ID   Q761V2_HUMAN            Unreviewed;        61 AA.
AC   Q761V2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-OCT-2025, entry version 112.
DE   RecName: Full=Cellular tumor antigen p53 {ECO:0000256|ARBA:ARBA00017135};
DE   AltName: Full=Tumor suppressor p53 {ECO:0000256|ARBA:ARBA00031653};
DE   Flags: Fragment;
GN   Name=p53 {ECO:0000313|EMBL:BAD11806.1};
GN   Synonyms=TP53 {ECO:0000313|EMBL:ABM69023.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD11806.1};
RN   [1] {ECO:0000313|EMBL:BAD11806.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takahashi T., Kawabe T., Okazaki Y., Ito C., Noda K., Tajima M., Satoh M.,
RA   Goto M., Mitsui Y., Tahara H., Ide T., Furuichi Y., Sugimoto M.;
RT   "In vitro establishment of tumorigenic human B-lymphoblastoid cell lines
RT   transformed by Epstein-Barr virus.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABM69023.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung biopsy {ECO:0000313|EMBL:ABM69023.1};
RA   Karami A., Biramijamal F., Arjmand S., Ghanei M., Eshraghi M.;
RT   "Sequence of exon 5 of p53 gene from lung tissue biopsy belongs to 12
RT   patients who were exposed to mustard gas.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ACA63978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Esophageal squamous cell carcinoma
RC   {ECO:0000313|EMBL:ACA63978.1};
RA   Silveira A.P.F., Manoel-Caetano F.S., Aoki S.M., Rahal P., Silva A.E.;
RT   "Detection of p53 mutation in esophageal carcinoma.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AEQ16483.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Singh S., Rajput S.K., Singh M., Singh A.K., Misra P.K., Singh R.K.,
RA   Gambhir I.S.;
RT   "p53 mutation analysis in breast cancer patients of North Eastern Indian
RT   population.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602117-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR602117-1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body
CC       {ECO:0000256|ARBA:ARBA00004322}.
CC   -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167}.
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DR   EMBL; EF178467; ABM69023.1; -; Genomic_DNA.
DR   EMBL; EU523098; ACA63978.1; -; Genomic_DNA.
DR   EMBL; JF923570; AEQ16483.1; -; Genomic_DNA.
DR   EMBL; AB118156; BAD11806.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q761V2; -.
DR   PeptideAtlas; Q761V2; -.
DR   ChiTaRS; TP53; human.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProtKB-ARBA.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.720; -; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR   InterPro; IPR011615; p53_DNA-bd.
DR   InterPro; IPR002117; p53_tumour_suppressor.
DR   PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1.
DR   PANTHER; PTHR11447:SF6; CELLULAR TUMOR ANTIGEN P53; 1.
DR   Pfam; PF00870; P53; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602117-1};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Necrosis {ECO:0000256|ARBA:ARBA00022590};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602117-1}.
FT   DOMAIN          1..60
FT                   /note="p53 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00870"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD11806.1"
FT   NON_TER         61
FT                   /evidence="ECO:0000313|EMBL:BAD11806.1"
SQ   SEQUENCE   61 AA;  7003 MW;  F130CCC26B24312F CRC64;
     YSPALNKMFC QLAKTCPVQL WVDSTPPPGT RVRAMAIYKQ SQHMTEVVRR CPHHERCSDS
     D
//