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UniProtKB/Swiss-Prot P04156: Variant p.Asp178Asn

Major prion protein
Gene: PRNP
Variant information

Variant position:  178
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Aspartate (D) to Asparagine (N) at position 178 (D178N, p.Asp178Asn).
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 acidic (D) to medium size and polar (N)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
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 FFI and CJD.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  178
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  253
The length of the canonical sequence.

Location on the sequence:   PNQVYYRPMDEYSNQNNFVH  D CVNITIKQHTVTTTTKGENF
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                         PNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTK--------GENF

Gorilla                       PNQVYYRPMDQYSNQNNFVHDCVNITIKQHTVTTTTK----

                              PNQVYYRSVDQYNNQSTFVHDCVNITVKQHTVTTT-K----

Rhesus macaque                PNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTK----

Chimpanzee                    PNQVYYRPMDQYSSQNNFVHDCVNITIKQHTVTTTTK----

Mouse                         PNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTK----

Rat                           PNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTK----

Pig                           PNQVYYRPVDQYSNQNSFVHDCVNITVKQHTVTTTTK----

Bovine                        PNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTK----

Rabbit                        PNQVYYRPVDQYSNQNSFVHDCVNITVKQHTVTTTTK----

Goat                          PNQVYYRPVDQYSNQNNFVHDCVNITVKQHTVTTTTK----

Sheep                         PNQVYYRPVDRYSNQNNFVHDCVNITVKQHTVTTTTK----

Cat                           PNQVYYRPVDQYSNQNNFVHDCVNITVKQHTVTTTTK----

Chicken                       PNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTS

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 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
Beta strand 178 – 181


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;

Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178.
Medori R.; Montagna P.; Tritschler H.J.; Leblanc A.; Cortelli P.; Tinuper P.; Lugaresi E.; Gambetti P.;
Neurology 42:669-670(1992)
Cited for: VARIANT FFI ASN-178;

New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred.
Goldfarb L.G.; Haltia M.; Brown P.; Nieto A.; Kovanen J.; McCombie W.R.; Trapp S.; Gajdusek D.C.;
Lancet 337:425-425(1991)
Cited for: VARIANT CJD ASN-178;

Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism.
Goldfarb L.G.; Petersen R.B.; Tabaton M.; Brown P.; LeBlanc A.C.; Montagna P.; Cortelli P.; Julien J.; Vital C.; Pendelbury W.W.;
Science 258:806-808(1992)
Cited for: VARIANT VAL-129; VARIANT CJD ASN-178; VARIANT FFI ASN-178; CHARACTERIZATION OF VARIANT VAL-129; CHARACTERIZATION OF VARIANT CJD ASN-178; CHARACTERIZATION OF VARIANT FFI ASN-178; POLYMORPHISM;

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.