Sequence information
Variant position: 179 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:
AMAIYKQSQHMTEVVRRCPH
H ERCSDSDGLAPPQHLIRVEG
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 AMAIYKQSQHMTEVVRRCPHH ERCSD-SDGLAPPQHLIRVEG
AMAIYKKSEFVTEVVRRCPHH ERCSDSSDGLAPPQHLIRVE
Rhesus macaque AMAIYKQSQHMTEVVRRCPHH ERCSD-SDGLAPPQHLIRVE
Mouse AMAIYKKSQHMTEVVRRCPHH ERCSD-GDGLAPPQHLIRVE
Rat AMAIYKKSQHMTEVVRRCPHH ERCSD-GDGLAPPQHLIRVE
Pig AMAIYKKSEYMTEVVRRCPHH ERSSDYSDGLAPPQHLIRVE
Bovine AMAIYKKLEHMTEVVRRCPHH ERSSDYSDGLAPPQHLIRVE
Rabbit AMAIYKKSQHMTEVVRRCPHH ERCSD-SDGLAPPQHLIRVE
Sheep AMAIYKKLEHMTEVVRRSPHH ERSSDYSDGLAPPQHLIRVE
Cat AMAIYKKSEFMTEVVRRCPHH ERCPDSSDGLAPPQHLIRVE
Chicken AVAVYKKSEHVAEVVRRCPHH ERCGGGTDGLAPAQHLIRVE
Xenopus laevis ATAVYKKSEHVAEVVKRCPHH ERSVEPGEDAAPPSHLMRVE
Zebrafish ATAIYKKSEHVAEVVRRCPHH ERTPD-GDNLAPAGHLIRVE
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
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
113 – 236
Required for interaction with FBXO42
Region
116 – 292
Interaction with AXIN1
Metal binding
176 – 176
Zinc
Metal binding
179 – 179
Zinc
Modified residue
183 – 183
Phosphoserine; by AURKB
Mutagenesis
183 – 183
S -> A. Abolishes strongly phosphorylation.
Mutagenesis
183 – 183
S -> E. Inhibits slightly its transcriptional activity.
Helix
177 – 180
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.