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UniProtKB/Swiss-Prot P04637: Variant p.Met237Ile

Cellular tumor antigen p53
Gene: TP53
Variant information

Variant position:  237
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 Methionine (M) to Isoleucine (I) at position 237 (M237I, p.Met237Ile).
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; no effect on susceptibility to calpain.
Any additional useful information about the variant.

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



Sequence information

Variant position:  237
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:   VVPYEPPEVGSDCTTIHYNY  M CNSSCMGGMNRRPILTIITL
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                         VVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITL

                              VVPYEPPEVGSDYTTIHYNYMCNSSCMGGMNRRPILTIITL

Rhesus macaque                VVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITL

Mouse                         VVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITL

Rat                           VVPYEPPEVGSDYTTIHYKYMCNSSCMGGMNRRPILTIITL

Pig                           VVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPILTIITL

Bovine                        VVPYESPEIDSECTTIHYNFMCNSSCMGGMNRRPILTIITL

Rabbit                        VVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITL

Sheep                         VVPYESPEIESECTTIHYNFMCNSSCMGGMNRRPILTIITL

Cat                           VVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPIITIITL

Chicken                       VVPYEPPEVGSDCTTVLYNFMCNSSCMGGMNRRPILTILTL

Xenopus laevis                CVPYEGPQVGTECTTVLYNYMCNSSCMGGMNRRPILTIITL

Zebrafish                     FVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIITL

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 116 – 292 Interaction with AXIN1
Metal binding 238 – 238 Zinc
Metal binding 242 – 242 Zinc
Mutagenesis 248 – 248 R -> S. Does not induce SNAI1 degradation.


Literature citations

Phosphorylation of Def Regulates Nucleolar p53 Turnover and Cell Cycle Progression through Def Recruitment of Calpain3.
Guan Y.; Huang D.; Chen F.; Gao C.; Tao T.; Shi H.; Zhao S.; Liao Z.; Lo L.J.; Wang Y.; Chen J.; Peng J.;
PLoS Biol. 14:e1002555-e1002555(2016)
Cited for: CHARACTERIZATION OF VARIANTS VAL-138; HIS-175; ILE-237; TRP-248 AND PRO-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.