UniProtKB/Swiss-Prot P04637 : Variant p.Pro36Leu
Cellular tumor antigen p53
Gene: TP53
Feedback ?
Variant information
Variant position:
36
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 Proline (P) to Leucine (L) at position 36 (P36L, p.Pro36Leu).
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:
-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 a sporadic cancer; somatic mutation.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
36
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:
QETFSDLWKLLPENNVLSPL
P SQAMDDLMLSPDDIEQWFTE
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 QETFSDLWKLLPENNVLSPLP S-QA--MDDLMLSPDDIEQW--FTE
QETFSELWNLLPENNVLSSEL C-PA--VDELLL-PESVVNW
Rhesus macaque QETFSDLWKLLPENNVLSPLP S-QA--VDDLMLSPDDLAQW
Mouse QETFSGLWKLLPPEDILPSPH C-----MDDLLL-PQDVEEF
Rat QETFSCLWKLLPPDDILPTTA TGSPNSMEDLFL-PQDVAEL
Pig QETFSDLWKLLPENNLLSSEL SLAA--VNDLLLSP--VTNW
Bovine QETFSDLWNLLPENNLLSSEL S-AP--VDDLLP-YTDVATW
Rabbit QETFSDLWKLLPENNLLTTSL N-PP--VDDLLS-AEDVANW
Sheep QETFSDLWNLLPENNLLSSEL S-AP--VDDLLPYSEDVVTW
Cat QETFSELWNLLPENNVLSSEL S-SA--MNELPL-SEDVANW
Chicken TEVFMDLWSMLPYS------- ------MQQLPL-PEDHSNW
Xenopus laevis QETFEDLWSLLPDP------- -------------LQTVTCR
Zebrafish ---FAELWE------------ ------KNLIIQPPGGGSCW
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
1 – 320
Interaction with CCAR2
Region
1 – 83
Interaction with HRMT1L2
Region
1 – 44
Transcription activation (acidic)
Modified residue
18 – 18
Phosphothreonine; by CK1, VRK1 and VRK2
Modified residue
20 – 20
Phosphoserine; by CHEK2, CK1 and PLK3
Modified residue
33 – 33
Phosphoserine; by CDK5 and CDK7
Modified residue
37 – 37
Phosphoserine; by MAPKAPK5
Modified residue
46 – 46
Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG
Modified residue
55 – 55
Phosphothreonine; by TAF1 and GRK5
Cross
24 – 24
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence
1 – 132
Missing. In isoform 7, isoform 8 and isoform 9.
Alternative sequence
1 – 39
Missing. In isoform 4, isoform 5 and isoform 6.
Mutagenesis
18 – 18
T -> A. No effect on interaction with MDM2 and increase in protein levels after DNA damage.
Mutagenesis
20 – 20
S -> A. Abolishes phosphorylation site. Abolishes increase in protein levels after DNA damage.
Mutagenesis
20 – 20
S -> D. Constitutively increased TP53 protein levels.
Mutagenesis
24 – 24
K -> R. Abolishes ubiquitination by MUL1.
Mutagenesis
37 – 37
S -> D. Abolishes phosphorylation by MAPKAPK5.
Mutagenesis
46 – 46
S -> A. Abolishes phosphorylation by DYRK2 and HIPK2 and acetylation of K-382 by CREBBP.
Mutagenesis
46 – 46
Missing. Alters interaction with WWOX.
Mutagenesis
55 – 55
T -> A. Blocks phosphorylation by TAF1.
Helix
36 – 38
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.