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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04637: Variant p.Tyr236Cys

Cellular tumor antigen p53
Gene: TP53
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Variant information Variant position: help 236 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 Tyrosine (Y) to Cysteine (C) at position 236 (Y236C, p.Tyr236Cys). 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 (Y) to medium size and polar (C) 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 LFS; germline mutation and in sporadic cancers; somatic mutation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 236 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 393 The length of the canonical sequence.
Location on the sequence: help VVVPYEPPEVGSDCTTIHYN Y MCNSSCMGGMNRRPILTIIT 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                         VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIIT

                              VVVPYEPPEVGSDYTTIHYNYMCNSSCMGGMNRRPILTIIT

Rhesus macaque                VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIIT

Mouse                         VVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIIT

Rat                           VVVPYEPPEVGSDYTTIHYKYMCNSSCMGGMNRRPILTIIT

Pig                           VVVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPILTIIT

Bovine                        VVVPYESPEIDSECTTIHYNFMCNSSCMGGMNRRPILTIIT

Rabbit                        VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIIT

Sheep                         VVVPYESPEIESECTTIHYNFMCNSSCMGGMNRRPILTIIT

Cat                           VVVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPIITIIT

Chicken                       VVVPYEPPEVGSDCTTVLYNFMCNSSCMGGMNRRPILTILT

Xenopus laevis                VCVPYEGPQVGTECTTVLYNYMCNSSCMGGMNRRPILTIIT

Zebrafish                     VFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIIT
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 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
Binding site 238 – 238
Binding site 242 – 242
Mutagenesis 248 – 248 R -> S. Does not induce SNAI1 degradation.
Beta strand 228 – 236



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.