Sequence information
Variant position: 175 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:
TRVRAMAIYKQSQHMTEVVR
R CPHHERCSDSDGLAPPQHLI
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 TRVRAMAIYKQSQHMTEVVRR CPHHERCSD-SDGLAPPQHLI
TCVRAMAIYKKSEFVTEVVRR CPHHERCSDSSDGLAPPQHL
Rhesus macaque SRVRAMAIYKQSQHMTEVVRR CPHHERCSD-SDGLAPPQHL
Mouse SRVRAMAIYKKSQHMTEVVRR CPHHERCSD-GDGLAPPQHL
Rat TRVRAMAIYKKSQHMTEVVRR CPHHERCSD-GDGLAPPQHL
Pig TRVRAMAIYKKSEYMTEVVRR CPHHERSSDYSDGLAPPQHL
Bovine TRVRAMAIYKKLEHMTEVVRR CPHHERSSDYSDGLAPPQHL
Rabbit TRVRAMAIYKKSQHMTEVVRR CPHHERCSD-SDGLAPPQHL
Sheep TRVRAMAIYKKLEHMTEVVRR SPHHERSSDYSDGLAPPQHL
Cat TCVRAMAIYKKSEFMTEVVRR CPHHERCPDSSDGLAPPQHL
Chicken SSLRAVAVYKKSEHVAEVVRR CPHHERCGGGTDGLAPAQHL
Xenopus laevis SILRATAVYKKSEHVAEVVKR CPHHERSVEPGEDAAPPSHL
Zebrafish SVVRATAIYKKSEHVAEVVRR CPHHERTPD-GDNLAPAGHL
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.
Literature citations
Hzf Determines cell survival upon genotoxic stress by modulating p53 transactivation.
Das S.; Raj L.; Zhao B.; Kimura Y.; Bernstein A.; Aaronson S.A.; Lee S.W.;
Cell 130:624-637(2007)
Cited for: INTERACTION WITH ZNF385A; CHARACTERIZATION OF VARIANTS ALA-143; HIS-175 AND PRO-175;
p53 inhibits tumor cell invasion via the degradation of snail protein in hepatocellular carcinoma.
Lim S.O.; Kim H.; Jung G.;
FEBS Lett. 584:2231-2236(2010)
Cited for: INTERACTION WITH SNAI1; CHARACTERIZATION OF VARIANTS LEU-110; PRO-155; HIS-175; SER-232; SER-249; HIS-273 AND TRP-282; MUTAGENESIS OF ARG-248;
p53 gene mutations in Barrett's epithelium and esophageal cancer.
Casson A.G.; Mukhopadhyay T.; Cleary K.R.; Ro J.Y.; Levin B.; Roth J.A.;
Cancer Res. 51:4495-4499(1991)
Cited for: VARIANTS SPORADIC CANCERS LEU-152; ALA-155; HIS-175; PHE-176 AND HIS-273;
Germ-line p53 mutations in 15 families with Li-Fraumeni syndrome.
Frebourg T.; Barbier N.; Yan Y.-X.; Garber J.E.; Dreyfus M.; Fraumeni J.F. Jr.; Li F.P.; Friend S.H.;
Am. J. Hum. Genet. 56:608-615(1995)
Cited for: VARIANTS LFS HIS-175; ARG-193; GLN-248; CYS-273 AND TYR-275;
An extended Li-Fraumeni kindred with gastric carcinoma and a codon 175 mutation in TP53.
Varley J.M.; McGrown G.; Thorncroft M.; Tricker K.J.; Teare M.D.; Santibanez-Koref M.F.; Houlston R.S.; Martin J.; Birch J.M.; Evans D.G.R.;
J. Med. Genet. 32:942-945(1995)
Cited for: VARIANT LFS HIS-175;
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;
Phosphorylation of Def Regulates Nucleolar p53 Turnover and Cell Cycle Progression through Def Recruitment of Calpain3.
Guan Y.; Huang D.; Chen F.; Gao C.; Tao T.; Shi H.; Zhao S.; Liao Z.; Lo L.J.; Wang Y.; Chen J.; Peng J.;
PLoS Biol. 14:e1002555-e1002555(2016)
Cited for: CHARACTERIZATION OF VARIANTS VAL-138; HIS-175; ILE-237; TRP-248 AND PRO-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.