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UniProtKB/Swiss-Prot P04637: Variant p.Tyr163Cys

Cellular tumor antigen p53
Gene: TP53
Variant information

Variant position:  163
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 Tyrosine (Y) to Cysteine (C) at position 163 (Y163C, p.Tyr163Cys).
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 large size and aromatic (Y) to medium size and polar (C)
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 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:  163
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:   VQLWVDSTPPPGTRVRAMAI  Y KQSQHMTEVVRRCPHHERCS
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                         VQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCS

                              VQLWVSSPPPPNTCVRAMAIYKKSEFVTEVVRRCPHHERCS

Rhesus macaque                VQLWVDSTPPPGSRVRAMAIYKQSQHMTEVVRRCPHHERCS

Mouse                         VQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCS

Rat                           VQLWVTSTPPPGTRVRAMAIYKKSQHMTEVVRRCPHHERCS

Pig                           VQLWVSSPPPPGTRVRAMAIYKKSEYMTEVVRRCPHHERSS

Bovine                        VQLWVDSPPPPGTRVRAMAIYKKLEHMTEVVRRCPHHERSS

Rabbit                        VQLWVDSTPPPGTRVRAMAIYKKSQHMTEVVRRCPHHERCS

Sheep                         VQLWVDSPPPPGTRVRAMAIYKKLEHMTEVVRRSPHHERSS

Cat                           VQLWVRSPPPPGTCVRAMAIYKKSEFMTEVVRRCPHHERCP

Chicken                       VQVRVGVAPPPGSSLRAVAVYKKSEHVAEVVRRCPHHERCG

Xenopus laevis                LLVRVESPPPRGSILRATAVYKKSEHVAEVVKRCPHHERSV

Zebrafish                     VQMVVDVAPPQGSVVRATAIYKKSEHVAEVVRRCPHHERTP

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.
Beta strand 156 – 165


Literature citations

The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Science 314:268-274(2006)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-134; PHE-157; CYS-163; HIS-175; ARG-177; ARG-193; PRO-213; PHE-241; PHE-242; GLN-248; TRP-248; SER-249; TRP-267; LYS-271; CYS-273; HIS-273; LEU-273; SER-278; ILE-280 AND HIS-281;

Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas.
Chanock S.J.; Burdett L.; Yeager M.; Llaca V.; Langeroed A.; Presswalla S.; Kaaresen R.; Strausberg R.L.; Gerhard D.S.; Kristensen V.; Perou C.M.; Boerresen-Dale A.-L.;
Breast Cancer Res. 9:R5-R5(2007)
Cited for: VARIANTS PRO-110; VAL-113; VAL-138; CYS-163; HIS-163; THR-195; MET-216; ALA-241; MET-249; SER-251; TYR-259 AND CYS-273;

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.