UniProtKB/Swiss-Prot P04637: Variant p.Val197Glu

Cellular tumor antigen p53
Gene: TP53
Chromosomal location: 17p13.1
Variant information

Variant position:  197
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Unclassified
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants have been found in patients and disease-association is reported in literature. However, this classification is not a definitive assessment of variant pathogenicity.
  • Polymorphism: No disease-association has been reported.
  • Unclassified: Variants have been found in patients but disease-association remains unclear.

Residue change:  From Valine (V) to Glutamate (E) at position 197 (V197E, p.Val197Glu).
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 hydrophobic (V) to medium size and acidic (E)
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 a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
Any additional useful information about the variant.



Sequence information

Variant position:  197
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  393
The length of the canonical sequence.

Location on the sequence:   PHHERCSDSDGLAPPQHLIR  V EGNLRVEYLDDRNTFRHSVV
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                         PHHERCSD-SDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVV

Rhesus macaque                PHHERCSD-SDGLAPPQHLIRVEGNLRVEYSDDRNTFRHSV

Mouse                         PHHERCSD-GDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSV

Rat                           PHHERCSD-GDGLAPPQHLIRVEGNPYAEYLDDRQTFRHSV

Pig                           PHHERSSDYSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSV

Bovine                        PHHERSSDYSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSV

Rabbit                        PHHERCSD-SDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSV

Sheep                         PHHERSSDYSDGLAPPQHLIRVEGNLRAEYFDDRNTFRHSV

Cat                           PHHERCPDSSDGLAPPQHLIRVEGNLHAKYLDDRNTFRHSV

Dog                           PHHERCSDSSDGLAPPQHLIRVEGNLRAKYLDDRNTFRHSV

Chicken                       PHHERCGGGTDGLAPAQHLIRVEGNPQARYHDDETTKRHSV

Xenopus laevis                PHHERSVEPGEDAAPPSHLMRVEGNLQAYYMEDVNSGRHSV

Zebrafish                     PHHERTPD-GDNLAPAGHLIRVEGNQRANYREDNITLRHSV

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 1 – 393 Cellular tumor antigen p53
DNA binding 102 – 292
Region 100 – 370 Interaction with HIPK1
Region 100 – 300 Required for interaction with ZNF385A
Region 113 – 236 Required for interaction with FBXO42
Region 116 – 292 Interaction with AXIN1
Metal binding 179 – 179 Zinc
Modified residue 183 – 183 Phosphoserine; by AURKB
Mutagenesis 183 – 183 S -> A. Abolishes strongly phosphorylation.
Mutagenesis 183 – 183 S -> E. Inhibits slightly its transcriptional activity.
Beta strand 194 – 199


Literature citations

No reference for the current variant in UniProtKB/Swiss-Prot.

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.