of the canonical sequence.
Location on the sequence: help DCVNITIKQHTVTTTTKGEN F TETDVKMMERVVEQMCITQY 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                         DCVNITIKQHTVTTTTK--------GENFTETDV--KMMERVVEQMCITQY

Gorilla                       DCVNITIKQHTVTTTTK--------GENFTETDV--KMMER

                              DCVNITVKQHTV-TTTK--------GENFTETDI--KMMER

Rhesus macaque                DCVNITIKQHTVTTTTK--------GENFTETDV--KMMER

Chimpanzee                    DCVNITIKQHTVTTTTK--------GENFTETDV--KMMER

Mouse                         DCVNITIKQHTVTTTTK--------GENFTETDV--KMMER

Rat                           DCVNITIKQHTVTTTTK--------GENFTETDV--KMMER

Pig                           DCVNITVKQHTVTTTTK--------GENFTETDV--KMIER

Bovine                        DCVNITVKEHTVTTTTK--------GENFTETDI--KMMER

Rabbit                        DCVNITVKQHTVTTTTK--------GENFTETDI--KIMER

Goat                          DCVNITVKQHTVTTTTK--------GENFTETDI--KIMER

Sheep                         DCVNITVKQHTVTTTTK--------GENFTETDI--KIMER

Cat                           DCVNITVKQHTVTTTTK--------GENFTETDM--KIMER

Chicken                       DCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTK
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 23 – 230 Major prion protein
Region 23 – 230 Interaction with GRB2, ERI3 and SYN1
Glycosylation 181 – 181 N-linked (GlcNAc...) asparagine
Glycosylation 197 – 197 N-linked (GlcNAc...) asparagine
Disulfide bond 179 – 214
Beta strand 196 – 202



Literature citations
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Lee S.; Antony L.; Hartmann R.; Knaus K.J.; Surewicz K.; Surewicz W.K.; Yee V.C.;
EMBO J. 29:251-262(2010)
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 125-227 OF VARIANT VAL-129; VARIANT VAL-129; VARIANT CJD ASN-178; VARIANT FFI ASN-178; VARIANT GSD SER-198; SUBUNIT; DOMAIN;
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.