UniProtKB/Swiss-Prot P04637 : Variant p.Ser392Leu
Cellular tumor antigen p53
Gene: TP53
Feedback ?
Variant information
Variant position:
392
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 Serine (S) to Leucine (L) at position 392 (S392L, p.Ser392Leu).
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 small size and polar (S) to medium size and hydrophobic (L)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-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:
In a sporadic cancer; somatic mutation.
Any additional useful information about the variant.
Sequence information
Variant position:
392
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:
KKGQSTSRHKKLMFKTEGPD
S D
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 KKGQSTSRHKKLMFKTEG-PDS D
KKGQSTSRHKKLMFKREG-LDS
Rhesus macaque KKGQSTSRHKKFMFKTEG-PDS
Mouse KKGQSTSRHKKTMVKKVG-PDS
Rat KKGQSTSRHKKPMIKKVG-PDS
Pig KKGQSPSRHKKPMFKREG-PDS
Bovine KKRPSPSCHKKPMLKREG-PDS
Rabbit KKGQSTSRHKKPMFKREG-PDS
Sheep KKGPSPSCHKKPMLKREG-PDS
Cat KKGQSTSRHKKPMLKREG-LDS
Chicken VEGPQPSCGKKLLQK--G-SD-
Xenopus laevis RDEIKPKKGKKLLVKDEQ-PDS
Zebrafish RESSEPKQGKKLMVKDEGRSDS
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
Region
300 – 393
Interaction with CARM1
Region
351 – 393
Disordered
Region
374 – 393
Interaction with MORN3
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; by KAT6A; 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
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.
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.