UniProtKB/Swiss-Prot P04637: Variant p.Tyr234Asp

Cellular tumor antigen p53
Gene: TP53
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Variant information Variant position:

234 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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 Aspartate (D) at position 234 (Y234D, p.Tyr234Asp). 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 acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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 sporadic cancers; somatic mutation. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs864622237 [ dbSNP | Ensembl ]

Sequence information Variant position:

234 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:

HSVVVPYEPPEVGSDCTTIH Y NYMCNSSCMGGMNRRPILTI 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                         HSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI

                              HSVVVPYEPPEVGSDYTTIHYNYMCNSSCMGGMNRRPILTI

Rhesus macaque                HSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI

Mouse                         HSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTI

Rat                           HSVVVPYEPPEVGSDYTTIHYKYMCNSSCMGGMNRRPILTI

Pig                           HSVVVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPILTI

Bovine                        HSVVVPYESPEIDSECTTIHYNFMCNSSCMGGMNRRPILTI

Rabbit                        HSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI

Sheep                         HSVVVPYESPEIESECTTIHYNFMCNSSCMGGMNRRPILTI

Cat                           HSVVVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPIITI

Chicken                       HSVVVPYEPPEVGSDCTTVLYNFMCNSSCMGGMNRRPILTI

Xenopus laevis                HSVCVPYEGPQVGTECTTVLYNYMCNSSCMGGMNRRPILTI

Zebrafish                     HSVFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTI

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.

Type	Positions	Description
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.