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UniProtKB/Swiss-Prot P04637: Variant p.Val173Met

Cellular tumor antigen p53
Gene: TP53
Variant information

Variant position:  173
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 Valine (V) to Methionine (M) at position 173 (V173M, p.Val173Met).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
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 LFS; germline mutation and in sporadic cancers; somatic mutation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  173
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:   PGTRVRAMAIYKQSQHMTEV  V RRCPHHERCSDSDGLAPPQH
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                         PGTRVRAMAIYKQSQHMTEVVRRCPHHERCSD-SDGLAPPQH

                              PNTCVRAMAIYKKSEFVTEVVRRCPHHERCSDSSDGLAPPQ

Rhesus macaque                PGSRVRAMAIYKQSQHMTEVVRRCPHHERCSD-SDGLAPPQ

Mouse                         AGSRVRAMAIYKKSQHMTEVVRRCPHHERCSD-GDGLAPPQ

Rat                           PGTRVRAMAIYKKSQHMTEVVRRCPHHERCSD-GDGLAPPQ

Pig                           PGTRVRAMAIYKKSEYMTEVVRRCPHHERSSDYSDGLAPPQ

Bovine                        PGTRVRAMAIYKKLEHMTEVVRRCPHHERSSDYSDGLAPPQ

Rabbit                        PGTRVRAMAIYKKSQHMTEVVRRCPHHERCSD-SDGLAPPQ

Sheep                         PGTRVRAMAIYKKLEHMTEVVRRSPHHERSSDYSDGLAPPQ

Cat                           PGTCVRAMAIYKKSEFMTEVVRRCPHHERCPDSSDGLAPPQ

Chicken                       PGSSLRAVAVYKKSEHVAEVVRRCPHHERCGGGTDGLAPAQ

Xenopus laevis                RGSILRATAVYKKSEHVAEVVKRCPHHERSVEPGEDAAPPS

Zebrafish                     QGSVVRATAIYKKSEHVAEVVRRCPHHERTPD-GDNLAPAG

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 1 – 320 Interaction with CCAR2
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 176 – 176 Zinc
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.


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.