Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04637: Variant p.Arg379His

Cellular tumor antigen p53
Gene: TP53
Feedback?
Variant information Variant position: help 379 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Histidine (H) at position 379 (R379H, p.Arg379His). 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 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 379 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 PGGSRAHSSHLKSKKGQSTS R HKKLMFKTEGPDSD 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                         PGGSRAH---SSHLKSKKGQSTSRHKKLMFKTEG-PDSD

                              PGGSRAH---SSHLKAKKGQSTSRHKKLMFKREG-

Rhesus macaque                PAGSRAH---SSHLKSKKGQSTSRHKKFMFKTEG-

Mouse                         SGDSRAH---SSYLKTKKGQSTSRHKKTMVKKVG-

Rat                           SGDSRAH---SSYPKTKKGQSTSRHKKPMIKKVG-

Pig                           SGENRAH---SSHLKSKKGQSPSRHKKPMFKREG-

Bovine                        PGESRAH---SSHLKSKKRPSPSCHKKPMLKREG-

Rabbit                        PGGSRAH---SSYLKAKKGQSTSRHKKPMFKREG-

Sheep                         PGESRAH---SSHLKSKKGPSPSCHKKPMLKREG-

Cat                           PGGSRAH---SSHLKAKKGQSTSRHKKPMLKREG-

Chicken                       PS--------KGRRVKVEGPQPSCGKKLLQK--G-

Xenopus laevis                VT--------IKCRKCRDEIKPKKGKKLLVKDEQ-

Zebrafish                     AEKYRQKFMTKNKKENRESSEPKQGKKLMVKDEGR
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
Region 300 – 393 Interaction with CARM1
Region 351 – 393 Disordered
Region 368 – 387 Basic (repression of DNA-binding)
Region 374 – 393 Interaction with MORN3
Compositional bias 365 – 384 Basic residues
Modified residue 370 – 370 N6,N6-dimethyllysine; alternate
Modified residue 370 – 370 N6-methyllysine; by SMYD2; alternate
Modified residue 372 – 372 N6-methyllysine; by SETD7
Modified residue 373 – 373 N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate
Modified residue 373 – 373 N6-acetyllysine; alternate
Modified residue 381 – 381 N6-acetyllysine
Modified residue 382 – 382 N6,N6-dimethyllysine; alternate
Modified residue 382 – 382 N6-acetyllysine; alternate
Modified residue 382 – 382 N6-methyllysine; by KMT5A; alternate
Modified residue 392 – 392 Phosphoserine; by CK2, CDK2 and NUAK1
Cross 386 – 386 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Alternative sequence 342 – 393 Missing. In isoform 2, isoform 5 and isoform 8.
Alternative sequence 347 – 393 Missing. In isoform 3, isoform 6 and isoform 9.
Mutagenesis 359 – 359 P -> D. Abolishes binding to USP7.
Mutagenesis 361 – 361 G -> E. Abolishes binding to USP7.
Mutagenesis 362 – 362 S -> A. Abolishes binding to USP7.
Mutagenesis 370 – 370 K -> R. Induces a decrease in methylation by SMYD2.
Mutagenesis 372 – 372 K -> R. Induces a decrease in protein stabilization.
Mutagenesis 373 – 373 K -> R. Abolishes dimethylation by EHMT1 and EHMT2.
Mutagenesis 381 – 381 K -> Q. Mimics acetylation, leading to increased stability.
Mutagenesis 381 – 381 K -> R. Decreased acetylation.
Mutagenesis 382 – 382 K -> A. Abolishes acetylation by CREBBP.
Mutagenesis 382 – 382 K -> R. Abolishes monomethylation by KMT5A.
Mutagenesis 383 – 383 L -> A. Abolishes S-315 phosphorylation by CDK2/cyclin A.
Mutagenesis 385 – 385 F -> A. Reduced SUMO1 conjugation.
Mutagenesis 386 – 386 K -> A. Abolishes SUMO1 conjugation, in vitro and in vivo.
Mutagenesis 387 – 387 T -> A. No effect SUMO1 conjugation.
Mutagenesis 388 – 388 E -> A. Abolishes SUMO1 conjugation.
Mutagenesis 392 – 392 S -> D. Mimics phosphorylation; promotes ability to undergo liquid-liquid phase separation.
Mutagenesis 392 – 392 S -> E. Abolished ability to undergo liquid-liquid phase separation.
Helix 375 – 380



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.