Sequence information
Variant position: 163 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:
VQLWVDSTPPPGTRVRAMAI
Y KQSQHMTEVVRRCPHHERCS
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 VQLWVDSTPPPGTRVRAMAIY KQSQHMTEVVRRCPHHERCS
VQLWVSSPPPPNTCVRAMAIY KKSEFVTEVVRRCPHHERCS
Rhesus macaque VQLWVDSTPPPGSRVRAMAIY KQSQHMTEVVRRCPHHERCS
Mouse VQLWVSATPPAGSRVRAMAIY KKSQHMTEVVRRCPHHERCS
Rat VQLWVTSTPPPGTRVRAMAIY KKSQHMTEVVRRCPHHERCS
Pig VQLWVSSPPPPGTRVRAMAIY KKSEYMTEVVRRCPHHERSS
Bovine VQLWVDSPPPPGTRVRAMAIY KKLEHMTEVVRRCPHHERSS
Rabbit VQLWVDSTPPPGTRVRAMAIY KKSQHMTEVVRRCPHHERCS
Sheep VQLWVDSPPPPGTRVRAMAIY KKLEHMTEVVRRSPHHERSS
Cat VQLWVRSPPPPGTCVRAMAIY KKSEFMTEVVRRCPHHERCP
Chicken VQVRVGVAPPPGSSLRAVAVY KKSEHVAEVVRRCPHHERCG
Xenopus laevis LLVRVESPPPRGSILRATAVY KKSEHVAEVVKRCPHHERSV
Zebrafish VQMVVDVAPPQGSVVRATAIY KKSEHVAEVVRRCPHHERTP
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.
Beta strand
156 – 165
Literature citations
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;
Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas.
Chanock S.J.; Burdett L.; Yeager M.; Llaca V.; Langeroed A.; Presswalla S.; Kaaresen R.; Strausberg R.L.; Gerhard D.S.; Kristensen V.; Perou C.M.; Boerresen-Dale A.-L.;
Breast Cancer Res. 9:R5-R5(2007)
Cited for: VARIANTS PRO-110; VAL-113; VAL-138; CYS-163; HIS-163; THR-195; MET-216; ALA-241; MET-249; SER-251; TYR-259 AND CYS-273;
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.