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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04637: Variant p.Arg273His

Cellular tumor antigen p53
Gene: TP53
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Variant information Variant position: help 273 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 Arginine (R) to Histidine (H) at position 273 (R273H, p.Arg273His). 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 basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; abolishes sequence-specific DNA binding; does not induce SNAI1 degradation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 273 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 TIITLEDSSGNLLGRNSFEV R VCACPGRDRRTEEENLRKKG 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                         TIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG

                              TIITLEDSSGNVLGRNSFEVRVCACPGRDRRTEEENFHKKG

Rhesus macaque                TIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENFRKKG

Mouse                         TIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKE

Rat                           TIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKE

Pig                           TIITLEDASGNLLGRNSFEVRVCACPGRDRRTEEENFLKKG

Bovine                        TIITLEDSCGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG

Rabbit                        TIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENFRKKG

Sheep                         TIITLEDSRGNLLGRSSFEVRVCACPGRDRRTEEENFRKKG

Cat                           TIITLEDSNGKLLGRNSFEVRVCACPGRDRRTEEENFRKKG

Chicken                       TILTLEGPGGQLLGRRCFEVRVCACPGRDRKIEEENFRKRG

Xenopus laevis                TIITLETPQGLLLGRRCFEVRVCACPGRDRRTEEDNYTKKR

Zebrafish                     TIITLETQEGQLLGRRSFEVRVCACPGRDRKTEESNFKKDQ
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 116 – 292 Interaction with AXIN1
Region 256 – 294 Interaction with E4F1
Region 273 – 280 Interaction with DNA
Modified residue 269 – 269 Phosphoserine; by AURKB
Modified residue 284 – 284 Phosphothreonine; by AURKB
Cross 291 – 291 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 292 – 292 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis 269 – 269 S -> A. Abolishes phosphorylation.
Mutagenesis 269 – 269 S -> E. Inhibits strongly its transcriptional activity.
Mutagenesis 284 – 284 T -> E. Inhibits strongly its transcriptional activity.
Beta strand 264 – 274



Literature citations
Identification of a tumor-rejection antigen recognized by HLA-B46 restricted CTL.
Azuma K.; Shichijo S.; Itoh K.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS HIS-273 AND SER-309; Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage.
Chehab N.H.; Malikzay A.; Stavridi E.S.; Halazonetis T.D.;
Proc. Natl. Acad. Sci. U.S.A. 96:13777-13782(1999)
Cited for: PHOSPHORYLATION AT SER-15 AND SER-20; INDUCTION BY DNA DAMAGE; CHARACTERIZATION OF LFS VARIANT HIS-273; MUTAGENESIS OF THR-18; SER-20 AND 22-LEU-TRP-23; SUBCELLULAR LOCATION; INTERACTION WITH PML AND MDM2; p53 inhibits tumor cell invasion via the degradation of snail protein in hepatocellular carcinoma.
Lim S.O.; Kim H.; Jung G.;
FEBS Lett. 584:2231-2236(2010)
Cited for: INTERACTION WITH SNAI1; CHARACTERIZATION OF VARIANTS LEU-110; PRO-155; HIS-175; SER-232; SER-249; HIS-273 AND TRP-282; MUTAGENESIS OF ARG-248; Germline mutations of the p53 tumor-suppressor gene in children and young adults with second malignant neoplasms.
Malkin D.; Jolly K.W.; Barbier N.; Look A.T.; Friend S.H.; Gebhardt M.C.; Andersen T.I.; Boerresen A.-L.; Li F.P.; Garber J.; Strong L.C.;
N. Engl. J. Med. 326:1309-1315(1992)
Cited for: VARIANTS LFS HIS-273 AND VAL-325; p53 mutations in colorectal cancer.
Rodrigues N.R.; Rowan A.; Smith M.E.F.; Kerr I.B.; Bodmer W.F.; Gannon J.V.; Lane D.P.;
Proc. Natl. Acad. Sci. U.S.A. 87:7555-7559(1990)
Cited for: VARIANTS SPORADIC CANCERS PHE-241 AND HIS-273; p53 gene mutations in Barrett's epithelium and esophageal cancer.
Casson A.G.; Mukhopadhyay T.; Cleary K.R.; Ro J.Y.; Levin B.; Roth J.A.;
Cancer Res. 51:4495-4499(1991)
Cited for: VARIANTS SPORADIC CANCERS LEU-152; ALA-155; HIS-175; PHE-176 AND HIS-273; Frequent p53 mutations in head and neck cancer.
Somers K.D.; Merrick M.A.; Lopez M.E.; Incognito L.S.; Schechter G.L.; Casey G.;
Cancer Res. 52:5997-6000(1992)
Cited for: VARIANTS SPORADIC CANCERS PHE-176; PHE-242; CYS-245; LEU-248 AND HIS-273; p53 alterations in human squamous cell carcinomas and carcinoma cell lines.
Caamano J.; Zhang S.Y.; Rosvold E.A.; Bauer B.; Klein-Szanto A.J.P.;
Am. J. Pathol. 142:1131-1139(1993)
Cited for: VARIANTS SPORADIC CANCERS SER-151; PRO-156; LYS-174; ARG-194; CYS-220; GLN-248; LEU-248 AND HIS-273; 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;
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.